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P56981 (UVRB_BACCA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
OrganismBacillus caldotenax
Taxonomic identifier1395 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length658 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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 MF_00204

Cofactor

Binds 1 magnesium ion per subunit.

Subunit structure

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

Subcellular location

Cytoplasm By similarity HAMAP MF_00204.

Domain

The beta-hairpin motif is involved in DNA binding. HAMAP 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 term3D-structure
Gene Ontology (GO)
   Biological processSOS response

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide-excision repair

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from electronic annotation. Source: InterPro

excinuclease ABC activity

Inferred from electronic annotation. Source: InterPro

helicase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed HAMAP MF_00204
Chain2 – 658657UvrABC system protein B HAMAP MF_00204
PRO_0000138379

Regions

Domain27 – 414388Helicase ATP-binding
Domain430 – 596167Helicase C-terminal
Domain622 – 65736UVR
Nucleotide binding40 – 478ATP Potential
Motif93 – 11624Beta-hairpin HAMAP MF_00204

Experimental info

Mutagenesis98 – 11316QPEAY…YIEKD → G: Inactive in incision, unable to form a stable complex with DNA. Ref.2

Secondary structure

1 ................................................................................................. 658
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56981 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: EEFCA1C76F56F826

FASTA65875,455
        10         20         30         40         50         60 
MVEGRFQLVA PYEPQGDQPQ AIAKLVDGLR RGVKHQTLLG ATGTGKTFTI SNVIAQVNKP 

        70         80         90        100        110        120 
TLVIAHNKTL AGQLYSELKE FFPHNAVEYF VSYYDYYQPE AYVPQTDTYI EKDAKINDEI 

       130        140        150        160        170        180 
DKLRHSATSA LFERRDVIIV ASVSCIYGLG SPEEYRELVV SLRVGMEIER NALLRRLVDI 

       190        200        210        220        230        240 
QYDRNDIDFR GTFRVRGDVV EIFPASRDEH CIRVEFFGDE IERIREVDAL TGKVLGEREH 

       250        260        270        280        290        300 
VAIFPASHFV TREEKMRLAI QNIEQELEER LAELRAQGKL LEAQRLEQRT RYDLEMMREM 

       310        320        330        340        350        360 
GFCSGIENYS RHLALRPPGS TPYTLLDYFP DDFLIIVDES HVTLPQLRGM YNGDRARKQV 

       370        380        390        400        410        420 
LVDHGFRLPS ALDNRPLTFE EFEQKINQII YVSATPGPYE LEHSPGVVEQ IIRPTGLLDP 

       430        440        450        460        470        480 
TIDVRPTKGQ IDDLIGEIRE RVERNERTLV TTLTKKMAED LTDYLKEAGI KVAYLHSEIK 

       490        500        510        520        530        540 
TLERIEIIRD LRLGKYDVLV GINLLREGLD IPEVSLVAIL DADKEGFLRS ERSLIQTIGR 

       550        560        570        580        590        600 
AARNANGHVI MYADTITKSM EIAIQETKRR RAIQEEYNRK HGIVPRTVKK EIRDVIRATY 

       610        620        630        640        650 
AAEETEMYEA KPAAAMTKQE REELIRTLEA EMKEAAKALD FERAAQLRDI IFELKAEG

« Hide

References

[1]"Crystal structure of UvrB, a DNA helicase adapted for nucleotide excision repair."
Theis K., Chen P.J., Skorvaga M., Van Houten B., Kisker C.
EMBO J. 18:6899-6907(1999) [PubMed: 10601012] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[2]"The beta-hairpin motif of UvrB is essential for DNA binding, damage processing, and UvrC-mediated incisions."
Skorvaga M., Theis K., Mandavilli B.S., Kisker C., Van Houten B.
J. Biol. Chem. 277:1553-1559(2002) [PubMed: 11687584] [Abstract]
Cited for: IMPORTANCE OF THE BETA-HAIRPIN MOTIF, MUTAGENESIS OF 98-GLN--ASP-113.
+Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D9XX-ray2.60A2-658[»]
1D9ZX-ray3.15A2-658[»]
1T5LX-ray2.60A/B2-657[»]
2FDCX-ray3.30A/B2-657[»]
ProteinModelPortalP56981.
SMRP56981. Positions 2-651.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_00204. UvrB.
[Tree]
InterProIPR014001. DEAD-like_helicase.
IPR006935. Helicase/UvrB_dom.
IPR001650. Helicase_C.
IPR004807. UvrABC_suB.
IPR001943. UvrB/C.
IPR009055. UvrB_UvrC-bd_C.
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. UvrB_C. 1 hit.
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_BACCA
AccessionPrimary (citable) accession number: P56981
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 23, 2007
Last modified: December 14, 2011
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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