UVRB_CUPPJ
ID UVRB_CUPPJ Reviewed; 695 AA.
AC Q473K3;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=Reut_A1051;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
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; CP000090; AAZ60430.1; -; Genomic_DNA.
DR RefSeq; WP_011297234.1; NC_007347.1.
DR AlphaFoldDB; Q473K3; -.
DR SMR; Q473K3; -.
DR STRING; 264198.Reut_A1051; -.
DR EnsemblBacteria; AAZ60430; AAZ60430; Reut_A1051.
DR KEGG; reu:Reut_A1051; -.
DR eggNOG; COG0556; Bacteria.
DR HOGENOM; CLU_009621_2_1_4; -.
DR OMA; EYVDRMV; -.
DR OrthoDB; 95696at2; -.
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; SOS response.
FT CHAIN 1..695
FT /note="UvrABC system protein B"
FT /id="PRO_0000227353"
FT DOMAIN 45..434
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 449..602
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 646..681
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT MOTIF 111..134
FT /note="Beta-hairpin"
FT BINDING 58..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
SQ SEQUENCE 695 AA; 79112 MW; 28CA8C3331587C9E CRC64;
MSNLAEVAPA LDEDKIVTFP GSPFQLYQPF PPAGDQPEAI RQLVEGIEDG LSFQTLLGVT
GSGKTYTMAN VIARMGRPAI VFAPNKTLAA QLYSEFREFF PRNAVEYFVS YYDYYQPEAY
VPQRDLFIEK DSSINEHIEQ MRLSATKSLL ERRDTIIVAT VSAIYGIGNP NEYHQMILTL
RTGDKISQRD VIARLIAMQY TRNETDFQRG TFRVRGDTID IFPAEHAEMA VRLEMFDDEV
ESLQFFDPLT GRVRQKIPRF TVYPSSHYVT PRETVLRAIE DIKAELRDRL EFFHKENRLV
EVQRLEQRTR FDLEMLSELG FCKGIENYSR HLSGAKPGEP PPTLVDYLPS DALMFLDESH
VLIGQLNGMY NGDRARKTTL VEYGFRLPSA LDNRPLKFEE FERKMRQVMF VSATPAQFEK
EHAGQVVEQV VRPTGLVDPI IIVRPATTQV DDLLSEINLR VEAGERVLVT TLTKRMAEQL
TEFLSENGVK VRYLHSDIDT VERVEIIRDL RLGTFDVLVG INLLREGLDI PEVSLVAILD
ADKEGFLRAE RSLIQTIGRA ARNVNGTAIL YADRITDSMR KAIDETERRR AKQMAFNEAN
GITPRGVIKR IKDIIDGVYD AGEVKAELLA AQERARYEDM SEKQVSKEIK RLEKLMMDHA
KNLEFEKAAQ VRDQLAKLKA QLFGASGEEA PMPPV
