ID UVRB_RICBR Reviewed; 661 AA. AC Q1RHI9; DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 27-MAR-2024, entry version 107. DE RecName: Full=UvrABC system protein B {ECO:0000255|HAMAP-Rule:MF_00204}; DE Short=Protein UvrB {ECO:0000255|HAMAP-Rule:MF_00204}; DE AltName: Full=Excinuclease ABC subunit B {ECO:0000255|HAMAP-Rule:MF_00204}; GN Name=uvrB {ECO:0000255|HAMAP-Rule:MF_00204}; GN OrderedLocusNames=RBE_1094; OS Rickettsia bellii (strain RML369-C). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group. OX NCBI_TaxID=336407; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RML369-C; RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076; RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., RA Fournier P.-E., Claverie J.-M., Raoult D.; RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in RT gene exchanges between intracellular pathogens."; RL PLoS Genet. 2:733-744(2006). 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:0000255|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:0000255|HAMAP-Rule:MF_00204}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00204}. CC -!- DOMAIN: The beta-hairpin motif is involved in DNA binding. CC {ECO:0000255|HAMAP-Rule:MF_00204}. CC -!- SIMILARITY: Belongs to the UvrB family. {ECO:0000255|HAMAP- CC Rule:MF_00204}. 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; CP000087; ABE05175.1; -; Genomic_DNA. DR RefSeq; WP_011477753.1; NC_007940.1. DR AlphaFoldDB; Q1RHI9; -. DR SMR; Q1RHI9; -. DR KEGG; rbe:RBE_1094; -. DR eggNOG; COG0556; Bacteria. DR HOGENOM; CLU_009621_2_1_5; -. DR OrthoDB; 9806651at2; -. DR Proteomes; UP000001951; Chromosome. 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:0004386; F:helicase activity; IEA:UniProtKB-KW. 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; Cytoplasm; DNA damage; DNA excision; DNA repair; KW Excision nuclease; Helicase; Hydrolase; Nucleotide-binding; KW Reference proteome; SOS response. FT CHAIN 1..661 FT /note="UvrABC system protein B" FT /id="PRO_0000277986" FT DOMAIN 25..182 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204" FT DOMAIN 430..592 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204" FT DOMAIN 621..656 FT /note="UVR" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204" FT MOTIF 91..114 FT /note="Beta-hairpin" FT BINDING 38..45 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204" SQ SEQUENCE 661 AA; 75518 MW; D4446CCF7424E0AB CRC64; MSNFSIISDY KPAGDQPKAI DEIIKGLNNK KRSQMLLGIT GSGKTFTMAN IIERTNRPTL IMAHNKTLAA QIYSEMKSIF PKNAVEYFVS YYDYYQPEAY IPKTDVFIEK DSSINEQIDL MRHSATRSLL ERRDVIVVSS VSCIYGLGSP DLYYQMTVNL EPGKSYPRDK LLNDLVNLQY ERNDIGFERG CFRVKGDNVD VFPSHYSDKA WRLSFFGNEL EYIHEFDPLT GEKLVKLDKA IIYGNSHFVM PKETVNKAIS EIEEELQKRI AFLKSQDKLL ETQRINQRTQ YDLEMLTETG SCKGVENYSR FFTGRKAGEP PPTLFEYLPK DALLFVDESH VSVPQIRAMY NGDRARKEVL VEHGFRLPSA LDNRPLKFEE WDNFRPQTVF VSATPSLFEL NETGGEVVEL IIRPTGLLDP ECIIKPATNQ VEDLVGEIQS TIAKGFCVLV TTLTKKMAED LTNYLQELKY KTSYLHSNIH TLERIEILRD LRQGTIDILV GINLLREGLD IPECGLVAIL DADKEGFLRS EVSLIQTIGR AARNSEGRVI LYADKMTKSI DKAISETMRR RTIQQEHNEK YGIIPKTINR TIHALAELEK VDSKLDKKQT HNLFENPAKL KAHIDKLRKE MLKAASNLEF EQAAKLRDQL KTLEEAALEL S //