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NCBI: 10-JUN-2013
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus COL
- locus tag: SACOL0823 [new locus tag: SACOL_RS04230 ]
- pan locus tag?: SAUPAN002672000
- symbol: uvrB
- pan gene symbol?: uvrB
- synonym:
- product: excinuclease ABC subunit B
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SACOL0823 [new locus tag: SACOL_RS04230 ]
- symbol: uvrB
- product: excinuclease ABC subunit B
- replicon: chromosome
- strand: +
- coordinates: 845540..847531
- length: 1992
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3237964 NCBI
- RefSeq: YP_185697 NCBI
- BioCyc: see SACOL_RS04230
- MicrobesOnline: 912295 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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1981GTGACAATGGTTGAACATTATCCTTTTAAAATACATTCTGATTTTGAGCCTCAAGGTGAC
CAACCGCAAGCAATTAAAGAAATCGTGGAAGGTATTAAAGCGGGGAAAAGACATCAAACT
TTATTAGGTGCTACTGGCACAGGGAAAACATTTACGATGAGTAATGTTATTAAAGAAGTT
GGGAAACCAACGTTAATTATCGCGCATAACAAAACATTAGCAGGACAATTATATAGTGAG
TTTAAAGAATTTTTTCCTGAAAACAGGGTGGAATACTTTGTAAGTTACTATGATTATTAT
CAACCAGAGGCATACGTACCGTCTACTGACACTTTTATTGAAAAAGATGCCTCAATCAAT
GATGAAATTGATCAACTACGACATTCTGCTACAAGTGCATTATTTGAACGCGATGATGTA
ATTATTATTGCTAGTGTAAGTTGTATATATGGTTTAGGTAATCCTGAAGAATATAAAGAT
TTAGTAGTAAGTGTTCGAGTTGGTATGGAAATGGATAGAAGTGAATTACTTAGAAAACTT
GTAGATGTGCAATATACACGAAATGACATCGATTTCCAACGAGGAACGTTTCGAGTGCGT
GGTGATGTAGTGGAAATATTCCCAGCCTCTAAAGAAGAACTTTGTATAAGGGTTGAGTTT
TTCGGCGATGAGATTGACCGTATCCGAGAAGTTAACTACCTAACAGGTGAAGTGTTGAAA
GAAAGAGAACATTTTGCGATATTCCCAGCTTCTCACTTCGTAACACGTGAAGAAAAGTTG
AAAGTTGCGATTGAACGTATTGAAAAAGAATTGGAAGAACGATTGAAAGAATTACGAGAT
GAGAATAAATTACTAGAAGCGCAAAGGTTAGAACAGCGTACCAACTATGATTTAGAAATG
ATGCGAGAGATGGGATTCTGTTCAGGAATTGAAAACTATTCCGTACATTTAACTTTGCGA
CCACTGGGTTCGACACCATATACTTTATTGGATTACTTTGGCGATGATTGGTTAGTAATG
ATTGATGAATCACATGTGACATTACCGCAAGTTCGAGGCATGTATAACGGAGACAGAGCG
CGTAAACAAGTTTTGGTGGATCATGGGTTTAGATTACCGAGTGCATTAGATAACCGTCCA
CTTAAATTTGAAGAATTTGAAGAAAAGACAAAACAACTTGTGTATGTATCTGCAACGCCT
GGACCATACGAAATTGAACATACGGATAAGATGGTTGAACAAATTATTCGTCCTACTGGT
TTACTGGATCCTAAGATTGAGGTTAGACCTACTGAAAATCAAATTGACGATTTATTAAGT
GAAATTCAAACAAGAGTTGAGCGTAATGAACGCGTACTTGTTACAACGCTCACTAAAAAG
ATGAGTGAAGATTTAACCACATACATGAAAGAAGCGGGTATTAAAGTTAATTATCTGCAT
TCAGAAATCAAGACATTAGAACGAATTGAAATAATTAGAGACTTACGAATGGGTACATAT
GATGTTATCGTAGGTATTAATTTATTAAGAGAGGGTATTGATATACCAGAAGTTTCTCTA
GTTGTCATATTAGATGCAGATAAAGAAGGGTTTTTACGTTCTAACCGCTCATTAATTCAA
ACAATAGGTAGAGCTGCGCGTAACGATAAAGGTGAAGTCATTATGTATGCCGATAAAATG
ACTGATTCGATGAAGTATGCAATTGATGAGACACAACGTCGTCGAGAAATACAGATGAAA
CATAATGAAAAACATGGTATTACACCTAAAACAATTAATAAAAAAATACATGATTTAATT
AGTGCTACTGTTGAAAATGACGAAAATAATGACAAAGCACAAACTGTGATACCTAAGAAG
ATGACGAAAAAAGAACGTCAAAAGACAATCGACAATATAGAAAAAGAAATGAAACAAGCA
GCGAAAGATTTAGATTTCGAGAAAGCTACAGAATTAAGAGATATGTTATTTGAATTAAAA
GCAGAAGGGTGA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SACOL0823 [new locus tag: SACOL_RS04230 ]
- symbol: UvrB
- description: excinuclease ABC subunit B
- length: 663
- theoretical pI: 5.05392
- theoretical MW: 76880.1
- GRAVY: -0.551131
⊟Function[edit | edit source]
- TIGRFAM: DNA metabolism DNA replication, recombination, and repair excinuclease ABC subunit B (TIGR00631; EC 3.1.25.-; HMM-score: 1110)and 8 moreDNA metabolism DNA replication, recombination, and repair transcription-repair coupling factor (TIGR00580; EC 3.6.1.-; HMM-score: 65.4)DNA metabolism DNA replication, recombination, and repair ATP-dependent DNA helicase RecG (TIGR00643; EC 3.6.4.12; HMM-score: 47.9)DNA phosphorothioation system restriction enzyme (TIGR04095; HMM-score: 40)DNA metabolism DNA replication, recombination, and repair primosomal protein N' (TIGR00595; EC 3.6.1.-; HMM-score: 32.1)DNA metabolism DNA replication, recombination, and repair ATP-dependent DNA helicase, RecQ family (TIGR00614; EC 3.6.4.12; HMM-score: 27.9)DNA metabolism DNA replication, recombination, and repair ATP-dependent DNA helicase RecQ (TIGR01389; EC 3.6.4.12; HMM-score: 27.6)DEXH box helicase, DNA ligase-associated (TIGR04121; EC 3.6.4.-; HMM-score: 18.1)helicase/secretion neighborhood putative DEAH-box helicase (TIGR03817; HMM-score: 13.6)
- TheSEED :
- Excinuclease ABC subunit B
- PFAM: P-loop_NTPase (CL0023) UvrB; Ultra-violet resistance protein B (PF12344; HMM-score: 84.2)Helicase_C; Helicase conserved C-terminal domain (PF00271; HMM-score: 73.4)and 13 moreResIII; Type III restriction enzyme, res subunit (PF04851; HMM-score: 47.1)no clan defined UVR; UvrB/uvrC motif (PF02151; HMM-score: 35.4)P-loop_NTPase (CL0023) DEAD; DEAD/DEAH box helicase (PF00270; HMM-score: 23.8)AAA_30; AAA domain (PF13604; HMM-score: 21.5)AAA; ATPase family associated with various cellular activities (AAA) (PF00004; HMM-score: 16)Kinesin; Kinesin motor domain (PF00225; HMM-score: 13.6)MEDS; MEDS: MEthanogen/methylotroph, DcmR Sensory domain (PF14417; HMM-score: 12.8)AAA_19; AAA domain (PF13245; HMM-score: 12.7)DUF853; Bacterial protein of unknown function (DUF853) (PF05872; HMM-score: 12.4)TrwB_AAD_bind; Type IV secretion-system coupling protein DNA-binding domain (PF10412; HMM-score: 12.4)AAA_25; AAA domain (PF13481; HMM-score: 11.2)PDDEXK (CL0236) Sen15; Sen15 protein (PF09631; HMM-score: 10.7)Oxa1 (CL0376) DUF106; Integral membrane protein DUF106 (PF01956; HMM-score: 9.9)
⊟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
- 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): 0.016715
- TAT(Tat/SPI): 0.021434
- LIPO(Sec/SPII): 0.000511
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MTMVEHYPFKIHSDFEPQGDQPQAIKEIVEGIKAGKRHQTLLGATGTGKTFTMSNVIKEVGKPTLIIAHNKTLAGQLYSEFKEFFPENRVEYFVSYYDYYQPEAYVPSTDTFIEKDASINDEIDQLRHSATSALFERDDVIIIASVSCIYGLGNPEEYKDLVVSVRVGMEMDRSELLRKLVDVQYTRNDIDFQRGTFRVRGDVVEIFPASKEELCIRVEFFGDEIDRIREVNYLTGEVLKEREHFAIFPASHFVTREEKLKVAIERIEKELEERLKELRDENKLLEAQRLEQRTNYDLEMMREMGFCSGIENYSVHLTLRPLGSTPYTLLDYFGDDWLVMIDESHVTLPQVRGMYNGDRARKQVLVDHGFRLPSALDNRPLKFEEFEEKTKQLVYVSATPGPYEIEHTDKMVEQIIRPTGLLDPKIEVRPTENQIDDLLSEIQTRVERNERVLVTTLTKKMSEDLTTYMKEAGIKVNYLHSEIKTLERIEIIRDLRMGTYDVIVGINLLREGIDIPEVSLVVILDADKEGFLRSNRSLIQTIGRAARNDKGEVIMYADKMTDSMKYAIDETQRRREIQMKHNEKHGITPKTINKKIHDLISATVENDENNDKAQTVIPKKMTKKERQKTIDNIEKEMKQAAKDLDFEKATELRDMLFELKAEG
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas
- protein localization: Cytoplasmic [1] [2] [3]
- quantitative data / protein copy number per cell: 28 [4]
- interaction partners:
SACOL1760 (ackA) acetate kinase [5] (data from MRSA252) SACOL0452 (ahpC) alkyl hydroperoxide reductase subunit C [5] (data from MRSA252) SACOL2657 (arcA) arginine deiminase [5] (data from MRSA252) SACOL0557 (cysK) cysteine synthase [5] (data from MRSA252) SACOL1800 (dat) D-alanine aminotransferase [5] (data from MRSA252) SACOL1637 (dnaK) molecular chaperone DnaK [5] (data from MRSA252) SACOL0842 (eno) phosphopyruvate hydratase [5] (data from MRSA252) SACOL0634 (eutD) phosphotransacetylase [5] (data from MRSA252) SACOL1329 (femC) glutamine synthetase [5] (data from MRSA252) SACOL0593 (fusA) elongation factor G [5] (data from MRSA252) SACOL0838 (gapA1) glyceraldehyde 3-phosphate dehydrogenase [5] (data from MRSA252) SACOL1734 (gapA2) glyceraldehyde 3-phosphate dehydrogenase 2 [5] (data from MRSA252) SACOL2145 (glmS) glucosamine--fructose-6-phosphate aminotransferase [5] (data from MRSA252) SACOL0460 (guaB) inosine-5'-monophosphate dehydrogenase [5] (data from MRSA252) SACOL1513 (hup) DNA-binding protein HU [5] (data from MRSA252) SACOL1741 (icd) isocitrate dehydrogenase [5] (data from MRSA252) SACOL1288 (infB) translation initiation factor IF-2 [5] (data from MRSA252) SACOL0222 (ldh1) L-lactate dehydrogenase [5] (data from MRSA252) SACOL2116 (murAB) UDP-N-acetylglucosamine 1-carboxyvinyltransferase [5] (data from MRSA252) SACOL1102 (pdhA) pyruvate dehydrogenase complex E1 component subunit alpha [5] (data from MRSA252) SACOL1103 (pdhB) pyruvate dehydrogenase complex E1 component subunit beta [5] (data from MRSA252) SACOL1104 (pdhC) branched-chain alpha-keto acid dehydrogenase E2 [5] (data from MRSA252) SACOL1105 (pdhD) dihydrolipoamide dehydrogenase [5] (data from MRSA252) SACOL0204 (pflB) formate acetyltransferase [5] (data from MRSA252) SACOL0841 (pgm) phosphoglyceromutase [5] (data from MRSA252) SACOL1091 (ptsH) phosphocarrier protein HPr [5] (data from MRSA252) SACOL1745 (pyk) pyruvate kinase [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) SACOL2207 (rplM) 50S ribosomal protein L13 [5] (data from MRSA252) SACOL1257 (rplS) 50S ribosomal protein L19 [5] (data from MRSA252) SACOL2234 (rplV) 50S ribosomal protein L22 [5] (data from MRSA252) SACOL2213 (rpoA) DNA-directed RNA polymerase subunit alpha [5] (data from MRSA252) SACOL0589 (rpoC) DNA-directed RNA polymerase subunit beta' [5] (data from MRSA252) SACOL2120 (rpoE) DNA-directed RNA polymerase subunit delta [5] (data from MRSA252) SACOL1274 (rpsB) 30S ribosomal protein S2 [5] (data from MRSA252) SACOL2222 (rpsE) 30S ribosomal protein S5 [5] (data from MRSA252) SACOL0592 (rpsG) 30S ribosomal protein S7 [5] (data from MRSA252) SACOL2215 (rpsM) 30S ribosomal protein S13 [5] (data from MRSA252) SACOL2230 (rpsQ) 30S ribosomal protein S17 [5] (data from MRSA252) SACOL0439 (rpsR) 30S ribosomal protein S18 [5] (data from MRSA252) SACOL2235 (rpsS) 30S ribosomal protein S19 [5] (data from MRSA252) SACOL1610 (sodA2) superoxide dismutase [5] (data from MRSA252) SACOL0095 (spa) immunoglobulin G binding protein A precursor [5] (data from MRSA252) SACOL1449 (sucA) 2-oxoglutarate dehydrogenase E1 component [5] (data from MRSA252) SACOL1448 (sucB) dihydrolipoamide succinyltransferase [5] (data from MRSA252) SACOL1722 (tig) trigger factor [5] (data from MRSA252) SACOL0840 (tpiA) triosephosphate isomerase [5] (data from MRSA252) SACOL0594 (tuf) elongation factor Tu [5] (data from MRSA252) SACOL0824 (uvrA) excinuclease ABC subunit A [5] (data from MRSA252) SACOL1157 (uvrC) excinuclease ABC subunit C [5] (data from MRSA252) SACOL0521 hypothetical protein [5] (data from MRSA252) SACOL0731 LysR family transcriptional regulator [5] (data from MRSA252) SACOL0944 NADH dehydrogenase [5] (data from MRSA252) SACOL0973 fumarylacetoacetate hydrolase [5] (data from MRSA252) SACOL2173 alkaline shock protein 23 [5] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟Regulation[edit | edit source]
- regulator: LexA (repression) regulon
LexA (TF) important in SOS response; RegPrecise
⊟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, 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 5.40 5.41 5.42 5.43 5.44 5.45 5.46 5.47 5.48 5.49 5.50 5.51 5.52 5.53 5.54 5.55 5.56 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)