ID UVRB_SALCH Reviewed; 673 AA. AC Q57RF9; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 1. DT 27-MAR-2024, entry version 102. 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=SCH_0796; OS Salmonella choleraesuis (strain SC-B67). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=321314; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC-B67; RX PubMed=15781495; DOI=10.1093/nar/gki297; RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S., RA Lee Y.-S.; RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly RT invasive and resistant zoonotic pathogen."; RL Nucleic Acids Res. 33:1690-1698(2005). 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; AE017220; AAX64702.1; -; Genomic_DNA. DR RefSeq; WP_000042502.1; NC_006905.1. DR AlphaFoldDB; Q57RF9; -. DR SMR; Q57RF9; -. DR KEGG; sec:SCH_0796; -. DR HOGENOM; CLU_009621_2_1_6; -. DR Proteomes; UP000000538; 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: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; 6.10.140.240; -; 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; Nucleotide-binding; SOS response. FT CHAIN 1..673 FT /note="UvrABC system protein B" FT /id="PRO_0000227357" FT DOMAIN 26..414 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204" FT DOMAIN 431..597 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204" FT DOMAIN 633..668 FT /note="UVR" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204" FT MOTIF 92..115 FT /note="Beta-hairpin" FT BINDING 39..46 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204" SQ SEQUENCE 673 AA; 76135 MW; 054E205FADA6C890 CRC64; MSKPFKLNSA FKPSGDQPDA IRRLEEGLED GLAHQTLLGV TGSGKTFTIA NVIADLQRPT MVLAPNKTLA AQLYGEMKEF FPENAVEYFV SYYDYYQPEA YVPSSDTFIE KDASVNEHIE QMRLSATKAL LERRDVVVVA SVSAIYGLGD PDLYLKMMLH LTVGMLIDQR AILRRLAELQ YTRNDQAFQR GTFRVRGEVI DIFPAESDDI ALRVELFDEE VERLSLFDPL TGQVESTVPR YTIYPKTHYV TPRERILQAM EEIKDELADR RKVLLANNKL LEEQRLSQRT QFDLEMMNEL GYCSGIENYS RFLSGRGPGE PPPTLFDYLP ADGLLVVDES HVTIPQIGGM YRGDRARKET LVEYGFRLPS ALDNRPLKFE EFEALAPQTI YVSATPGNYE LEKSGDEVVD QVVRPTGLLD PIIEVRPVAT QVDDLLSEIR QRAAINERVL VTTLTKRMAE DLTEYLEEHG ERVRYLHSDI DTVERMEIIR DLRLGEFDVL VGINLLREGL DMPEVSLVAI LDADKEGFLR SERSLIQTIG RAARNVNGKA ILYGDKITPS MAKAIGETER RREKQQKYNE EHGITPQGLN KKVVDILALG QNIAKTKAKG KGKGRSTAKA GIVELDMTPK ALQQKIHELE GQMMQHAQNL EFEEAAQIRD QLHQLRELFI AAS //