ID UVRB_ESCF3 Reviewed; 673 AA.
AC B7LJY3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 01-MAY-2013, entry version 38.
DE RecName: Full=UvrABC system protein B;
DE Short=Protein UvrB;
DE AltName: Full=Excinuclease ABC subunit B;
GN Name=uvrB; OrderedLocusNames=EFER_2332;
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / CDC 0568-73;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A.,
RA Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M.,
RA Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M.,
RA Johnson J., Le Bouguenec C., Lescat M., Mangenot S.,
RA Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A.,
RA Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B.,
RA Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928158; CAQ89833.1; -; Genomic_DNA.
DR RefSeq; YP_002383448.1; NC_011740.1.
DR STRING; 585054.EFER_2332; -.
DR EnsemblBacteria; CAQ89833; CAQ89833; EFER_2332.
DR GeneID; 7122087; -.
DR KEGG; efe:EFER_2332; -.
DR PATRIC; 32129012; VBIEscFer122920_2249.
DR eggNOG; COG0556; -.
DR HOGENOM; HOG000073580; -.
DR KO; K03702; -.
DR ProtClustDB; PRK05298; -.
DR BioCyc; EFER585054:GJJM-2325-MONOMER; -.
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 1 673 UvrABC system protein B.
FT /FTId=PRO_1000200548.
FT DOMAIN 26 183 Helicase ATP-binding.
FT DOMAIN 431 597 Helicase C-terminal.
FT DOMAIN 633 668 UVR.
FT NP_BIND 39 46 ATP (By similarity).
FT MOTIF 92 115 Beta-hairpin.
SQ SEQUENCE 673 AA; 76256 MW; 35BD8AE8545ECBC6 CRC64;
MSKPFKLNSA FKPSGDQPEA IRRLEEGLED GLAHQTLLGV TGSGKTFTIA NVIADLQRPT
MVLAPNKTLA AQLYGEMKEF FPENAVEYFV SYYDYYQPEA YVPSSDTFIE KDASVNEHIE
QMRLSATKAM LERRDVVVVA SVSAIYGLGD PDLYLKMMLH LTVGMIIDQR AILRRLAELQ
YTRNDQAFQR GTFRVRGEVI DIFPAESDDI ALRVELFDEE VERLSLFDPL TGQIVSTIPR
FTIYPKTHYV TPRERIVQAM EEIKEELAAR RKVLLENNKL LEEQRLTQRT QFDLEMMNEL
GYCSGIENYS RFLSGRGPGE PPPTLFDYLP ADGLLVVDES HVTIPQIGGM YRGDRARKET
LVEYGFRLPS ALDNRPLKFE EFEALAPQTI YVSATPGNYE LEKSGGDVVD QVVRPTGLLD
PIIEVRPVAT QVDDLLSEIR QRAAINERVL VTTLTKRMAE DLTEYLEEHG ERVRYLHSDI
DTVERMEIIR DLRLGEFDVL VGINLLREGL DMPEVSLVAI LDADKEGFLR SERSLIQTIG
RAARNVNGKA ILYGDKITPS MAKAIGETER RREKQQKYNE EHGITPQGLN KKVVDILALG
QNIAKTKAKG RGKSRPIVEP DNVPMDMSPK ALQQKIHELE GLMMQHAQNL EFEEAAQIRD
QLHQLRELFI AAS
//
