NCBI: 26-AUG-2013

⊟Summary[edit | edit source]

organism: Staphylococcus aureus N315

locus tag: SA2041 [new locus tag: SA_RS11735 ]

pan locus tag^?: SAUPAN005696000

symbol: rpsC

pan gene symbol^?: rpsC

synonym:
product: 30S ribosomal protein S3

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

type: CDS
locus tag: SA2041 [new locus tag: SA_RS11735 ]
symbol: rpsC
product: 30S ribosomal protein S3
replicon: chromosome
strand: -
coordinates: 2304448..2305101
length: 654
essential: yes ^[1] DEG other strains

⊟Accession numbers[edit | edit source]

Gene ID: 1124962 NCBI
RefSeq: NP_375357 NCBI
BioCyc: see SA_RS11735
MicrobesOnline: 104383 MicrobesOnline

⊟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
601
GTGGGTCAAAAAATTAATCCAATCGGACTTCGTGTTGGTATTATCCGTGATTGGGAAGCT
AAATGGTATGCTGAAAAAGACTTCGCTTCACTTTTACACGAAGATTTAAAAATCCGTAAA
TTTATTGATAATGAATTAAAAGAAGCATCAGTTTCTCACGTAGAGATTGAACGTGCTGCA
AACCGTATCAACATTGCAATTCATACTGGTAAACCTGGTATGGTAATTGGTAAAGGCGGT
TCAGAAATCGAAAAATTACGCAACAAATTAAATGCGTTAACTGATAAAAAAGTACACATC
AACGTAATTGAAATCAAAAAAGTTGATCTTGACGCTCGTTTAGTAGCTGAAAACATCGCA
CGTCAATTAGAAAACCGTGCTTCATTCCGTCGTGTACAAAAACAAGCAATCACTAGAGCT
ATGAAACTTGGTGCTAAAGGTATCAAAACTCAAGTATCTGGTCGTTTAGGCGGAGCTGAC
ATCGCTCGTGCTGAACAATATTCAGAAGGAACTGTTCCACTTCATACGTTACGTGCTGAC
ATCGATTATGCACACGCTGAAGCTGACACTACTTACGGTAAATTAGGCGTTAAAGTATGG
ATCTATCGTGGAGAAGTTCTTCCTACTAAGAACACTAGTGGAGGAGGAAAATAA
60
120
180
240
300
360
420
480
540
600
654

⊟Protein[edit | edit source]

⊟General[edit | edit source]

locus tag: SA2041 [new locus tag: SA_RS11735 ]
symbol: RpsC
description: 30S ribosomal protein S3
length: 217
theoretical pI: 10.4222
theoretical MW: 24099.6
GRAVY: -0.428111

⊟Function[edit | edit source]

⊞⊞TIGRFAM:
Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein uS3 (TIGR01009; HMM-score: 312.7)
and 3 more
Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein uS3 (TIGR01008; HMM-score: 113.8)
NusA family KH domain protein, archaeal (TIGR01952; HMM-score: 20.1)
Genetic information processing Transcription Degradation of RNA polyribonucleotide nucleotidyltransferase (TIGR03591; EC 2.7.7.8; HMM-score: 14.6)
TheSEED :
- SSU ribosomal protein S3p (S3e)
Protein Metabolism Protein biosynthesis Ribosome SSU bacterial SSU ribosomal protein S3p (S3e)
⊞⊞PFAM:
no clan defined Ribosomal_S3_C; Ribosomal protein S3, C-terminal domain (PF00189; HMM-score: 127.6)
and 6 more
KH (CL0007) KH_2; KH domain (PF07650; HMM-score: 76.5)
no clan defined VAR1; Mitochondrial ribosomal protein (VAR1) (PF05316; HMM-score: 34.1)
KH (CL0007) KH_KhpA-B; KhpA/KhpB, KH domain (PF13083; HMM-score: 20.4)
KH_5; NusA-like KH domain (PF13184; HMM-score: 16.1)
KH_1; KH domain (PF00013; HMM-score: 15.8)
MRP-S24; Mitochondrial ribosome subunit S24 (PF14955; HMM-score: 14)

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

domains:
modifications:
cofactors:
effectors:

⊟Localization[edit | edit source]

⊞⊞
PSORTb: Cytoplasmic
- Cytoplasmic Score: 9.97
- Cytoplasmic Membrane Score: 0
- Cellwall Score: 0.01
- Extracellular Score: 0.02
- Internal Helices: 0
⊞⊞
DeepLocPro: Extracellular
- Cytoplasmic Score: 0.3048
- Cytoplasmic Membrane Score: 0.0037
- Cell wall & surface Score: 0.0013
- Extracellular Score: 0.6901
⊞⊞
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): 0.002317
- TAT(Tat/SPI): 0.000116
- LIPO(Sec/SPII): 0.000356
predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

GI: 15927824 NCBI
RefSeq: NP_375357 NCBI
UniProt: P66553 UniProt

⊟Protein sequence[edit | edit source]

MGQKINPIGLRVGIIRDWEAKWYAEKDFASLLHEDLKIRKFIDNELKEASVSHVEIERAANRINIAIHTGKPGMVIGKGGSEIEKLRNKLNALTDKKVHINVIEIKKVDLDARLVAENIARQLENRASFRRVQKQAITRAMKLGAKGIKTQVSGRLGGADIARAEQYSEGTVPLHTLRADIDYAHAEADTTYGKLGVKVWIYRGEVLPTKNTSGGGK

⊟Experimental data[edit | edit source]

experimentally validated: data available for COL, NCTC8325
protein localization: data available for COL
quantitative data / protein copy number per cell: data available for COL

⊟⊟interaction partners:

SA0033	(aadD)	kanamycin nucleotidyltransferase ^[2] (data from MRSA252)
SA0366	(ahpC)	alkyl hydroperoxide reductase ^[2] (data from MRSA252)
SA1409	(dnaK)	molecular chaperone DnaK ^[2] (data from MRSA252)
SA0731	(eno)	phosphopyruvate hydratase ^[2] (data from MRSA252)
SA0843	(fab)	3-oxoacyl-ACP synthase ^[2] (data from MRSA252)
SA0727	(gap)	glyceraldehyde-3-phosphate dehydrogenase ^[2] (data from MRSA252)
SA1305	(hu)	DNA-binding protein II ^[2] (data from MRSA252)
SA1112	(infB)	translation initiation factor IF-2 ^[2] (data from MRSA252)
SA1504	(infC)	translation initiation factor IF-3 ^[2] (data from MRSA252)
SA1244	(odhB)	dihydrolipoamide succinyltransferase ^[2] (data from MRSA252)
SA0943-1	(pdhA)	pyruvate dehydrogenase E1 component subunit alpha ^[2] (data from MRSA252)
SA0944	(pdhB)	pyruvate dehydrogenase E1 component subunit beta ^[2] (data from MRSA252)
SA0945	(pdhC)	branched-chain alpha-keto acid dehydrogenase E2 subunit ^[2] (data from MRSA252)
SA0946	(pdhD)	dihydrolipoamide dehydrogenase ^[2] (data from MRSA252)
SA0496	(rplA)	50S ribosomal protein L1 ^[2] (data from MRSA252)
SA2044	(rplB)	50S ribosomal protein L2 ^[2] (data from MRSA252)
SA2046	(rplD)	50S ribosomal protein L4 ^[2] (data from MRSA252)
SA2035	(rplE)	50S ribosomal protein L5 ^[2] (data from MRSA252)
SA2033	(rplF)	50S ribosomal protein L6 ^[2] (data from MRSA252)
SA0497	(rplJ)	50S ribosomal protein L10 ^[2] (data from MRSA252)
SA0498	(rplL)	50S ribosomal protein L7/L12 ^[2] (data from MRSA252)
SA2017	(rplM)	50S ribosomal protein L13 ^[2] (data from MRSA252)
SA2029	(rplO)	50S ribosomal protein L15 ^[2] (data from MRSA252)
SA1084	(rplS)	50S ribosomal protein L19 ^[2] (data from MRSA252)
SA1502	(rplT)	50S ribosomal protein L20 ^[2] (data from MRSA252)
SA1473	(rplU)	50S ribosomal protein L21 ^[2] (data from MRSA252)
SA2042	(rplV)	50S ribosomal protein L22 ^[2] (data from MRSA252)
SA2045	(rplW)	50S ribosomal protein L23 ^[2] (data from MRSA252)
SA2039	(rpmC)	50S ribosomal protein L29 ^[2] (data from MRSA252)
SA0501	(rpoC)	DNA-directed RNA polymerase subunit beta' ^[2] (data from MRSA252)
SAS052	(rpsD)	30S ribosomal protein S4 ^[2] (data from MRSA252)
SA2031	(rpsE)	30S ribosomal protein S5 ^[2] (data from MRSA252)
SA0352	(rpsF)	30S ribosomal protein S6 ^[2] (data from MRSA252)
SA0504	(rpsG)	30S ribosomal protein S7 ^[2] (data from MRSA252)
SA2016	(rpsI)	30S ribosomal protein S9 ^[2] (data from MRSA252)
SA2024	(rpsK)	30S ribosomal protein S11 ^[2] (data from MRSA252)
SA2025	(rpsM)	30S ribosomal protein S13 ^[2] (data from MRSA252)
SA1116	(rpsO)	30S ribosomal protein S15 ^[2] (data from MRSA252)
SA2038	(rpsQ)	30S ribosomal protein S17 ^[2] (data from MRSA252)
SA2043	(rpsS)	30S ribosomal protein S19 ^[2] (data from MRSA252)
SA0107	(spa)	immunoglobulin G binding protein A ^[2] (data from MRSA252)
SA1245	(sucA)	2-oxoglutarate dehydrogenase E1 ^[2] (data from MRSA252)
SA1089	(sucD)	succinyl-CoA synthetase subunit alpha ^[2] (data from MRSA252)
SA1100	(tsf)	elongation factor Ts ^[2] (data from MRSA252)
SA0506	(tuf)	elongation factor Tu ^[2] (data from MRSA252)
SA0295		hypothetical protein ^[2] (data from MRSA252)
SA0627		hypothetical protein ^[2] (data from MRSA252)
SA0637		hypothetical protein ^[2] (data from MRSA252)
SA0802		hypothetical protein ^[2] (data from MRSA252)
SA1528		hypothetical protein ^[2] (data from MRSA252)
SA1532		hypothetical protein ^[2] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

MicrobesOnline: adk < secY < rplO < rpmD < rpsE < rplR < rplF < rpsH < rpsN < rplE < rplX < rplN < rpsQ < rpmC < rplP < rpsC < rplV < rpsS < rplB < rplW < rplD < rplC < rpsJ

⊟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]

⊞Other Information[edit | edit source]

⊟Literature[edit | edit source]

⊟References[edit | edit source]

↑ R Allyn Forsyth, Robert J Haselbeck, Kari L Ohlsen, Robert T Yamamoto, Howard Xu, John D Trawick, Daniel Wall, Liangsu Wang, Vickie Brown-Driver, Jamie M Froelich, Kedar G C, Paula King, Melissa McCarthy, Cheryl Malone, Brian Misiner, David Robbins, Zehui Tan, Zhan-yang Zhu Zy, Grant Carr, Deborah A Mosca, Carlos Zamudio, J Gordon Foulkes, Judith W Zyskind
A genome-wide strategy for the identification of essential genes in Staphylococcus aureus.
Mol Microbiol: 2002, 43(6);1387-400
[PubMed:11952893] [WorldCat.org] [DOI] (P p)
↑ ^{Jump up to: 2.00} ^2.01 ^2.02 ^2.03 ^2.04 ^2.05 ^2.06 ^2.07 ^2.08 ^2.09 ^2.10 ^2.11 ^2.12 ^2.13 ^2.14 ^2.15 ^2.16 ^2.17 ^2.18 ^2.19 ^2.20 ^2.21 ^2.22 ^2.23 ^2.24 ^2.25 ^2.26 ^2.27 ^2.28 ^2.29 ^2.30 ^2.31 ^2.32 ^2.33 ^2.34 ^2.35 ^2.36 ^2.37 ^2.38 ^2.39 ^2.40 ^2.41 ^2.42 ^2.43 ^2.44 ^2.45 ^2.46 ^2.47 ^2.48 ^2.49 ^2.50 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]

[pubmed11952893-1] R Allyn Forsyth, Robert J Haselbeck, Kari L Ohlsen, Robert T Yamamoto, Howard Xu, John D Trawick, Daniel Wall, Liangsu Wang, Vickie Brown-Driver, Jamie M Froelich, Kedar G C, Paula King, Melissa McCarthy, Cheryl Malone, Brian Misiner, David Robbins, Zehui Tan, Zhan-yang Zhu Zy, Grant Carr, Deborah A Mosca, Carlos Zamudio, J Gordon Foulkes, Judith W Zyskind
A genome-wide strategy for the identification of essential genes in Staphylococcus aureus.
Mol Microbiol: 2002, 43(6);1387-400
[PubMed:11952893] [WorldCat.org] [DOI] (P p)

[pubmed21166474-2] {Jump up to: 2.00} ^2.01 ^2.02 ^2.03 ^2.04 ^2.05 ^2.06 ^2.07 ^2.08 ^2.09 ^2.10 ^2.11 ^2.12 ^2.13 ^2.14 ^2.15 ^2.16 ^2.17 ^2.18 ^2.19 ^2.20 ^2.21 ^2.22 ^2.23 ^2.24 ^2.25 ^2.26 ^2.27 ^2.28 ^2.29 ^2.30 ^2.31 ^2.32 ^2.33 ^2.34 ^2.35 ^2.36 ^2.37 ^2.38 ^2.39 ^2.40 ^2.41 ^2.42 ^2.43 ^2.44 ^2.45 ^2.46 ^2.47 ^2.48 ^2.49 ^2.50 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)

[1]

[2]

SA0033	(aadD)	kanamycin nucleotidyltransferase ^[1] (data from MRSA252)
SA0366	(ahpC)	alkyl hydroperoxide reductase ^[1] (data from MRSA252)
SA1409	(dnaK)	molecular chaperone DnaK ^[1] (data from MRSA252)
SA0731	(eno)	phosphopyruvate hydratase ^[1] (data from MRSA252)
SA0843	(fab)	3-oxoacyl-ACP synthase ^[1] (data from MRSA252)
SA0727	(gap)	glyceraldehyde-3-phosphate dehydrogenase ^[1] (data from MRSA252)
SA1305	(hu)	DNA-binding protein II ^[1] (data from MRSA252)
SA1112	(infB)	translation initiation factor IF-2 ^[1] (data from MRSA252)
SA1504	(infC)	translation initiation factor IF-3 ^[1] (data from MRSA252)
SA1244	(odhB)	dihydrolipoamide succinyltransferase ^[1] (data from MRSA252)
SA0943-1	(pdhA)	pyruvate dehydrogenase E1 component subunit alpha ^[1] (data from MRSA252)
SA0944	(pdhB)	pyruvate dehydrogenase E1 component subunit beta ^[1] (data from MRSA252)
SA0945	(pdhC)	branched-chain alpha-keto acid dehydrogenase E2 subunit ^[1] (data from MRSA252)
SA0946	(pdhD)	dihydrolipoamide dehydrogenase ^[1] (data from MRSA252)
SA0496	(rplA)	50S ribosomal protein L1 ^[1] (data from MRSA252)
SA2044	(rplB)	50S ribosomal protein L2 ^[1] (data from MRSA252)
SA2046	(rplD)	50S ribosomal protein L4 ^[1] (data from MRSA252)
SA2035	(rplE)	50S ribosomal protein L5 ^[1] (data from MRSA252)
SA2033	(rplF)	50S ribosomal protein L6 ^[1] (data from MRSA252)
SA0497	(rplJ)	50S ribosomal protein L10 ^[1] (data from MRSA252)
SA0498	(rplL)	50S ribosomal protein L7/L12 ^[1] (data from MRSA252)
SA2017	(rplM)	50S ribosomal protein L13 ^[1] (data from MRSA252)
SA2029	(rplO)	50S ribosomal protein L15 ^[1] (data from MRSA252)
SA1084	(rplS)	50S ribosomal protein L19 ^[1] (data from MRSA252)
SA1502	(rplT)	50S ribosomal protein L20 ^[1] (data from MRSA252)
SA1473	(rplU)	50S ribosomal protein L21 ^[1] (data from MRSA252)
SA2042	(rplV)	50S ribosomal protein L22 ^[1] (data from MRSA252)
SA2045	(rplW)	50S ribosomal protein L23 ^[1] (data from MRSA252)
SA2039	(rpmC)	50S ribosomal protein L29 ^[1] (data from MRSA252)
SA0501	(rpoC)	DNA-directed RNA polymerase subunit beta' ^[1] (data from MRSA252)
SAS052	(rpsD)	30S ribosomal protein S4 ^[1] (data from MRSA252)
SA2031	(rpsE)	30S ribosomal protein S5 ^[1] (data from MRSA252)
SA0352	(rpsF)	30S ribosomal protein S6 ^[1] (data from MRSA252)
SA0504	(rpsG)	30S ribosomal protein S7 ^[1] (data from MRSA252)
SA2016	(rpsI)	30S ribosomal protein S9 ^[1] (data from MRSA252)
SA2024	(rpsK)	30S ribosomal protein S11 ^[1] (data from MRSA252)
SA2025	(rpsM)	30S ribosomal protein S13 ^[1] (data from MRSA252)
SA1116	(rpsO)	30S ribosomal protein S15 ^[1] (data from MRSA252)
SA2038	(rpsQ)	30S ribosomal protein S17 ^[1] (data from MRSA252)
SA2043	(rpsS)	30S ribosomal protein S19 ^[1] (data from MRSA252)
SA0107	(spa)	immunoglobulin G binding protein A ^[1] (data from MRSA252)
SA1245	(sucA)	2-oxoglutarate dehydrogenase E1 ^[1] (data from MRSA252)
SA1089	(sucD)	succinyl-CoA synthetase subunit alpha ^[1] (data from MRSA252)
SA1100	(tsf)	elongation factor Ts ^[1] (data from MRSA252)
SA0506	(tuf)	elongation factor Tu ^[1] (data from MRSA252)
SA0295		hypothetical protein ^[1] (data from MRSA252)
SA0627		hypothetical protein ^[1] (data from MRSA252)
SA0637		hypothetical protein ^[1] (data from MRSA252)
SA0802		hypothetical protein ^[1] (data from MRSA252)
SA1528		hypothetical protein ^[1] (data from MRSA252)
SA1532		hypothetical protein ^[1] (data from MRSA252)

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⊟Summary[edit | edit source]

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

⊟Accession numbers[edit | edit source]

⊟Phenotype[edit | edit source]

⊟DNA sequence[edit | edit source]

⊟Protein[edit | edit source]

⊟General[edit | edit source]

⊟Function[edit | edit source]

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

⊟Localization[edit | edit source]

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

⊟Experimental data[edit | edit source]

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

⊞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]

⊟Literature[edit | edit source]

⊟References[edit | edit source]

⊟Relevant publications[edit | edit source]

⊟Summary[edit | edit source]

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

⊟Accession numbers[edit | edit source]

⊟Phenotype[edit | edit source]

⊟DNA sequence[edit | edit source]

⊟Protein[edit | edit source]

⊟General[edit | edit source]

⊟Function[edit | edit source]

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

⊟Localization[edit | edit source]

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

⊟Experimental data[edit | edit source]

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

⊞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]

⊟Literature[edit | edit source]

⊟References[edit | edit source]

⊟Relevant publications[edit | edit source]