UVRB_LACLM
ID UVRB_LACLM Reviewed; 692 AA.
AC A2RIP3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=llmg_0534;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
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; AM406671; CAL97138.1; -; Genomic_DNA.
DR RefSeq; WP_011834568.1; NZ_WJVF01000027.1.
DR AlphaFoldDB; A2RIP3; -.
DR SMR; A2RIP3; -.
DR STRING; 416870.llmg_0534; -.
DR PRIDE; A2RIP3; -.
DR EnsemblBacteria; CAL97138; CAL97138; llmg_0534.
DR KEGG; llm:llmg_0534; -.
DR eggNOG; COG0556; Bacteria.
DR HOGENOM; CLU_009621_2_1_9; -.
DR OMA; EYVDRMV; -.
DR PhylomeDB; A2RIP3; -.
DR BioCyc; LLAC416870:LLMG_RS02800-MON; -.
DR Proteomes; UP000000364; 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; 2.
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..692
FT /note="UvrABC system protein B"
FT /id="PRO_1000077899"
FT DOMAIN 32..187
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 436..631
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 656..691
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT MOTIF 98..121
FT /note="Beta-hairpin"
FT BINDING 45..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
SQ SEQUENCE 692 AA; 79015 MW; C2031D5B763B2EA6 CRC64;
MAIERITDNK FELVSKYDPA GDQGQAISEL VENIENGEKA QILRGATGTG KTYTMSQVIA
QTGKPTLVMA HNKTLAGQLY SEFKEFFPNN AVEYFVSYYD YYQPEAYVPS SDTYIEKDSS
VNDEIDKLRH SATSSLLERN DVIVVASVSC IYGLGSPKEY QDSVVSLRPG QEISRDQLLN
DLVGIQFERN DIDFQRGCFR VRGDVVEVFP ASRDEHAFRV EFFGDEIDRI REIEVLTGQV
LGEVDHLAIF PATHFMTNDD RMEESIAKIE AELEAQLKVF RSEGKLLEAQ RLEQRTNYDI
EMLREMGYCN GVENYSRHMD GREEGEPPYT LLDFFPDDFM IMIDESHMTM GQVKGMYNGD
RARKEMLCNY GFRLPSALDN RPLKREEFES HVHQIVYVSA TPGDYEMEQT DTIVEQIIRP
TGLLDPVVEV RPMMGQIDDL VGEIHKRAEK NERVFVTTLT KKMSEDLTAY FKEMGIKVKY
MHSDIKTLER TEIIRDLRLG VFDVLVGINL LREGIDVPEV SLVAILDADK EGFLRNERGL
IQTIGRAARN SEGHVILYSD MAKALDENDP ADKEILDSGY YTEYEGKKYK ITRSMKHAMD
ETARRRDIQM AYNEEHGITP QTIKKEIRDL IAITKKTDSG ELEEVDASAM NKKERKALVK
KLEKEMQQAA AALDFEGAAQ LRDMVLELRA MD
