ID UVRB_HELPY Reviewed; 658 AA. AC P94846; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 27-MAR-2024, entry version 143. 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=HP_1114; OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=85962; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 53726 / 84-183; RX PubMed=9583946; DOI=10.1016/s0378-1119(98)00028-6; RA Thompson S.A., Latch R.L., Blaser J.M.; RT "Molecular characterization of the Helicobacter pylori uvr B gene."; RL Gene 209:113-122(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700392 / 26695; RX PubMed=9252185; DOI=10.1038/41483; RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A., RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.; RT "The complete genome sequence of the gastric pathogen Helicobacter RT pylori."; RL Nature 388:539-547(1997). 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; U80807; AAC46270.1; -; Genomic_DNA. DR EMBL; AE000511; AAD08158.1; -; Genomic_DNA. DR PIR; B64659; B64659. DR RefSeq; NP_207905.1; NC_000915.1. DR RefSeq; WP_001127890.1; NC_018939.1. DR AlphaFoldDB; P94846; -. DR SMR; P94846; -. DR DIP; DIP-3238N; -. DR IntAct; P94846; 18. DR MINT; P94846; -. DR STRING; 85962.HP_1114; -. DR PaxDb; 85962-C694_05745; -. DR EnsemblBacteria; AAD08158; AAD08158; HP_1114. DR KEGG; hpy:HP_1114; -. DR PATRIC; fig|85962.47.peg.1195; -. DR eggNOG; COG0556; Bacteria. DR InParanoid; P94846; -. DR OrthoDB; 9806651at2; -. DR PhylomeDB; P94846; -. DR Proteomes; UP000000429; 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; 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; 2. 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; Reference proteome; SOS response. FT CHAIN 1..658 FT /note="UvrABC system protein B" FT /id="PRO_0000138396" FT DOMAIN 25..414 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204" FT DOMAIN 433..607 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204" FT DOMAIN 623..658 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" FT VARIANT 59 FT /note="A -> T (in strain: 84-183)" FT VARIANT 231 FT /note="K -> R (in strain: 84-183)" FT VARIANT 259 FT /note="I -> V (in strain: 84-183)" FT VARIANT 376 FT /note="N -> T (in strain: 84-183)" FT VARIANT 407 FT /note="K -> Q (in strain: 84-183)" FT VARIANT 443 FT /note="L -> S (in strain: 84-183)" FT VARIANT 475 FT /note="A -> V (in strain: 84-183)" FT VARIANT 501 FT /note="I -> V (in strain: 84-183)" FT VARIANT 607 FT /note="R -> K (in strain: 84-183)" FT VARIANT 636..637 FT /note="CT -> HA (in strain: 84-183)" SQ SEQUENCE 658 AA; 75916 MW; 06BC0EE689AB3ADE CRC64; MPLFDLKSPY PPAGDQPQAI EALTKSLKNN NHYQTLVGVT GSGKTYTMAN IIAQTNKPAL IMSHNKTLCA QLYSEFKAFF PHNRVEYFIS HFDYYQPESY IPRRDLFIEK DSSINDDLER LRLSATTSLL GYDDVIVIAS VSANYGLGNP EEYLKVMEKI KVGEKRAYKS FLLKLVEMGY SRNEVVFDRG SFRATGECVD IFPAYNDAEF IRIEFFGDEI ERIAVFDALE KNEIKRLDSV MLYAASQFAV GSERLNLAIK SIEDELALRL KFFKEQDKML EYNRLKQRTE HDLEMISATG VCKGIENYAR HFTGKAPNET PFCLFDYLGI FEREFLVIVD ESHVSLPQFG GMYAGDMSRK SVLVEYGFRL PSALDNRPLK FDEFIHKNCQ FLFVSATPNK LELELSKKNV AEQIIRPTGL LDPKFEVRDS DKQVQDLFDE IKLVVARGER VLITTLTKKM AEELCKYYAE WGLKARYMHS EIDAIERNHI IRSLRLKEFD ILIGINLLRE GLDLPEVSLV AIMDADKEGF LRSETSLIQT MGRAARNANG KVLLYAKKIT QSMQKAFEIT SYRRAKQEEF NKIHNITPKT VTRALEEELK LRDDEIRIAK ALKKDKMPKS EREKIIKELD KKMRECTKNL DFEEAMRLRD EIAQLRTL //