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Database: UniProt
Entry: Q12TR7
LinkDB: Q12TR7
Original site: Q12TR7 
ID   UVRB_METBU              Reviewed;         660 AA.
AC   Q12TR7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   31-JUL-2019, entry version 90.
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=Mbur_2303;
OS   Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS   ACE-M).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=259564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX   PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA   Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA   De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z.,
RA   Ting L., Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J.,
RA   Ivanova N., Dalin E., Martinez M., Lapidus A., Hauser L., Land M.,
RA   Thomas T., Cavicchioli R.;
RT   "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT   burtonii: the role of genome evolution in cold adaptation.";
RL   ISME J. 3:1012-1035(2009).
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; CP000300; ABE53159.1; -; Genomic_DNA.
DR   RefSeq; WP_011500294.1; NC_007955.1.
DR   SMR; Q12TR7; -.
DR   PRIDE; Q12TR7; -.
DR   EnsemblBacteria; ABE53159; ABE53159; Mbur_2303.
DR   GeneID; 3998882; -.
DR   KEGG; mbu:Mbur_2303; -.
DR   eggNOG; arCOG04748; Archaea.
DR   eggNOG; COG0556; LUCA.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   OrthoDB; 4923at2157; -.
DR   BioCyc; MBUR259564:G1G6A-2414-MONOMER; -.
DR   Proteomes; UP000001979; 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: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   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; Helicase; Hydrolase;
KW   Nucleotide-binding; Reference proteome; SOS response.
FT   CHAIN         1    660       UvrABC system protein B.
FT                                /FTId=PRO_1000204137.
FT   DOMAIN       25    183       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      431    593       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      622    657       UVR. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   NP_BIND      38     45       ATP. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   MOTIF        91    114       Beta-hairpin.
SQ   SEQUENCE   660 AA;  74685 MW;  C7B5740075790EFE CRC64;
     MSGFELVSDY EPKGDQPEAI RKLSEGLNKG LKHQVLLGVT GSGKTFTVAN VIQNVQKPTL
     VIAHNKTLAA QLFSEFREFF PNNAVEYFVS YYDYYQPEAY LPTTDTYIEK DSSVNEEIDR
     LRLSATKSLI ERKDVIVVSS VSSIYNIGSP DEWRRMSVIL RTGDEVGRSD LFAALINIHY
     ERNDIESAKG SFRSKGDTIE VFPAQDNHGV RIELFGDEID RISSFDPVTG KTIDEVKEDN
     SIVIYPAKHF VMPQEEMVKA LGSIEKELEG QVAKLVSENR ILESQRLTQR AKFDLEMIRE
     LGYCSGIENY SRHFDGRKPG DPPSSLLEFF PDDFLLVIDE SHVTIPQIRG MHNGDRARKE
     ALINYGFRLP SAYDNRPLTY NEFHHKINQA IYVSATPADY ELGISSAVVE QIIRPTGLVD
     PVVFIRPVEN QIDDLIGEVN KVTEKGYRTL VTTLTKRMAE DLTEYLLEMG IRVRYMHSDI
     DTLERAEIIR DLRKGVFDVL VGINLLREGL DIPEVAFVAI LDADKEGFLR SERSLIQTMG
     RASRNADGYV ILYAGKVTGS IEAALRETNR RRQIQLAYNE KHGIVPQTIH KALQRELVET
     EYGEVVSEVL GVAEDLSDIE IADMVIELEA EMHLAAKNLE FERAAALRDN IKELRSTYSL
//
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