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NCBI: 10-JUN-2013

Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0968 [new locus tag: SACOL_RS04960 ]
  • pan locus tag?: SAUPAN003073000
  • symbol: spsA
  • pan gene symbol?: spsA
  • synonym:
  • product: signal peptidase IA, inactive

Genome View[edit | edit source]

Gene[edit | edit source]

General[edit | edit source]

  • type: CDS
  • locus tag: SACOL0968 [new locus tag: SACOL_RS04960 ]
  • symbol: spsA
  • product: signal peptidase IA, inactive
  • replicon: chromosome
  • strand: +
  • coordinates: 970707..971231
  • length: 525
  • 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
    GTGAAAAAAGTTGTAAAATATTTGATTTCATTGATACTTGCTATTATCATTGTACTGTTC
    GTACAAACTTTTGTAATAGTTGGTCATGTCATTCCGAATAATGATATGTCACCAACCCTT
    AACAAAGGGGATCGTGTTATTGTAAATAAAATTAAAGTTACATTTAATCAATTGAATAAT
    GGTGATATCATTACATATAGGCGTGGTAACGAGATATATACTAGTCGAATTATTGCCAAA
    CCTGGTCAATCAATGGCGTTTCGTCAGGGACAATTATACCGTGATGACCGACCGGTTGAC
    GCATCTTATGCCAAGAACAGAAAAATTAAAGATTTTAGTTTGCGCAATTTTAAAGAATTA
    GATGGTGATATTATTCCGCCAAACAATTTTGTTGTGCTAAATGATCAAGATAATAACAAG
    CACGATTCAAGACAATTTGGTTTAATCGATAAAAAGGATATTATTGGTAATGTTAGTTTA
    CGATACTATCCTTTTTCAAAATGGACTGTTCAGTTCAAATCTTAA
    60
    120
    180
    240
    300
    360
    420
    480
    525

Protein[edit | edit source]

General[edit | edit source]

  • locus tag: SACOL0968 [new locus tag: SACOL_RS04960 ]
  • symbol: SpsA
  • description: signal peptidase IA, inactive
  • length: 174
  • theoretical pI: 10.4619
  • theoretical MW: 20109.1
  • GRAVY: -0.310345

Function[edit | edit source]

  • TIGRFAM:
    Genetic information processing Protein fate Protein and peptide secretion and trafficking signal peptidase I (TIGR02227; EC 3.4.21.89; HMM-score: 152.6)
    and 4 more
    Cellular processes Cellular processes Detoxification nickel-type superoxide dismutase maturation protease (TIGR02754; EC 3.4.21.-; HMM-score: 40.4)
    Genetic information processing Protein fate Protein modification and repair nickel-type superoxide dismutase maturation protease (TIGR02754; EC 3.4.21.-; HMM-score: 40.4)
    conjugative transfer signal peptidase TraF (TIGR02771; HMM-score: 32)
    signal peptidase I (TIGR02228; EC 3.4.21.89; HMM-score: 28.7)
  • 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: 38.7)
    and 4 more
    Peptidase_S26; Signal peptidase, peptidase S26 (PF10502; HMM-score: 27.6)
    no clan defined DUF2534; Protein of unknown function (DUF2534) (PF10749; HMM-score: 13.6)
    AsmA-like (CL0401) AsmA; AsmA family (PF05170; HMM-score: 13.2)
    no clan defined E1-E2_ATPase; E1-E2 ATPase (PF00122; HMM-score: 9.1)

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: 0
    • N-terminally Anchored Score: 7
    • Predicted Cleavage Site: No CleavageSite
  • SignalP: no predicted signal peptide
    • SP(Sec/SPI): 0.473598
    • TAT(Tat/SPI): 0.000476
    • LIPO(Sec/SPII): 0.051893
  • predicted transmembrane helices (TMHMM): 1

Accession numbers[edit | edit source]

Protein sequence[edit | edit source]

  • MKKVVKYLISLILAIIIVLFVQTFVIVGHVIPNNDMSPTLNKGDRVIVNKIKVTFNQLNNGDIITYRRGNEIYTSRIIAKPGQSMAFRQGQLYRDDRPVDASYAKNRKIKDFSLRNFKELDGDIIPPNNFVVLNDQDNNKHDSRQFGLIDKKDIIGNVSLRYYPFSKWTVQFKS

Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Signal peptide containing [1] [2] [3]
  • quantitative data / protein copy number per cell:
  • interaction partners:
    SACOL0842(eno)phosphopyruvate hydratase  [4] (data from MRSA252)
    SACOL1329(femC)glutamine synthetase  [4] (data from MRSA252)
    SACOL1072(folD)bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase  [4] (data from MRSA252)
    SACOL1199(ftsZ)cell division protein FtsZ  [4] (data from MRSA252)
    SACOL0460(guaB)inosine-5'-monophosphate dehydrogenase  [4] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [4] (data from MRSA252)
    SACOL0222(ldh1)L-lactate dehydrogenase  [4] (data from MRSA252)
    SACOL2116(murAB)UDP-N-acetylglucosamine 1-carboxyvinyltransferase  [4] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [4] (data from MRSA252)
    SACOL1103(pdhB)pyruvate dehydrogenase complex E1 component subunit beta  [4] (data from MRSA252)
    SACOL1104(pdhC)branched-chain alpha-keto acid dehydrogenase E2  [4] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [4] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [4] (data from MRSA252)
    SACOL0841(pgm)phosphoglyceromutase  [4] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [4] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [4] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [4] (data from MRSA252)
    SACOL2238(rplD)50S ribosomal protein L4  [4] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [4] (data from MRSA252)
    SACOL0586(rplL)50S ribosomal protein L7/L12  [4] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [4] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [4] (data from MRSA252)
    SACOL1725(rplT)50S ribosomal protein L20  [4] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [4] (data from MRSA252)
    SACOL2228(rplX)50S ribosomal protein L24  [4] (data from MRSA252)
    SACOL2213(rpoA)DNA-directed RNA polymerase subunit alpha  [4] (data from MRSA252)
    SACOL0588(rpoB)DNA-directed RNA polymerase subunit beta  [4] (data from MRSA252)
    SACOL0589(rpoC)DNA-directed RNA polymerase subunit beta'  [4] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [4] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [4] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [4] (data from MRSA252)
    SACOL0437(rpsF)30S ribosomal protein S6  [4] (data from MRSA252)
    SACOL0592(rpsG)30S ribosomal protein S7  [4] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [4] (data from MRSA252)
    SACOL0095(spa)immunoglobulin G binding protein A precursor  [4] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [4] (data from MRSA252)
    SACOL1722(tig)trigger factor  [4] (data from MRSA252)
    SACOL1276(tsf)elongation factor Ts  [4] (data from MRSA252)
    SACOL0435GTP-dependent nucleic acid-binding protein EngD  [4] (data from MRSA252)
    SACOL0455hypothetical protein  [4] (data from MRSA252)
    SACOL0521hypothetical protein  [4] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [4] (data from MRSA252)
    SACOL1952ferritins family protein  [4] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [4] (data from MRSA252)
    SACOL2553pyruvate oxidase  [4] (data from MRSA252)

Expression & Regulation[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: no data available

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. 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)
  4. 4.00 4.01 4.02 4.03 4.04 4.05 4.06 4.07 4.08 4.09 4.10 4.11 4.12 4.13 4.14 4.15 4.16 4.17 4.18 4.19 4.20 4.21 4.22 4.23 4.24 4.25 4.26 4.27 4.28 4.29 4.30 4.31 4.32 4.33 4.34 4.35 4.36 4.37 4.38 4.39 4.40 4.41 4.42 4.43 4.44 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)

Relevant publications[edit | edit source]