UVRB_BACTN
ID UVRB_BACTN Reviewed; 677 AA.
AC Q8AA95;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=BT_0570;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
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; AE015928; AAO75677.1; -; Genomic_DNA.
DR RefSeq; NP_809483.1; NC_004663.1.
DR RefSeq; WP_008763156.1; NZ_UYXG01000009.1.
DR AlphaFoldDB; Q8AA95; -.
DR SMR; Q8AA95; -.
DR STRING; 226186.BT_0570; -.
DR PaxDb; Q8AA95; -.
DR PRIDE; Q8AA95; -.
DR EnsemblBacteria; AAO75677; AAO75677; BT_0570.
DR GeneID; 60926527; -.
DR KEGG; bth:BT_0570; -.
DR PATRIC; fig|226186.12.peg.571; -.
DR eggNOG; COG0556; Bacteria.
DR HOGENOM; CLU_009621_2_1_10; -.
DR InParanoid; Q8AA95; -.
DR OMA; EYVDRMV; -.
DR Proteomes; UP000001414; 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..677
FT /note="UvrABC system protein B"
FT /id="PRO_0000227288"
FT DOMAIN 24..412
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 429..591
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 636..671
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT MOTIF 90..113
FT /note="Beta-hairpin"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
SQ SEQUENCE 677 AA; 77113 MW; D915939CCB40898C CRC64;
MNFELTSAYK PTGDQPEAIA QLTEGVLQGV PAQTLLGVTG SGKTFTIANV IANINKPTLI
LSHNKTLAAQ LYSEFKGFFP NNAVEYYVSY YDYYQPEAYL PNSDTYIEKD LAINDEIDKL
RLAATSSLLS GRKDVVVVSS VSCIYGMGNP SDFYKNVIEI ERGRMLDRNV FLRRLVDSLY
VRNDIDLNRG NFRVKGDTVD IFLAYSDTLL RVTFWGDEID GIEEVDPITG VTTAPFEAYK
IYPANLFMTT KEATLRAIHE IEDDLTKQVA FFESIGKEYE AKRLYERVTY DMEMIRELGH
CSGIENYSRY FDGRAAGTRP YCLLDFFPDD FLLVIDESHV SVPQVRAMYG GDRARKINLV
EYGFRLPAAM DNRPLKFEEF EEMTKQVIYV SATPAEYELI QSEGIVVEQV IRPTGLLDPV
IEVRPSLNQI DDLMEEIQLR IEKEERVLVT TLTKRMAEEL TEYLLNNNVR CNYIHSDVDT
LERVKIMDDL RQGVYDVLIG VNLLREGLDL PEVSLVAILD ADKEGFLRSH RSLTQTAGRA
ARNVNGKVIM YADKITDSMR LTIDETNRRR EKQLAYNEAN GITPQQIKKA RNLSVFGSPG
SEADELLKEK HAYVEPSSPN IAADPIVQYM SKAQMEKSIE RTRKLMQEAA KKLEFIEAAQ
YRNELLKLED LMKEKWG
