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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0969 [new locus tag: SACOL_RS04965 ]
  • pan locus tag?: SAUPAN003074000
  • symbol: spsB
  • pan gene symbol?: spsB
  • synonym:
  • product: signal peptidase IB

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL0969 [new locus tag: SACOL_RS04965 ]
  • symbol: spsB
  • product: signal peptidase IB
  • replicon: chromosome
  • strand: +
  • coordinates: 971238..971822
  • length: 585
  • essential: unknown other strains

⊟Accession numbers[edit | edit source]

⊟Phenotype[edit | edit source]

Share your knowledge and add information here. [edit]

⊟DNA sequence[edit | edit source]

  • 1
    61
    121
    181
    241
    301
    361
    421
    481
    541
    GTGTCAAAATTGAAAAAAGAAATATTGGAATGGATTATTTCAATTGCAGTCGCTTTTGTC
    ATTTTATTTATAGTAGGTAAATTTATTGTTACGCCATATACAATTAAAGGTGAATCAATG
    GATCCAACTTTGAAAGATGGCGAGCGAGTAGCTGTAAACATTGTTGGATATAAAACAGGT
    GGTTTGGAAAAAGGTAATGTAGTTGTCTTCCATGCAAACAAAAATGATGACTATGTTAAA
    CGTGTCATCGGTGTTCCTGGTGATAAAGTAGAATACAAAAATGATACATTATATGTCAAT
    GGTAAAAAACAAGATGAACCATATTTAAACTACAATTTAAAACATAAACAAGGTGATTAC
    ATTACTGGGACTTTCCAAGTTAAAGATTTACCGAATGCGAATCCTAAATCAAATGTCATT
    CCAAAAGGTAAATATTTAGTGCTTGGAGATAATCGTGAAGTAAGTAAAGATAGCCGTGCG
    TTTGGCCTCATTGATGAAGACCAAATTGTTGGTAAAGTTTCATTTAGGTTCTGGCCATTT
    AGTGAATTTAAACATAATTTCAATCCTGAAAATACTAAAAATTAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    585

⊟Protein[edit | edit source]

Protein Data Bank: 4WVG
Protein Data Bank: 4WVH
Protein Data Bank: 4WVI
Protein Data Bank: 4WVJ

⊟General[edit | edit source]

  • locus tag: SACOL0969 [new locus tag: SACOL_RS04965 ]
  • symbol: SpsB
  • description: signal peptidase IB
  • length: 194
  • theoretical pI: 9.66728
  • theoretical MW: 22006.1
  • GRAVY: -0.431959

⊟Function[edit | edit source]

  • reaction:
    EC 3.4.21.89?  ExPASy
    Signal peptidase I Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins
  • TIGRFAM:
    Genetic information processing Protein fate Protein and peptide secretion and trafficking signal peptidase I (TIGR02227; EC 3.4.21.89; HMM-score: 177.4)
    and 4 more
    Cellular processes Cellular processes Detoxification nickel-type superoxide dismutase maturation protease (TIGR02754; EC 3.4.21.-; HMM-score: 49)
    Genetic information processing Protein fate Protein modification and repair nickel-type superoxide dismutase maturation protease (TIGR02754; EC 3.4.21.-; HMM-score: 49)
    conjugative transfer signal peptidase TraF (TIGR02771; HMM-score: 36.4)
    signal peptidase I (TIGR02228; EC 3.4.21.89; HMM-score: 30.2)
  • TheSEED  :
    • Signal peptidase I (EC 3.4.21.89)
    Protein Metabolism Protein processing and modification Signal peptidase  Signal peptidase I (EC 3.4.21.89)
  • PFAM:
    Peptidase_SF (CL0299) Peptidase_S24; Peptidase S24-like (PF00717; HMM-score: 72.7)
    and 1 more
    Peptidase_S26; Signal peptidase, peptidase S26 (PF10502; HMM-score: 36.1)

⊟Structure, modifications & cofactors[edit | edit source]

  • domains:
  • modifications:
  • cofactors:
  • effectors:

⊟Localization[edit | edit source]

  • PSORTb: Cellwall
    • Cytoplasmic Score: 0
    • Cytoplasmic Membrane Score: 0.53
    • Cellwall Score: 8.76
    • Extracellular Score: 0.7
    • Internal Helix: 1
  • LocateP: N-terminally anchored (No CS)
    • Prediction by SwissProt Classification: Membrane
    • Pathway Prediction: Sec-(SPI)
    • Intracellular possibility: 0.17
    • Signal peptide possibility: -1
    • N-terminally Anchored Score: 4
    • Predicted Cleavage Site: No CleavageSite
  • SignalP: no predicted signal peptide
    • SP(Sec/SPI): 0.188318
    • TAT(Tat/SPI): 0.000849
    • LIPO(Sec/SPII): 0.023068
  • predicted transmembrane helices (TMHMM): 1

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MSKLKKEILEWIISIAVAFVILFIVGKFIVTPYTIKGESMDPTLKDGERVAVNIVGYKTGGLEKGNVVVFHANKNDDYVKRVIGVPGDKVEYKNDTLYVNGKKQDEPYLNYNLKHKQGDYITGTFQVKDLPNANPKSNVIPKGKYLVLGDNREVSKDSRAFGLIDEDQIVGKVSFRFWPFSEFKHNFNPENTKN

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Integral membrane [1] [2] [3] [4]
  • quantitative data / protein copy number per cell:
  • interaction partners:
    SACOL1760(ackA)acetate kinase  [5] (data from MRSA252)
    SACOL0452(ahpC)alkyl hydroperoxide reductase subunit C  [5] (data from MRSA252)
    SACOL1478(ald1)alanine dehydrogenase  [5] (data from MRSA252)
    SACOL2657(arcA)arginine deiminase  [5] (data from MRSA252)
    SACOL2656(arcB2)ornithine carbamoyltransferase  [5] (data from MRSA252)
    SACOL0570(clpC)  [5] (data from MRSA252)
    SACOL0557(cysK)cysteine synthase  [5] (data from MRSA252)
    SACOL1800(dat)D-alanine aminotransferase  [5] (data from MRSA252)
    SACOL0123(deoC1)deoxyribose-phosphate aldolase  [5] (data from MRSA252)
    SACOL2130(deoD)purine nucleoside phosphorylase  [5] (data from MRSA252)
    SACOL1637(dnaK)molecular chaperone DnaK  [5] (data from MRSA252)
    SACOL0002(dnaN)DNA polymerase III subunit beta  [5] (data from MRSA252)
    SACOL1587(efp)elongation factor P  [5] (data from MRSA252)
    SACOL0842(eno)phosphopyruvate hydratase  [5] (data from MRSA252)
    SACOL0988(fabF)3-oxoacyl-ACP synthase  [5] (data from MRSA252)
    SACOL1245(fabG1)3-oxoacyl-ACP reductase  [5] (data from MRSA252)
    SACOL2117(fbaA)fructose-bisphosphate aldolase  [5] (data from MRSA252)
    SACOL2622(fdaB)fructose-1,6-bisphosphate aldolase  [5] (data from MRSA252)
    SACOL1782(fhs)formate--tetrahydrofolate ligase  [5] (data from MRSA252)
    SACOL1199(ftsZ)cell division protein FtsZ  [5] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [5] (data from MRSA252)
    SACOL0838(gapA1)glyceraldehyde 3-phosphate dehydrogenase  [5] (data from MRSA252)
    SACOL1734(gapA2)glyceraldehyde 3-phosphate dehydrogenase 2  [5] (data from MRSA252)
    SACOL1961(gatA)aspartyl/glutamyl-tRNA amidotransferase subunit A  [5] (data from MRSA252)
    SACOL2145(glmS)glucosamine--fructose-6-phosphate aminotransferase  [5] (data from MRSA252)
    SACOL1622(glyS)glycyl-tRNA synthetase  [5] (data from MRSA252)
    SACOL1554(gnd)6-phosphogluconate dehydrogenase  [5] (data from MRSA252)
    SACOL0461(guaA)GMP synthase  [5] (data from MRSA252)
    SACOL0460(guaB)inosine-5'-monophosphate dehydrogenase  [5] (data from MRSA252)
    SACOL0006(gyrA)DNA gyrase, A subunit  [5] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [5] (data from MRSA252)
    SACOL1288(infB)translation initiation factor IF-2  [5] (data from MRSA252)
    SACOL1727(infC)translation initiation factor IF-3  [5] (data from MRSA252)
    SACOL0222(ldh1)L-lactate dehydrogenase  [5] (data from MRSA252)
    SACOL2618(ldh2)L-lactate dehydrogenase  [5] (data from MRSA252)
    SACOL2623(mqo2)malate:quinone oxidoreductase  [5] (data from MRSA252)
    SACOL2116(murAB)UDP-N-acetylglucosamine 1-carboxyvinyltransferase  [5] (data from MRSA252)
    SACOL0792(nrdE)ribonucleotide-diphosphate reductase subunit alpha  [5] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [5] (data from MRSA252)
    SACOL1103(pdhB)pyruvate dehydrogenase complex E1 component subunit beta  [5] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [5] (data from MRSA252)
    SACOL2128(pdp)pyrimidine-nucleoside phosphorylase  [5] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [5] (data from MRSA252)
    SACOL0966(pgi)glucose-6-phosphate isomerase  [5] (data from MRSA252)
    SACOL0839(pgk)phosphoglycerate kinase  [5] (data from MRSA252)
    SACOL0841(pgm)phosphoglyceromutase  [5] (data from MRSA252)
    SACOL1293(pnp)polynucleotide phosphorylase/polyadenylase  [5] (data from MRSA252)
    SACOL1982(ppaC)manganese-dependent inorganic pyrophosphatase  [5] (data from MRSA252)
    SACOL1091(ptsH)phosphocarrier protein HPr  [5] (data from MRSA252)
    SACOL1092(ptsI)phosphoenolpyruvate-protein phosphotransferase  [5] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [5] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [5] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [5] (data from MRSA252)
    SACOL2238(rplD)50S ribosomal protein L4  [5] (data from MRSA252)
    SACOL2227(rplE)50S ribosomal protein L5  [5] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [5] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [5] (data from MRSA252)
    SACOL0583(rplK)50S ribosomal protein L11  [5] (data from MRSA252)
    SACOL0586(rplL)50S ribosomal protein L7/L12  [5] (data from MRSA252)
    SACOL2207(rplM)50S ribosomal protein L13  [5] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [5] (data from MRSA252)
    SACOL2232(rplP)50S ribosomal protein L16  [5] (data from MRSA252)
    SACOL2212(rplQ)50S ribosomal protein L17  [5] (data from MRSA252)
    SACOL2223(rplR)50S ribosomal protein L18  [5] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [5] (data from MRSA252)
    SACOL1725(rplT)50S ribosomal protein L20  [5] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [5] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [5] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [5] (data from MRSA252)
    SACOL0545(rplY)50S ribosomal protein L25/general stress protein Ctc  [5] (data from MRSA252)
    SACOL2231(rpmC)50S ribosomal protein L29  [5] (data from MRSA252)
    SACOL2221(rpmD)50S ribosomal protein L30  [5] (data from MRSA252)
    SACOL2112(rpmE2)50S ribosomal protein L31  [5] (data from MRSA252)
    SACOL2213(rpoA)DNA-directed RNA polymerase subunit alpha  [5] (data from MRSA252)
    SACOL0588(rpoB)DNA-directed RNA polymerase subunit beta  [5] (data from MRSA252)
    SACOL0589(rpoC)DNA-directed RNA polymerase subunit beta'  [5] (data from MRSA252)
    SACOL1516(rpsA)30S ribosomal protein S1  [5] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [5] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [5] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [5] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [5] (data from MRSA252)
    SACOL0437(rpsF)30S ribosomal protein S6  [5] (data from MRSA252)
    SACOL0592(rpsG)30S ribosomal protein S7  [5] (data from MRSA252)
    SACOL2225(rpsH)30S ribosomal protein S8  [5] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [5] (data from MRSA252)
    SACOL2240(rpsJ)30S ribosomal protein S10  [5] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [5] (data from MRSA252)
    SACOL2215(rpsM)30S ribosomal protein S13  [5] (data from MRSA252)
    SACOL1254(rpsP)30S ribosomal protein S16  [5] (data from MRSA252)
    SACOL0439(rpsR)30S ribosomal protein S18  [5] (data from MRSA252)
    SACOL2235(rpsS)30S ribosomal protein S19  [5] (data from MRSA252)
    SACOL0095(spa)immunoglobulin G binding protein A precursor  [5] (data from MRSA252)
    SACOL1449(sucA)2-oxoglutarate dehydrogenase E1 component  [5] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [5] (data from MRSA252)
    SACOL1262(sucC)succinyl-CoA synthetase subunit beta  [5] (data from MRSA252)
    SACOL1831(tal)translaldolase  [5] (data from MRSA252)
    SACOL0626(thiD1)phosphomethylpyrimidine kinase  [5] (data from MRSA252)
    SACOL1729(thrS)threonyl-tRNA synthetase  [5] (data from MRSA252)
    SACOL1722(tig)trigger factor  [5] (data from MRSA252)
    SACOL1762(tpx)thiol peroxidase  [5] (data from MRSA252)
    SACOL1001(trpS)tryptophanyl-tRNA synthetase  [5] (data from MRSA252)
    SACOL1276(tsf)elongation factor Ts  [5] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [5] (data from MRSA252)
    SACOL2104(upp)uracil phosphoribosyltransferase  [5] (data from MRSA252)
    SACOL0506ABC transporter substrate-binding protein  [5] (data from MRSA252)
    SACOL0552hypothetical protein  [5] (data from MRSA252)
    SACOL0564pyridoxal biosynthesis lyase PdxS  [5] (data from MRSA252)
    SACOL0688ABC transporter substrate-binding protein  [5] (data from MRSA252)
    SACOL0815ribosomal subunit interface protein  [5] (data from MRSA252)
    SACOL0914FeS assembly ATPase SufC  [5] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [5] (data from MRSA252)
    SACOL0973fumarylacetoacetate hydrolase  [5] (data from MRSA252)
    SACOL1020hypothetical protein  [5] (data from MRSA252)
    SACOL1240DAK2 domain-containing protein  [5] (data from MRSA252)
    SACOL1427ABC transporter ATP-binding protein  [5] (data from MRSA252)
    SACOL1437CSD family cold shock protein  [5] (data from MRSA252)
    SACOL1593glycine dehydrogenase subunit 2  [5] (data from MRSA252)
    SACOL1759universal stress protein  [5] (data from MRSA252)
    SACOL1801dipeptidase PepV  [5] (data from MRSA252)
    SACOL1933ThiJ/PfpI family protein  [5] (data from MRSA252)
    SACOL1952ferritins family protein  [5] (data from MRSA252)
    SACOL1992hypothetical protein  [5] (data from MRSA252)
    SACOL2114aldehyde dehydrogenase  [5] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [5] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator:

⊟Transcription pattern[edit | edit source]

⊟Protein synthesis (provided by Aureolib)[edit | edit source]

⊟Protein stability[edit | edit source]

  • half-life: 2.22 h [6]

⊟Biological Material[edit | edit source]

⊟Mutants[edit | edit source]

⊟Expression vector[edit | edit source]

⊟lacZ fusion[edit | edit source]

⊟GFP fusion[edit | edit source]

⊟two-hybrid system[edit | edit source]

⊟FLAG-tag construct[edit | edit source]

⊟Antibody[edit | edit source]

⊟Other Information[edit | edit source]

You are kindly invited to share additional interesting facts.

⊟Literature[edit | edit source]

⊟References[edit | edit source]

  1. ↑ Dörte Becher, Kristina Hempel, Susanne Sievers, Daniela Zühlke, Jan Pané-Farré, Andreas Otto, Stephan Fuchs, Dirk Albrecht, Jörg Bernhardt, Susanne Engelmann, Uwe Völker, Jan Maarten van Dijl, Michael Hecker
    A proteomic view of an important human pathogen--towards the quantification of the entire Staphylococcus aureus proteome.
    PLoS One: 2009, 4(12);e8176
    [PubMed:19997597] [WorldCat.org] [DOI] (I e)
  2. ↑ Kristina Hempel, Jan Pané-Farré, Andreas Otto, Susanne Sievers, Michael Hecker, Dörte Becher
    Quantitative cell surface proteome profiling for SigB-dependent protein expression in the human pathogen Staphylococcus aureus via biotinylation approach.
    J Proteome Res: 2010, 9(3);1579-90
    [PubMed:20108986] [WorldCat.org] [DOI] (I p)
  3. ↑ Kristina Hempel, Florian-Alexander Herbst, Martin Moche, Michael Hecker, Dörte Becher
    Quantitative proteomic view on secreted, cell surface-associated, and cytoplasmic proteins of the methicillin-resistant human pathogen Staphylococcus aureus under iron-limited conditions.
    J Proteome Res: 2011, 10(4);1657-66
    [PubMed:21323324] [WorldCat.org] [DOI] (I p)
  4. ↑ Andreas Otto, Jan Maarten van Dijl, Michael Hecker, Dörte Becher
    The Staphylococcus aureus proteome.
    Int J Med Microbiol: 2014, 304(2);110-20
    [PubMed:24439828] [WorldCat.org] [DOI] (I p)
  5. ↑ 5.000 5.001 5.002 5.003 5.004 5.005 5.006 5.007 5.008 5.009 5.010 5.011 5.012 5.013 5.014 5.015 5.016 5.017 5.018 5.019 5.020 5.021 5.022 5.023 5.024 5.025 5.026 5.027 5.028 5.029 5.030 5.031 5.032 5.033 5.034 5.035 5.036 5.037 5.038 5.039 5.040 5.041 5.042 5.043 5.044 5.045 5.046 5.047 5.048 5.049 5.050 5.051 5.052 5.053 5.054 5.055 5.056 5.057 5.058 5.059 5.060 5.061 5.062 5.063 5.064 5.065 5.066 5.067 5.068 5.069 5.070 5.071 5.072 5.073 5.074 5.075 5.076 5.077 5.078 5.079 5.080 5.081 5.082 5.083 5.084 5.085 5.086 5.087 5.088 5.089 5.090 5.091 5.092 5.093 5.094 5.095 5.096 5.097 5.098 5.099 5.100 5.101 5.102 5.103 5.104 5.105 5.106 5.107 5.108 5.109 5.110 5.111 5.112 5.113 5.114 5.115 5.116 5.117 5.118 5.119 5.120 5.121 5.122 5.123 Artem Cherkasov, Michael Hsing, Roya Zoraghi, Leonard J Foster, Raymond H See, Nikolay Stoynov, Jihong Jiang, Sukhbir Kaur, Tian Lian, Linda Jackson, Huansheng Gong, Rick Swayze, Emily Amandoron, Farhad Hormozdiari, Phuong Dao, Cenk Sahinalp, Osvaldo Santos-Filho, Peter Axerio-Cilies, Kendall Byler, William R McMaster, Robert C Brunham, B Brett Finlay, Neil E Reiner
    Mapping the protein interaction network in methicillin-resistant Staphylococcus aureus.
    J Proteome Res: 2011, 10(3);1139-50
    [PubMed:21166474] [WorldCat.org] [DOI] (I p)
  6. ↑ Stephan Michalik, Jörg Bernhardt, Andreas Otto, Martin Moche, Dörte Becher, Hanna Meyer, Michael Lalk, Claudia Schurmann, Rabea Schlüter, Holger Kock, Ulf Gerth, Michael Hecker
    Life and death of proteins: a case study of glucose-starved Staphylococcus aureus.
    Mol Cell Proteomics: 2012, 11(9);558-70
    [PubMed:22556279] [WorldCat.org] [DOI] (I p)

⊟Relevant publications[edit | edit source]

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