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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL1098 [new locus tag: SACOL_RS05605 ]
- pan locus tag?: SAUPAN003312000
- symbol: SACOL1098
- pan gene symbol?: rnjA
- synonym:
- product: hypothetical protein
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL1098 [new locus tag: SACOL_RS05605 ]
- symbol: SACOL1098
- product: hypothetical protein
- replicon: chromosome
- strand: -
- coordinates: 1107961..1109658
- length: 1698
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3237632 NCBI
- RefSeq: YP_185962 NCBI
- BioCyc: see SACOL_RS05605
- MicrobesOnline: 912566 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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1681ATGAAACAATTACATCCAAATGAAGTAGGTGTATATGCACTTGGAGGTCTAGGTGAAATC
GGTAAAAATACTTATGCAGTTGAGTATAAAGACGAAATTGTCATTATCGATGCAGGTATC
AAATTCCCTGATGATAACTTATTAGGGATTGATTATGTTATACCTGACTACACATATCTA
GTTCAAAACCAAGATAAAATTGTTGGCCTATTTATAACACATGGTCACGAAGACCATATA
GGCGGTGTGCCCTTCCTATTAAAACAACTTAATATACCTATTTATGGTGGTCCTTTAGCA
TTAGGTTTAATCCGTAATAAACTTGAAGAACATCATTTATTACGTACTGCTAAACTAAAT
GAAATCAATGAGGACAGTGTGATTAAATCTAAGCACTTTACGATTTCTTTCTACTTAACT
ACACATAGTATTCCTGAAACTTATGGCGTCATCGTAGATACACCTGAAGGAAAAGTAGTT
CATACCGGTGACTTTAAATTTGATTTTACACCTGTAGGCAAACCAGCAAACATTGCTAAA
ATGGCTCAATTAGGCGAAGAAGGCGTTCTATGTTTACTTTCAGACTCAACAAATTCACTT
GTGCCTGATTTTACTTTAAGCGAACGTGAAGTTGGTCAAAACGTAGATAAGATCTTCCGT
AATTGTAAAGGTCGTATTATATTTGCTACCTTCGCTTCTAATATTTACCGAGTTCAACAA
GCAGTTGAAGCTGCTATCAAAAATAACCGTAAAATTGTTACGTTCGGTCGTTCGATGGAA
AACAATATTAAAATAGGTATGGAACTTGGTTATATTAAAGCACCACCTGAAACATTTATT
GAACCTAATAAAATTAATACCGTACCGAAGCATGAGTTATTGATACTATGTACTGGTTCA
CAAGGTGAACCAATGGCAGCATTATCTAGAATTGCTAATGGTACTCATAAGCAAATTAAA
ATTATACCTGAAGATACCGTTGTATTTAGTTCATCACCTATCCCAGGTAATACAAAAAGT
ATTAACAGAACTATTAATTCCTTGTATAAAGCTGGTGCAGATGTTATCCATAGCAAGATT
TCTAACATCCATACTTCAGGGCATGGTTCTCAAGGTGATCAACAATTAATGCTTCGATTA
ATCAAGCCGAAATATTTCTTACCTATTCATGGTGAATACCGTATGTTAAAAGCACATGGT
GAGACTGGTGTTGAATGCGGCGTTGAAGAAGATAATGTCTTCATCTTTGATATTGGAGAT
GTCTTAGCTTTAACACACGATTCAGCACGTAAAGCTGGTCGCATTCCATCTGGTAATGTA
CTTGTTGATGGTAGTGGTATCGGTGATATCGGTAATGTTGTAATAAGAGACCGTAAGCTA
TTATCTGAAGAAGGTTTAGTTATCGTTGTTGTTAGTATTGATTTTAATACAAATAAATTA
CTTTCTGGTCCAGACATTATTTCTCGAGGATTTGTATATATGAGGGAATCAGGTCAATTA
ATTTATGATGCACAACGCAAAATCAAAACTGATGTTATTAGTAAGTTAAATCAAAATAAA
GATATTCAATGGCATCAGATTAAATCTTCTATCATTGAAACATTACAACCTTATTTATTT
GAAAAAACAGCTAGAAAACCAATGATTTTACCAGTCATTATGAAGGTAAACGAACAAAAA
GAATCAAACAATAAATAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL1098 [new locus tag: SACOL_RS05605 ]
- symbol: SACOL1098
- description: hypothetical protein
- length: 565
- theoretical pI: 7.3306
- theoretical MW: 62668.7
- GRAVY: -0.169735
⊟Function[edit | edit source]
- reaction: EC 3.1.-.-? ExPASy
- TIGRFAM: Transcription Degradation of RNA beta-CASP ribonuclease, RNase J family (TIGR00649; EC 3.1.-.-; HMM-score: 688.9)and 4 morearCOG00543 universal archaeal KH-domain/beta-lactamase-domain protein (TIGR03675; HMM-score: 33.3)Transcription RNA processing ribonuclease Z (TIGR02651; EC 3.1.26.11; HMM-score: 25.1)Cellular processes Detoxification hydroxyacylglutathione hydrolase (TIGR03413; EC 3.1.2.6; HMM-score: 24)Cellular processes DNA transformation DNA internalization-related competence protein ComEC/Rec2 (TIGR00361; HMM-score: 12.4)
- TheSEED :
- Ribonuclease J2 (endoribonuclease in RNA processing)
- PFAM: Metallo-HOrase (CL0381) Lactamase_B; Metallo-beta-lactamase superfamily (PF00753; HMM-score: 62.8)and 2 moreRMMBL_DRMBL (CL0398) RMMBL; Zn-dependent metallo-hydrolase RNA specificity domain (PF07521; HMM-score: 40.6)Metallo-HOrase (CL0381) Lactamase_B_2; Beta-lactamase superfamily domain (PF12706; HMM-score: 37.3)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors: Zn2+
- effectors:
⊟Localization[edit | edit source]
- PSORTb: Cytoplasmic
- Cytoplasmic Score: 7.5
- Cytoplasmic Membrane Score: 1.15
- Cellwall Score: 0.62
- Extracellular Score: 0.73
- Internal Helices: 0
- LocateP: Intracellular
- Prediction by SwissProt Classification: Cytoplasmic
- Pathway Prediction: No pathway
- Intracellular possibility: 1
- Signal peptide possibility: -1
- N-terminally Anchored Score: 1
- Predicted Cleavage Site: No CleavageSite
- SignalP: no predicted signal peptide
- SP(Sec/SPI): 0.017007
- TAT(Tat/SPI): 0.000282
- LIPO(Sec/SPII): 0.002342
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MKQLHPNEVGVYALGGLGEIGKNTYAVEYKDEIVIIDAGIKFPDDNLLGIDYVIPDYTYLVQNQDKIVGLFITHGHEDHIGGVPFLLKQLNIPIYGGPLALGLIRNKLEEHHLLRTAKLNEINEDSVIKSKHFTISFYLTTHSIPETYGVIVDTPEGKVVHTGDFKFDFTPVGKPANIAKMAQLGEEGVLCLLSDSTNSLVPDFTLSEREVGQNVDKIFRNCKGRIIFATFASNIYRVQQAVEAAIKNNRKIVTFGRSMENNIKIGMELGYIKAPPETFIEPNKINTVPKHELLILCTGSQGEPMAALSRIANGTHKQIKIIPEDTVVFSSSPIPGNTKSINRTINSLYKAGADVIHSKISNIHTSGHGSQGDQQLMLRLIKPKYFLPIHGEYRMLKAHGETGVECGVEEDNVFIFDIGDVLALTHDSARKAGRIPSGNVLVDGSGIGDIGNVVIRDRKLLSEEGLVIVVVSIDFNTNKLLSGPDIISRGFVYMRESGQLIYDAQRKIKTDVISKLNQNKDIQWHQIKSSIIETLQPYLFEKTARKPMILPVIMKVNEQKESNNK
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas
- protein localization: Cytoplasmic [1] [2] [3]
- quantitative data / protein copy number per cell: 1039 [4]
- interaction partners:
SACOL2657 (arcA) arginine deiminase [5] (data from MRSA252) SACOL0593 (fusA) elongation factor G [5] (data from MRSA252) SACOL1513 (hup) DNA-binding protein HU [5] (data from MRSA252) SACOL1727 (infC) translation initiation factor IF-3 [5] (data from MRSA252) SACOL1105 (pdhD) dihydrolipoamide dehydrogenase [5] (data from MRSA252) SACOL0204 (pflB) formate acetyltransferase [5] (data from MRSA252) SACOL0584 (rplA) 50S ribosomal protein L1 [5] (data from MRSA252) SACOL2236 (rplB) 50S ribosomal protein L2 [5] (data from MRSA252) SACOL2239 (rplC) 50S ribosomal protein L3 [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) SACOL0586 (rplL) 50S ribosomal protein L7/L12 [5] (data from MRSA252) SACOL2220 (rplO) 50S ribosomal protein L15 [5] (data from MRSA252) SACOL2232 (rplP) 50S ribosomal protein L16 [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) 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) SACOL0592 (rpsG) 30S ribosomal protein S7 [5] (data from MRSA252) SACOL2206 (rpsI) 30S ribosomal protein S9 [5] (data from MRSA252) SACOL2214 (rpsK) 30S ribosomal protein S11 [5] (data from MRSA252) SACOL1292 (rpsO) 30S ribosomal protein S15 [5] (data from MRSA252) SACOL2230 (rpsQ) 30S ribosomal protein S17 [5] (data from MRSA252) SACOL2235 (rpsS) 30S ribosomal protein S19 [5] (data from MRSA252) SACOL1448 (sucB) dihydrolipoamide succinyltransferase [5] (data from MRSA252) SACOL0594 (tuf) elongation factor Tu [5] (data from MRSA252) SACOL0303 5'-nucleotidase [5] (data from MRSA252) SACOL0731 LysR family transcriptional regulator [5] (data from MRSA252) SACOL0914 FeS assembly ATPase SufC [5] (data from MRSA252) SACOL0944 NADH dehydrogenase [5] (data from MRSA252) SACOL1753 universal stress protein [5] (data from MRSA252) SACOL1759 universal stress protein [5] (data from MRSA252) SACOL2072 DEAD/DEAH box helicase [5] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟Regulation[edit | edit source]
- regulator:
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: data available for NCTC8325
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
- Aureolib: no data available
⊟Protein stability[edit | edit source]
- half-life: 33.57 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]
- ↑ 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) - ↑ 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) - ↑ 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) - ↑ Daniela Zühlke, Kirsten Dörries, Jörg Bernhardt, Sandra Maaß, Jan Muntel, Volkmar Liebscher, Jan Pané-Farré, Katharina Riedel, Michael Lalk, Uwe Völker, Susanne Engelmann, Dörte Becher, Stephan Fuchs, Michael Hecker
Costs of life - Dynamics of the protein inventory of Staphylococcus aureus during anaerobiosis.
Sci Rep: 2016, 6;28172
[PubMed:27344979] [WorldCat.org] [DOI] (I e) - ↑ 5.00 5.01 5.02 5.03 5.04 5.05 5.06 5.07 5.08 5.09 5.10 5.11 5.12 5.13 5.14 5.15 5.16 5.17 5.18 5.19 5.20 5.21 5.22 5.23 5.24 5.25 5.26 5.27 5.28 5.29 5.30 5.31 5.32 5.33 5.34 5.35 5.36 5.37 5.38 5.39 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) - ↑ 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)