GenomeNet

Database: UniProt
Entry: Q9CI06
LinkDB: Q9CI06
Original site: Q9CI06 
ID   UVRB_LACLA              Reviewed;         692 AA.
AC   Q9CI06;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   18-SEP-2019, entry version 118.
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=LL0562;
GN   ORFNames=L0257;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus
OS   lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K.,
RA   Weissenbach J., Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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; AE005176; AAK04660.1; -; Genomic_DNA.
DR   PIR; B86695; B86695.
DR   RefSeq; NP_266718.1; NC_002662.1.
DR   RefSeq; WP_003130812.1; NC_002662.1.
DR   SMR; Q9CI06; -.
DR   STRING; 272623.L0257; -.
DR   PaxDb; Q9CI06; -.
DR   PRIDE; Q9CI06; -.
DR   EnsemblBacteria; AAK04660; AAK04660; L0257.
DR   GeneID; 1114181; -.
DR   KEGG; lla:L0257; -.
DR   PATRIC; fig|272623.7.peg.600; -.
DR   eggNOG; ENOG4105CCW; Bacteria.
DR   eggNOG; COG0556; LUCA.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   BioCyc; LLAC272623:L0257-MONOMER; -.
DR   Proteomes; UP000002196; 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; 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; Complete proteome; Cytoplasm; DNA damage; DNA excision;
KW   DNA repair; Excision nuclease; Nucleotide-binding; Reference proteome;
KW   SOS response.
FT   CHAIN         1    692       UvrABC system protein B.
FT                                /FTId=PRO_0000138398.
FT   DOMAIN       32    418       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      436    631       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      656    691       UVR. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   NP_BIND      45     52       ATP. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   MOTIF        98    121       Beta-hairpin.
SQ   SEQUENCE   692 AA;  79131 MW;  9585B28875E7C402 CRC64;
     MAIERITDNK FELVSKYEPA GDQGEAIAEL VDNIENGEKA QILRGATGTG KTYTMSQVIA
     RTGKPTLVMA HNKTLAGQLY SEFKEFFPNN AVEYFVSYYD YYQPEAYVPS SDTYIEKDSS
     VNDEIDKLRH SATSSLLERN DVIVVASVSC IYGLGSPKEY QDSVVSLRPG QEISRDQLLN
     DLVGIQFERN DIDFQRGCFR VRGDVVEVFP ASRDEHAFRV EFFGDEIDRI REIEVLTGQV
     LGEVDHLAIF PATHFMTNDD RMEESIAKIE AELEEQLKVF 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 VDKEILDSGY YTEYEGQKYK ITRSMKHAMD
     ETARRREIQM AYNEEHGITP QTIKKEIRDL IAITKKTDSG EIEEVDASAM TKKERKALVK
     KLEKEMQQAA SALDFEGAAQ LRDMVLELRA MD
//
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