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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_00902
- pan locus tag?: SAUPAN003073000
- symbol: SAOUHSC_00902
- pan gene symbol?: spsA
- synonym:
- product: signal peptidase IA
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SAOUHSC_00902
- symbol: SAOUHSC_00902
- product: signal peptidase IA
- replicon: chromosome
- strand: +
- coordinates: 867096..867620
- length: 525
- essential: no DEG other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3921748 NCBI
- RefSeq: YP_499455 NCBI
- BioCyc: G1I0R-845 BioCyc
- MicrobesOnline: 1289366 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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525
⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_00902
- symbol: SAOUHSC_00902
- description: signal peptidase IA
- length: 174
- theoretical pI: 10.4619
- theoretical MW: 20109.1
- GRAVY: -0.310345
⊟Function[edit | edit source]
- reaction: EC 3.4.21.89? ExPASySignal peptidase I Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins
- 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 [1] [2]
- protein localization: data available for COL
- quantitative data / protein copy number per cell:
- interaction partners:
SAOUHSC_00799 (eno) phosphopyruvate hydratase [3] (data from MRSA252) SAOUHSC_00519 (rplA) 50S ribosomal protein L1 [3] (data from MRSA252) SAOUHSC_02509 (rplB) 50S ribosomal protein L2 [3] (data from MRSA252) SAOUHSC_02511 (rplD) 50S ribosomal protein L4 [3] (data from MRSA252) SAOUHSC_00520 (rplJ) 50S ribosomal protein L10 [3] (data from MRSA252) SAOUHSC_00521 (rplL) 50S ribosomal protein L7/L12 [3] (data from MRSA252) SAOUHSC_02492 (rplO) 50S ribosomal protein L15 [3] (data from MRSA252) SAOUHSC_01211 (rplS) 50S ribosomal protein L19 [3] (data from MRSA252) SAOUHSC_01784 (rplT) 50S ribosomal protein L20 [3] (data from MRSA252) SAOUHSC_01757 (rplU) 50S ribosomal protein L21 [3] (data from MRSA252) SAOUHSC_02501 (rplX) 50S ribosomal protein L24 [3] (data from MRSA252) SAOUHSC_00524 (rpoB) DNA-directed RNA polymerase subunit beta [3] (data from MRSA252) SAOUHSC_01232 (rpsB) 30S ribosomal protein S2 [3] (data from MRSA252) SAOUHSC_02506 (rpsC) 30S ribosomal protein S3 [3] (data from MRSA252) SAOUHSC_01829 (rpsD) 30S ribosomal protein S4 [3] (data from MRSA252) SAOUHSC_00348 (rpsF) 30S ribosomal protein S6 [3] (data from MRSA252) SAOUHSC_01779 (tig) trigger factor [3] (data from MRSA252) SAOUHSC_01234 (tsf) elongation factor Ts [3] (data from MRSA252) SAOUHSC_00069 protein A [3] (data from MRSA252) SAOUHSC_00187 formate acetyltransferase [3] (data from MRSA252) SAOUHSC_00206 L-lactate dehydrogenase [3] (data from MRSA252) SAOUHSC_00346 GTP-dependent nucleic acid-binding protein EngD [3] (data from MRSA252) SAOUHSC_00369 hypothetical protein [3] (data from MRSA252) SAOUHSC_00374 inosine-5'-monophosphate dehydrogenase [3] (data from MRSA252) SAOUHSC_00444 hypothetical protein [3] (data from MRSA252) SAOUHSC_00525 DNA-directed RNA polymerase subunit beta' [3] (data from MRSA252) SAOUHSC_00528 30S ribosomal protein S7 [3] (data from MRSA252) SAOUHSC_00798 2,3-bisphosphoglycerate-independent phosphoglycerate mutase [3] (data from MRSA252) SAOUHSC_00878 hypothetical protein [3] (data from MRSA252) SAOUHSC_01007 bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase [3] (data from MRSA252) SAOUHSC_01040 pyruvate dehydrogenase complex, E1 component subunit alpha [3] (data from MRSA252) SAOUHSC_01041 pyruvate dehydrogenase complex, E1 component subunit beta [3] (data from MRSA252) SAOUHSC_01042 branched-chain alpha-keto acid dehydrogenase subunit E2 [3] (data from MRSA252) SAOUHSC_01043 dihydrolipoamide dehydrogenase [3] (data from MRSA252) SAOUHSC_01150 cell division protein FtsZ [3] (data from MRSA252) SAOUHSC_01287 glutamine synthetase [3] (data from MRSA252) SAOUHSC_01416 dihydrolipoamide succinyltransferase [3] (data from MRSA252) SAOUHSC_01801 isocitrate dehydrogenase [3] (data from MRSA252) SAOUHSC_01806 pyruvate kinase [3] (data from MRSA252) SAOUHSC_02108 ferritin [3] (data from MRSA252) SAOUHSC_02365 UDP-N-acetylglucosamine 1-carboxyvinyltransferase [3] (data from MRSA252) SAOUHSC_02441 alkaline shock protein 23 [3] (data from MRSA252) SAOUHSC_02485 DNA-directed RNA polymerase subunit alpha [3] (data from MRSA252) SAOUHSC_02486 30S ribosomal protein S11 [3] (data from MRSA252) SAOUHSC_02849 pyruvate oxidase [3] (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: [4] Multi-gene expression profiles
⊟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]
- ↑ Maren Depke, Stephan Michalik, Alexander Rabe, Kristin Surmann, Lars Brinkmann, Nico Jehmlich, Jörg Bernhardt, Michael Hecker, Bernd Wollscheid, Zhi Sun, Robert L Moritz, Uwe Völker, Frank Schmidt
A peptide resource for the analysis of Staphylococcus aureus in host-pathogen interaction studies.
Proteomics: 2015, 15(21);3648-61
[PubMed:26224020] [WorldCat.org] [DOI] (I p) - ↑ Stephan Michalik, Maren Depke, Annette Murr, Manuela Gesell Salazar, Ulrike Kusebauch, Zhi Sun, Tanja C Meyer, Kristin Surmann, Henrike Pförtner, Petra Hildebrandt, Stefan Weiss, Laura Marcela Palma Medina, Melanie Gutjahr, Elke Hammer, Dörte Becher, Thomas Pribyl, Sven Hammerschmidt, Eric W Deutsch, Samuel L Bader, Michael Hecker, Robert L Moritz, Ulrike Mäder, Uwe Völker, Frank Schmidt
A global Staphylococcus aureus proteome resource applied to the in vivo characterization of host-pathogen interactions.
Sci Rep: 2017, 7(1);9718
[PubMed:28887440] [WorldCat.org] [DOI] (I e) - ↑ 3.00 3.01 3.02 3.03 3.04 3.05 3.06 3.07 3.08 3.09 3.10 3.11 3.12 3.13 3.14 3.15 3.16 3.17 3.18 3.19 3.20 3.21 3.22 3.23 3.24 3.25 3.26 3.27 3.28 3.29 3.30 3.31 3.32 3.33 3.34 3.35 3.36 3.37 3.38 3.39 3.40 3.41 3.42 3.43 3.44 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) - ↑ 4.0 4.1 Ulrike Mäder, Pierre Nicolas, Maren Depke, Jan Pané-Farré, Michel Debarbouille, Magdalena M van der Kooi-Pol, Cyprien Guérin, Sandra Dérozier, Aurelia Hiron, Hanne Jarmer, Aurélie Leduc, Stephan Michalik, Ewoud Reilman, Marc Schaffer, Frank Schmidt, Philippe Bessières, Philippe Noirot, Michael Hecker, Tarek Msadek, Uwe Völker, Jan Maarten van Dijl
Staphylococcus aureus Transcriptome Architecture: From Laboratory to Infection-Mimicking Conditions.
PLoS Genet: 2016, 12(4);e1005962
[PubMed:27035918] [WorldCat.org] [DOI] (I e)