UVRB_BIFLS
ID UVRB_BIFLS Reviewed; 703 AA.
AC B7GSZ2; E8MLF9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 79.
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};
GN OrderedLocusNames=Blon_1747, BLIJ_1806;
OS Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM
OS 1222 / NCTC 11817 / S12).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=391904;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX PubMed=19033196; DOI=10.1073/pnas.0809584105;
RA Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R.,
RA Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P.,
RA Richardson P.M., Mills D.A.;
RT "The genome sequence of Bifidobacterium longum subsp. infantis reveals
RT adaptations for milk utilization within the infant microbiome.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX PubMed=21270894; DOI=10.1038/nature09646;
RA Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T.,
RA Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J.,
RA Morita H., Hattori M., Ohno H.;
RT "Bifidobacteria can protect from enteropathogenic infection through
RT production of acetate.";
RL Nature 469:543-547(2011).
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; CP001095; ACJ52822.1; -; Genomic_DNA.
DR EMBL; AP010889; BAJ69386.1; -; Genomic_DNA.
DR RefSeq; WP_012578046.1; NZ_JDTT01000008.1.
DR AlphaFoldDB; B7GSZ2; -.
DR SMR; B7GSZ2; -.
DR PRIDE; B7GSZ2; -.
DR EnsemblBacteria; ACJ52822; ACJ52822; Blon_1747.
DR KEGG; bln:Blon_1747; -.
DR KEGG; blon:BLIJ_1806; -.
DR PATRIC; fig|391904.8.peg.1814; -.
DR HOGENOM; CLU_009621_2_1_11; -.
DR OMA; EYVDRMV; -.
DR Proteomes; UP000001360; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
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; Helicase; Hydrolase; Nucleotide-binding; SOS response.
FT CHAIN 1..703
FT /note="UvrABC system protein B"
FT /id="PRO_1000200532"
FT DOMAIN 33..190
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; 79583 MW; BBE14086E4C155F9 CRC64;
MGFNIERVDK PFVVKSPYQP SGDQPKAIEE LATRIENGEN DVVLMGATGT GKTATTAWLI
ERLQRPTLII EPNKTLAAQL CAEFRELMPD NAVSYFVSYY DYYQPEAYIP QTDTYIEKDS
NINDDVERLR HQATANLLTR RDCVVVATVS CIYGLGTPEE YAGRMLFLKE GQQINRDDLL
RRFVAMQYKR NDIAFTRGTF RVRGDTVEII PVYEELAIRI EFFGDEIDRI STLHPLTGDV
IAHEPQVHIF PASHYVAGPE RMERALKTIR EELDGRLSEL RKQGKELEAQ RLDMRTTYDL
EMLTQVGVCS GVENYSRHLD GRAAGTPPHT LLDFFPDDFL LVIDESHVTV PQIGAMYEGD
ASRKRTLVEH GFRLPSAMDN RPLKWPEFLQ RVGQTVYLSA TPGDYELGLS DGVVEQIIRP
TGLLDPKIDV RPVKGQIDDL LAEIKARVAR NERALVTTLT KKMAEDLTDY LLERGIKVEY
LHSDVDTLRR VELLRMLREG KIDVIVGINL LREGLDLPEV SLVAILDADK EGFLRSYRSL
IQTIGRAARN VSGVVIMYAD ETTEAMRQAI DETDRRRAKQ IAYNQEHGID PKPLIKKISD
VNDMLAKEDV DTQTLLEGGY RNAGKAGNTH LGVPVLDPNE ADKRHEEILK AGLPAQDLAD
LIRQLSEQMH TAAEQLQFEL AARLRDEIRD LKKELRQMTE AGQ
