UVRB_CLOPE
ID UVRB_CLOPE Reviewed; 659 AA.
AC Q46323;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 136.
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}; OrderedLocusNames=CPE0303;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 69-155.
RC STRAIN=CPN50;
RX PubMed=7559358; DOI=10.1128/jb.177.19.5680-5685.1995;
RA Katayama S., Dupuy B., Garnier T., Cole S.T.;
RT "Rapid expansion of the physical and genetic map of the chromosome of
RT Clostridium perfringens CPN50.";
RL J. Bacteriol. 177:5680-5685(1995).
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}.
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DR EMBL; BA000016; BAB80009.1; -; Genomic_DNA.
DR EMBL; X86531; CAA60243.1; -; Genomic_DNA.
DR RefSeq; WP_011009723.1; NC_003366.1.
DR AlphaFoldDB; Q46323; -.
DR SMR; Q46323; -.
DR STRING; 195102.gene:10489559; -.
DR EnsemblBacteria; BAB80009; BAB80009; BAB80009.
DR KEGG; cpe:CPE0303; -.
DR HOGENOM; CLU_009621_2_1_9; -.
DR OMA; EYVDRMV; -.
DR Proteomes; UP000000818; 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 Gene3D; 3.40.50.300; -; 3.
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 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 Pfam; PF17757; UvrB_inter; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF46600; SSF46600; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
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; Cytoplasm; DNA damage; DNA excision; DNA repair;
KW Excision nuclease; Nucleotide-binding; Reference proteome; SOS response.
FT CHAIN 1..659
FT /note="UvrABC system protein B"
FT /id="PRO_0000138389"
FT DOMAIN 25..412
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 429..582
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 622..657
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 CONFLICT 69..75
FT /note="AAQLCAE -> GSALIVK (in Ref. 2; CAA60243)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 659 AA; 75523 MW; 4F0D94B3C647B01A CRC64;
MGEFKIQSKF KPTGDQPKAI DTLVQSIENG NRGQTLLGVT GSGKTFTMAN IIERTQKPTL
ILAHNKTLAA QLCAEFKEFF PDNIVEYFVS YYDYYQPEAY VPQTDTFIEK DASINDEIDK
LRHSATSALL ERRDVIIVAS VSCIYGLGNP EEYKKLTISL RPGMIKDRDE VIKKLIEIQY
ERNDIDFARG TFRVRGDNLD IIPSSSSSKG IRIEFFGDEI DRIREFDVLT GNIIGERQHV
SITPASHFAA SEETLEKSIR VIEDELEDRL KVLTAEDKIL EAQRLKQRTN YDIEMIREMG
YCQGIENYSR ILDGRMPGTP PQTLLDYFPE DFLMFIDESH VTLPQVRAMY AGDRSRKTSL
VEFGFRLPCA FDNRPLKFSE FESKINQVVF VSATPGEYEL DHSEIVAEQI IRPTGLLDPV
IEIRPIQGQI DDLYGEIQRT VQRGFRVLIT TLTKRMAEDL TKYLKDLNVK ATYMHSDIDT
LERMKIIREL RLGEVDVLIG INLLREGLDI PEVALVAILD ADKEGFLRSE TSLIQTIGRA
ARNSESKVIM YADNITKSMD KSIKETERRR VIQMEYNEEH NITPTTVIKG VRDIIEATKV
SEEKENYESE VKKAAKKDIP VEKLIEQYEE EMKEAAKNLQ FERAAELRDI IKDLKENSK
