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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]
- Gene ID: 3237945 NCBI
- RefSeq: YP_185837 NCBI
- BioCyc: see SACOL_RS04960
- MicrobesOnline: 912438 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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481GTGAAAAAAGTTGTAAAATATTTGATTTCATTGATACTTGCTATTATCATTGTACTGTTC
GTACAAACTTTTGTAATAGTTGGTCATGTCATTCCGAATAATGATATGTCACCAACCCTT
AACAAAGGGGATCGTGTTATTGTAAATAAAATTAAAGTTACATTTAATCAATTGAATAAT
GGTGATATCATTACATATAGGCGTGGTAACGAGATATATACTAGTCGAATTATTGCCAAA
CCTGGTCAATCAATGGCGTTTCGTCAGGGACAATTATACCGTGATGACCGACCGGTTGAC
GCATCTTATGCCAAGAACAGAAAAATTAAAGATTTTAGTTTGCGCAATTTTAAAGAATTA
GATGGTGATATTATTCCGCCAAACAATTTTGTTGTGCTAAATGATCAAGATAATAACAAG
CACGATTCAAGACAATTTGGTTTAATCGATAAAAAGGATATTATTGGTAATGTTAGTTTA
CGATACTATCCTTTTTCAAAATGGACTGTTCAGTTCAAATCTTAA60
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⊟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: Protein fate Protein and peptide secretion and trafficking signal peptidase I (TIGR02227; EC 3.4.21.89; HMM-score: 152.6)and 4 moreCellular processes Detoxification nickel-type superoxide dismutase maturation protease (TIGR02754; EC 3.4.21.-; HMM-score: 40.4)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)
- PFAM: Peptidase_SF (CL0299) Peptidase_S24; Peptidase S24-like (PF00717; HMM-score: 38.7)and 4 morePeptidase_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) SACOL0435 GTP-dependent nucleic acid-binding protein EngD [4] (data from MRSA252) SACOL0455 hypothetical protein [4] (data from MRSA252) SACOL0521 hypothetical protein [4] (data from MRSA252) SACOL0944 NADH dehydrogenase [4] (data from MRSA252) SACOL1952 ferritins family protein [4] (data from MRSA252) SACOL2173 alkaline shock protein 23 [4] (data from MRSA252) SACOL2553 pyruvate oxidase [4] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
- MicrobesOnline: SACOL0967 > spsA > spsB
⊟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: 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]
- ↑ 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, 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) - ↑ 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) - ↑ 4.00 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)