UVRB_BIFLO
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 03-AUG-2022, entry version 108.
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., Pessi G.,
RA Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT 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 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; AE014295; AAN24798.1; -; Genomic_DNA.
DR RefSeq; NP_696162.1; NC_004307.2.
DR RefSeq; WP_011068239.1; NC_004307.2.
DR AlphaFoldDB; Q8G5L9; -.
DR SMR; Q8G5L9; -.
DR STRING; 206672.BL0990; -.
DR EnsemblBacteria; AAN24798; AAN24798; BL0990.
DR KEGG; blo:BL0990; -.
DR PATRIC; fig|206672.9.peg.692; -.
DR HOGENOM; CLU_009621_2_1_11; -.
DR OMA; EYVDRMV; -.
DR PhylomeDB; Q8G5L9; -.
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: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..703
FT /note="UvrABC system protein B"
FT /id="PRO_0000227289"
FT DOMAIN 33..419
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 436..589
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 659..694
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT MOTIF 99..122
FT /note="Beta-hairpin"
FT BINDING 46..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
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
