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Database: UniProt
Entry: Q8G5L9
LinkDB: Q8G5L9
Original site: Q8G5L9 
ID   UVRB_BIFLO              Reviewed;         703 AA.
AC   Q8G5L9;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   31-JUL-2019, entry version 100.
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=BL0990;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B.,
RA   Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M.,
RA   Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation
RT   to the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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; AE014295; AAN24798.1; -; Genomic_DNA.
DR   RefSeq; NP_696162.1; NC_004307.2.
DR   RefSeq; WP_011068239.1; NC_004307.2.
DR   SMR; Q8G5L9; -.
DR   PRIDE; Q8G5L9; -.
DR   EnsemblBacteria; AAN24798; AAN24798; BL0990.
DR   GeneID; 1022497; -.
DR   KEGG; blo:BL0990; -.
DR   PATRIC; fig|206672.9.peg.692; -.
DR   eggNOG; ENOG4105CCW; Bacteria.
DR   eggNOG; COG0556; LUCA.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   PhylomeDB; Q8G5L9; -.
DR   BioCyc; BLON206672:G1FZZ-665-MONOMER; -.
DR   Proteomes; UP000000439; 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; Reference proteome;
KW   SOS response.
FT   CHAIN         1    703       UvrABC system protein B.
FT                                /FTId=PRO_0000227289.
FT   DOMAIN       33    419       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      436    589       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      659    694       UVR. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   NP_BIND      46     53       ATP. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   MOTIF        99    122       Beta-hairpin.
SQ   SEQUENCE   703 AA;  79662 MW;  65505D5544F5D424 CRC64;
     MGFNIERADK PFVVKSPYKP SGDQPQAIAE LAERIENGEN DVVLMGATGT GKTATTAWLI
     EKLQRPTLII EPNKTLAAQL CAEFRELMPD NAVSYFVSYY DYYQPEAYIP QTDTYIEKDS
     NINDDVERLR HQATANLLTR RDCVVVATVS CIYGLGTPEE YAGRMLFLKV GQEINRDDLL
     RQFVAMQYKR NDIAFTRGTF RVRGDTVEII PVYEELAVRI EFFGDEIDRI STLHPLTGDE
     IDEENEVHIF PASHYVAGPE RMERALKTIR EELEERLAEL RKQGKELEAQ RLNMRTTYDL
     EMLTQVGVCS GVENYSRHFD GRAAGTPPHT LLDFFPDDFL LVIDESHVTV PQIGAMYEGD
     ASRKRTLVEH GFRLPSAMDN RPLKWPEFLQ RVGQTVYLSA TPGDYEMGLS DGVVEQIIRP
     TGLLDPKIDV RPVKGQIDDL LAEIKARVAK NERALVTTLT KKMAEDLTDY LLERGIKVEY
     LHSDVDTLRR VELLRMLREG KIDVIVGINL LREGLDLPEV SLVAILDADK EGFLRSYRSL
     IQTIGRAARN VSGTVIMYAD ETTEAMRQAI DETDRRRAKQ IAYNQEHGID PKPLIKKISD
     VNDMLAKEDV DTQTLLEGGY RNAGKAGNTH LGVPVLDPNE ADKRHEEILK AGLPAQDLAD
     LIRQLSEQMH TAAEQLQFEL AARLRDEIRD LKKELRQMTE ANK
//
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