ID A0A1P8MC71_9VIBR Unreviewed; 676 AA. AC A0A1P8MC71; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 13-SEP-2023, entry version 23. DE RecName: Full=UvrABC system protein B {ECO:0000256|ARBA:ARBA00029504, ECO:0000256|HAMAP-Rule:MF_00204}; DE Short=Protein UvrB {ECO:0000256|HAMAP-Rule:MF_00204}; DE AltName: Full=Excinuclease ABC subunit B {ECO:0000256|HAMAP-Rule:MF_00204}; GN Name=uvrB {ECO:0000256|HAMAP-Rule:MF_00204}; GN ORFNames=BWP24_05295 {ECO:0000313|EMBL:APX05624.1}; OS Vibrio campbellii. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=680 {ECO:0000313|EMBL:APX05624.1, ECO:0000313|Proteomes:UP000186174}; RN [1] {ECO:0000313|EMBL:APX05624.1, ECO:0000313|Proteomes:UP000186174} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMB29 {ECO:0000313|EMBL:APX05624.1, RC ECO:0000313|Proteomes:UP000186174}; RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.; RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and CC processing of DNA lesions. A damage recognition complex composed of 2 CC UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of CC the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps CC around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB CC and probably causes local melting of the DNA helix, facilitating CC insertion of UvrB beta-hairpin between the DNA strands. Then UvrB CC probes one DNA strand for the presence of a lesion. If a lesion is CC found the UvrA subunits dissociate and the UvrB-DNA preincision complex CC is formed. This complex is subsequently bound by UvrC and the second CC UvrB is released. If no lesion is found, the DNA wraps around the other CC UvrB subunit that will check the other stand for damage. CC {ECO:0000256|HAMAP-Rule:MF_00204}. CC -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for CC lesions. Interacts with UvrC in an incision complex. CC {ECO:0000256|ARBA:ARBA00026033, ECO:0000256|HAMAP-Rule:MF_00204, CC ECO:0000256|RuleBase:RU003587}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_00204, ECO:0000256|RuleBase:RU003587}. CC -!- DOMAIN: The beta-hairpin motif is involved in DNA binding. CC {ECO:0000256|HAMAP-Rule:MF_00204}. CC -!- SIMILARITY: Belongs to the UvrB family. {ECO:0000256|ARBA:ARBA00008533, CC ECO:0000256|HAMAP-Rule:MF_00204, ECO:0000256|RuleBase:RU003587}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP019293; APX05624.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1P8MC71; -. DR EnsemblBacteria; APX05624; APX05624; BWP24_05295. DR OrthoDB; 9806651at2; -. DR Proteomes; UP000186174; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-UniRule. DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule. DR CDD; cd17916; DEXHc_UvrB; 1. DR CDD; cd18790; SF2_C_UvrB; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3. DR Gene3D; 4.10.860.10; UVR domain; 1. DR HAMAP; MF_00204; UvrB; 1. DR InterPro; IPR006935; Helicase/UvrB_N. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001943; UVR_dom. DR InterPro; IPR036876; UVR_dom_sf. DR InterPro; IPR004807; UvrB. DR InterPro; IPR041471; UvrB_inter. DR InterPro; IPR024759; UvrB_YAD/RRR_dom. DR NCBIfam; TIGR00631; uvrb; 1. DR PANTHER; PTHR24029; UVRABC SYSTEM PROTEIN B; 1. DR PANTHER; PTHR24029:SF0; UVRABC SYSTEM PROTEIN B; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF04851; ResIII; 1. DR Pfam; PF02151; UVR; 1. DR Pfam; PF12344; UvrB; 1. DR Pfam; PF17757; UvrB_inter; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF46600; C-terminal UvrC-binding domain of UvrB; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00204}; Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00204}; KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP- KW Rule:MF_00204}; KW DNA excision {ECO:0000256|ARBA:ARBA00022769, ECO:0000256|HAMAP- KW Rule:MF_00204}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP- KW Rule:MF_00204}; KW Excision nuclease {ECO:0000256|ARBA:ARBA00022881, ECO:0000256|HAMAP- KW Rule:MF_00204}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00204}; KW SOS response {ECO:0000256|ARBA:ARBA00023236, ECO:0000256|HAMAP- KW Rule:MF_00204}. FT DOMAIN 26..159 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 432..598 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT DOMAIN 636..671 FT /note="UVR" FT /evidence="ECO:0000259|PROSITE:PS50151" FT COILED 258..285 FT /evidence="ECO:0000256|SAM:Coils" FT MOTIF 92..115 FT /note="Beta-hairpin" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204" FT BINDING 39..46 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00204" SQ SEQUENCE 676 AA; 77037 MW; CBFD3E1188F32574 CRC64; MSKVYELVSE YQPSGDQPTA IKQLLEGLDS GLAHQTLLGV TGSGKTFTLA NVIAEAQRPA ILLAPNKTLA AQLYGEMKAF FPNNAVEYFV SYYDYYQPEA YVPTTDTFIE KDASVNAHIE QMRLSATKAL LERKDAIIVA SVSAIYGLGD PESYLQMMLH LRRGDVIDQR DMLRRLAELQ YSRNDVAFER GQFRVRGEVI DIFPAESDQD AVRVEMFDDE VDCISVFDPL TGVVKQRDLP RYTIYPKTHY VTPRERILDA IESIKDELEV RKKQLLDSNK LLEEQRISQR TQFDIEMMNE LGFCSGIENY SRYLSGRAEG EPPPTLFDYL PHDGLLIIDE SHVTVPQIGA MYKGDRSRKE TLVEFGFRLP SALDNRPMKF EEFEAISPQT IFVSATPGNY ELEKSADEIA DQVVRPTGLL DPELEVRPVA TQVDDLLSEI RIRAAQDERV LVTTLTKRMA EDLTEYLHEH DVKVRYLHSD IDTVERVEII RDLRLGEFDV LVGINLLREG LDMPEVSLVA ILDADKEGFL RSERSLIQTI GRAARNIKGK AILYADSITK SMKKAMDETD RRREKQKAYN AEMGIEPQAL KRNIKDIMEL GDITKSKRQR NTKQVPLSKV AEPSQTYEIM SPQQLEKEIS RLEAAMYQHA QDLEFELAAQ KRDEIEKLRA QFIANS //