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Q5HQX0 (UVRB_STAEQ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UvrABC system protein B

Short name=Protein UvrB
Alternative name(s):
Excinuclease ABC subunit B
Gene names
Name:uvrB
Ordered Locus Names:SERP0426
OrganismStaphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]
Taxonomic identifier176279 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length661 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA2B2 complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage By similarity. HAMAP-Rule MF_00204

Subunit structure

Forms a heterotetramer with UvrA during the search for lesions. Interacts with UvrC in an incision complex By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00204.

Domain

The beta-hairpin motif is involved in DNA binding By similarity. HAMAP-Rule MF_00204

Sequence similarities

Belongs to the UvrB family.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 UVR domain.

Ontologies

Keywords
   Biological processDNA damage
DNA excision
DNA repair
SOS response
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionExcision nuclease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processSOS response

Inferred from electronic annotation. Source: UniProtKB-HAMAP

nucleotide-excision repair

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

DNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

excinuclease ABC activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

helicase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 661661UvrABC system protein B HAMAP-Rule MF_00204
PRO_0000138431

Regions

Domain28 – 414387Helicase ATP-binding
Domain432 – 598167Helicase C-terminal
Domain625 – 66036UVR
Nucleotide binding41 – 488ATP Potential
Motif94 – 11724Beta-hairpin HAMAP-Rule MF_00204

Sequences

Sequence LengthMass (Da)Tools
Q5HQX0 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 342D968A43FA1112

FASTA66176,669
        10         20         30         40         50         60 
MVEHVPFKLK SEFEPQGDQP QAIQKIVDGV NEGKRHQTLL GATGTGKTFT MSNVIKEVGK 

        70         80         90        100        110        120 
PTLIIAHNKT LAGQLYSEFK EFFPENRVEY FVSYYDYYQP EAYVPSTDTF IEKDASINDE 

       130        140        150        160        170        180 
IDQLRHSATS SLFERDDVII IASVSCIYGL GNPEEYKNLV VSVRVGMEME RSELLRKLVD 

       190        200        210        220        230        240 
VQYSRNDIDF QRGTFRVRGD VVEIFPASRE EMCIRVEFFG DEIDRIREVN YLTGEVIRER 

       250        260        270        280        290        300 
EHFTIFPASH FVTREEKMKV AIERIEKELE ERLKELRDEN KLLEAQRLEQ RTNYDLEMMR 

       310        320        330        340        350        360 
EMGFCSGIEN YSVHLTLRPL GSTPYTLLDY FGDDWLVMID ESHVTLPQIR GMYNGDRARK 

       370        380        390        400        410        420 
QVLIDHGFRL PSALDNRPLK FEEFEEKTKQ LVYVSATPGP YELEHTDEMV EQIIRPTGLL 

       430        440        450        460        470        480 
DPKIDVRPTE NQIDDLLSEI QDRVDKDERV LVTTLTKKMS EDLTTYMKEA GIKVNYLHSE 

       490        500        510        520        530        540 
IKTLERIEII RDLRMGTYDA IVGINLLREG IDIPEVSLVV ILDADKEGFL RSDRSLIQTI 

       550        560        570        580        590        600 
GRAARNDKGE VIMYADKITD SMQYAIDETQ RRREIQIAHN KEHGITPKTI NKKIHDVISA 

       610        620        630        640        650        660 
TVESDETNQQ QQTELPKKMT KKERQKTIEN IEKEMKKAAK DLDFEKATEL RDMLFELKAE 


G 

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References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35984 / RP62A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000029 Genomic DNA. Translation: AAW53840.1.
RefSeqYP_188019.1. NC_002976.3.

3D structure databases

ProteinModelPortalQ5HQX0.
SMRQ5HQX0. Positions 7-654.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING176279.SERP0426.

Proteomic databases

PRIDEQ5HQX0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW53840; AAW53840; SERP0426.
GeneID3240773.
KEGGser:SERP0426.
PATRIC19611717. VBIStaEpi130894_0405.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0556.
HOGENOMHOG000073580.
KOK03702.
OMALEKQMHE.
OrthoDBEOG6B360R.

Enzyme and pathway databases

BioCycSEPI176279:GJJB-447-MONOMER.

Family and domain databases

Gene3D3.40.50.300. 4 hits.
4.10.860.10. 1 hit.
HAMAPMF_00204. UvrB.
InterProIPR006935. Helicase/UvrB_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR001943. UVR_dom.
IPR004807. UvrB.
IPR024759. UvrB_YAD/RRR_dom.
[Graphical view]
PANTHERPTHR24029. PTHR24029. 1 hit.
PfamPF00271. Helicase_C. 1 hit.
PF04851. ResIII. 1 hit.
PF02151. UVR. 1 hit.
PF12344. UvrB. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF46600. SSF46600. 1 hit.
SSF52540. SSF52540. 3 hits.
TIGRFAMsTIGR00631. uvrb. 1 hit.
PROSITEPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50151. UVR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameUVRB_STAEQ
AccessionPrimary (citable) accession number: Q5HQX0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: February 15, 2005
Last modified: May 14, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families