ID UVRB_SYNJA Reviewed; 695 AA.
AC Q2JRR3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 01-MAY-2013, entry version 54.
DE RecName: Full=UvrABC system protein B;
DE Short=Protein UvrB;
DE AltName: Full=Excinuclease ABC subunit B;
GN Name=uvrB; OrderedLocusNames=CYA_2564;
OS Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium
OS Yellowstone A-Prime).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Synechococcus.
OX NCBI_TaxID=321327;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-3-3Ab;
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M.,
RA Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community
RT revealed by comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(2007).
CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and
CC processing of DNA lesions. A damage recognition complex composed
CC of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon
CC binding of the UvrA(2)B(2) complex to a putative damaged site, the
CC DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP
CC binding by UvrB and probably causes local melting of the DNA
CC helix, facilitating insertion of UvrB beta-hairpin between the DNA
CC strands. Then UvrB probes one DNA strand for the presence of a
CC lesion. If a lesion is found the UvrA subunits dissociate and the
CC UvrB-DNA preincision complex is formed. This complex is
CC subsequently bound by UvrC and the second UvrB is released. If no
CC lesion is found, the DNA wraps around the other UvrB subunit that
CC will check the other stand for damage (By similarity).
CC -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for
CC lesions. Interacts with UvrC in an incision complex (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- DOMAIN: The beta-hairpin motif is involved in DNA binding (By
CC similarity).
CC -!- SIMILARITY: Belongs to the UvrB family.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC -!- SIMILARITY: Contains 1 UVR domain.
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DR EMBL; CP000239; ABD00683.1; -; Genomic_DNA.
DR RefSeq; YP_475946.1; NC_007775.1.
DR HSSP; P56981; 2FDC.
DR ProteinModelPortal; Q2JRR3; -.
DR SMR; Q2JRR3; 4-616.
DR STRING; 321327.CYA_2564; -.
DR EnsemblBacteria; ABD00683; ABD00683; CYA_2564.
DR GeneID; 3899899; -.
DR KEGG; cya:CYA_2564; -.
DR PATRIC; 23813386; VBISynSp90045_2518.
DR eggNOG; COG0556; -.
DR HOGENOM; HOG000073580; -.
DR KO; K03702; -.
DR OMA; CIYGLGI; -.
DR ProtClustDB; PRK05298; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0003677; F:DNA binding; IEA:HAMAP.
DR GO; GO:0009381; F:excinuclease ABC activity; IEA:HAMAP.
DR GO; GO:0004386; F:helicase activity; IEA:HAMAP.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:HAMAP.
DR GO; GO:0009432; P:SOS response; IEA:HAMAP.
DR Gene3D; 4.10.860.10; -; 1.
DR HAMAP; MF_00204; UvrB; 1; -.
DR InterPro; IPR006935; Helicase/UvrB_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR001943; UVR_dom.
DR InterPro; IPR004807; UvrB.
DR InterPro; IPR024759; UvrB_YAD/RRR_dom.
DR PANTHER; PTHR24029; PTHR24029; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04851; ResIII; 1.
DR Pfam; PF02151; UVR; 1.
DR Pfam; PF12344; UvrB; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF46600; UvrB_C; 1.
DR TIGRFAMs; TIGR00631; uvrb; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50151; UVR; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Cytoplasm; DNA damage; DNA excision;
KW DNA repair; Excision nuclease; Helicase; Hydrolase;
KW Nucleotide-binding; SOS response.
FT CHAIN 1 695 UvrABC system protein B.
FT /FTId=PRO_1000077934.
FT DOMAIN 25 176 Helicase ATP-binding.
FT DOMAIN 454 617 Helicase C-terminal.
FT DOMAIN 652 687 UVR.
FT NP_BIND 38 45 ATP (By similarity).
FT MOTIF 91 114 Beta-hairpin.
SQ SEQUENCE 695 AA; 79027 MW; 28C6FCE2217E5E56 CRC64;
MSEFQLVSSY QPTGDQPKAI AGLVKSILEG HRFQTLLGAT GTGKTFTIAH TIQQVGRPTL
VMAPNKTLAA QLCNELRELF PYNAVEYFIS YYDYYQPEAY VPSTDTYIAK SSSINDEIDM
LRHSATRSLF ERRDVIVVAS VSCIYGLGMP EEYLKASIPF QVGQEINQRE VLRDLAGIQY
ERNDLELARG RFRVKGDVLE IVPAYEDRVI RIEFFGDEIE AIRLIDPVTG EILTSLSALR
VYPARHFVTP EAQLQQAILN IEQELEEQLA FFRKQGKLLE AQRLEQRTRY DLEMLREVGY
CNGIENYSRH LTGRKEGEPP ACLVDYFKAN DWLLVVDESH VTVPQIRGMY NGDRARKQVL
VDHGFRLPSA LDNRPLKAEE FWAKVHQCVF VSATPGNWEL EQSGAQFETV VENGKTLKFY
VPGTGRVIEQ VIRPTGVVDP EVHVRPTAGQ VEDLLGEIYL RLERSQQGLP ERVIVTTLTK
RMAEDLTEYL QERGIRVRYL HSEISSIERI EILQDFREGA FDVLVGVNLL REGLDLPEVS
LVAILDADKE GFLRAERSLI QMIGRAARNV RGTVVMYADT LTGSMARAIA ETQRRREIQL
QYNRQHNITP KPIIKKNSNA ILSFLAISRK LNSQDLEKAF PVADEIPLSE IPELIGQLEL
KMKAAAKNLE FEEAAQLRDQ IKKLRQRLLG HHQST
//
