ID A0A1P8MC71_9VIBR Unreviewed; 676 AA. AC A0A1P8MC71; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 10-MAY-2017, entry version 2. DE RecName: Full=UvrABC system protein B {ECO:0000256|HAMAP-Rule:MF_00204, ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS00632035}; 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; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; 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 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. {ECO:0000256|HAMAP- CC Rule:MF_00204, ECO:0000256|SAAS:SAAS00632042}. CC -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for CC lesions. Interacts with UvrC in an incision complex. CC {ECO:0000256|HAMAP-Rule:MF_00204, ECO:0000256|RuleBase:RU003587, CC ECO:0000256|SAAS:SAAS00632049}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00204, CC ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS00632032}. 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|HAMAP- CC Rule:MF_00204, ECO:0000256|RuleBase:RU003587, CC ECO:0000256|SAAS:SAAS00632074}. 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 RefSeq; WP_077200428.1; NZ_CP019293.1. DR RefSeq; WP_077200428.1; NZ_CP019293.1. DR Proteomes; UP000186174; Chromosome 1. DR Gene3D; 4.10.860.10; -; 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; 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; SSF46600; 1. DR SUPFAM; SSF52540; SSF52540; 3. 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 {ECO:0000256|HAMAP-Rule:MF_00204, KW ECO:0000256|SAAS:SAAS00632044}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000186174}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00204, KW ECO:0000256|SAAS:SAAS00632071}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00204, KW ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS00632043}; KW DNA excision {ECO:0000256|HAMAP-Rule:MF_00204, KW ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS00632054}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_00204, KW ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS00632038}; KW Excision nuclease {ECO:0000256|HAMAP-Rule:MF_00204, KW ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS00632031}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00204, KW ECO:0000256|SAAS:SAAS00632060}; KW SOS response {ECO:0000256|HAMAP-Rule:MF_00204, KW ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS00632076}. FT DOMAIN 26 159 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. FT DOMAIN 432 598 Helicase C-terminal. FT {ECO:0000259|PROSITE:PS51194}. FT DOMAIN 636 671 UVR. {ECO:0000259|PROSITE:PS50151}. FT NP_BIND 39 46 ATP. {ECO:0000256|HAMAP-Rule:MF_00204}. FT COILED 258 285 {ECO:0000256|SAM:Coils}. FT MOTIF 92 115 Beta-hairpin. {ECO:0000256|HAMAP-Rule: FT 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 //