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Database: UniProt
Entry: Q64T09
LinkDB: Q64T09
Original site: Q64T09 
ID   UVRB_BACFR              Reviewed;         677 AA.
AC   Q64T09;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   31-JUL-2019, entry version 94.
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=BF2620;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA
RT   inversions regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
CC   -!- FUNCTION: The UvrABC repair system catalyzes the recognition and
CC       processing of DNA lesions. A damage recognition complex composed
CC       of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon
CC       binding of the UvrA(2)B(2) complex to a putative damaged site, the
CC       DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP
CC       binding by UvrB and probably causes local melting of the DNA
CC       helix, facilitating insertion of UvrB beta-hairpin between the DNA
CC       strands. Then UvrB probes one DNA strand for the presence of a
CC       lesion. If a lesion is found the UvrA subunits dissociate and the
CC       UvrB-DNA preincision complex is formed. This complex is
CC       subsequently bound by UvrC and the second UvrB is released. If no
CC       lesion is found, the DNA wraps around the other UvrB subunit that
CC       will check the other stand for damage. {ECO:0000255|HAMAP-
CC       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}.
DR   EMBL; AP006841; BAD49370.1; -; Genomic_DNA.
DR   RefSeq; WP_011202946.1; NC_006347.1.
DR   RefSeq; YP_099904.1; NC_006347.1.
DR   SMR; Q64T09; -.
DR   EnsemblBacteria; BAD49370; BAD49370; BF2620.
DR   GeneID; 3083645; -.
DR   KEGG; bfr:BF2620; -.
DR   PATRIC; fig|295405.11.peg.2531; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   Proteomes; UP000002197; 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:ATPase 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   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; Complete proteome; Cytoplasm; DNA damage; DNA excision;
KW   DNA repair; Excision nuclease; Nucleotide-binding; SOS response.
FT   CHAIN         1    677       UvrABC system protein B.
FT                                /FTId=PRO_0000227286.
FT   DOMAIN       24    412       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      429    591       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      635    670       UVR. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   NP_BIND      37     44       ATP. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   MOTIF        90    113       Beta-hairpin.
SQ   SEQUENCE   677 AA;  77112 MW;  4FDFCCBF94AD39C9 CRC64;
     MNFELTSAYK PTGDQPEAIA QLTEGVLEGV PAQTLLGVTG SGKTFTIANV IANINKPTLI
     LSHNKTLAAQ LYSEFKGFFP NNAVEYYVSY YDYYQPEAYL PSSDTYIEKD LAINDEIDKL
     RLAATSALLS GRKDVVVVSS VSCIYGMGNP SDFYNNVIEI ERGRTINRNV FLRRLVDSLY
     MRNDIELNRG NFRVKGDTVD IYLAYSDNLL RVTFWGDEID GIEEVDPVSG VTIAPFEAYK
     IYPANLFMTT KEATLRAIHE IEDDLTKQVA YFESIGKEYE AKRLYERVTY DMEMIRELGH
     CSGIENYSRY FDGRAAGTRP YCLLDFFPDD FLIVIDESHV SVPQIRAMYG GDRARKINLV
     EYGFRLPAAM DNRPLKFEEF ESMAKQVIYV SATPADYELV QSEGIVVEQV IRPTGLLDPV
     IEVRPSLNQI DDLMEEIQIR IEKEERILVT TLTKRMAEEL TEYLLNNNVR CNYIHSDVDT
     LERVKIMDDL RQGVYDVLIG VNLLREGLDL PEVSLVAILD ADKEGFLRSH RSLTQTAGRA
     ARNVNGMVIM YADKITDSMR LTIDETNRRR EKQLAYNEEH GITPQQIKKA RNLSVFGNGA
     ETEDTQKGTR AYVEPSSPNI AADPVVQYMS KTQLEKSMER TRKLMQEAAK KLEFIEAAQY
     RDELLKMEDL MKEKWPG
//
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