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Database: UniProt
Entry: Q67T57
LinkDB: Q67T57
Original site: Q67T57 
ID   UVRB_SYMTH              Reviewed;         659 AA.
AC   Q67T57;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   31-JUL-2019, entry version 101.
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=STH151;
OS   Symbiobacterium thermophilum (strain T / IAM 14863).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Symbiobacteriaceae;
OC   Symbiobacterium.
OX   NCBI_TaxID=292459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T / IAM 14863;
RX   PubMed=15383646; DOI=10.1093/nar/gkh830;
RA   Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T.,
RA   Morimura K., Ikeda H., Hattori M., Beppu T.;
RT   "Genome sequence of Symbiobacterium thermophilum, an uncultivable
RT   bacterium that depends on microbial commensalism.";
RL   Nucleic Acids Res. 32:4937-4944(2004).
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; AP006840; BAD39136.1; -; Genomic_DNA.
DR   RefSeq; WP_011194286.1; NC_006177.1.
DR   SMR; Q67T57; -.
DR   STRING; 292459.STH151; -.
DR   EnsemblBacteria; BAD39136; BAD39136; STH151.
DR   KEGG; sth:STH151; -.
DR   eggNOG; ENOG4105CCW; Bacteria.
DR   eggNOG; COG0556; LUCA.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   OrthoDB; 95696at2; -.
DR   BioCyc; STHE292459:G1G28-160-MONOMER; -.
DR   Proteomes; UP000000417; 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; 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; Nucleotide-binding; Reference proteome;
KW   SOS response.
FT   CHAIN         1    659       UvrABC system protein B.
FT                                /FTId=PRO_0000227373.
FT   DOMAIN       25    414       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      431    597       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      620    655       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   659 AA;  75407 MW;  CD202F659C8EB5B3 CRC64;
     MKPFKVVAPF EPTGDQPQAI ERLSEGVRRG AREQILLGAT GTGKTFTIAK VIEQVQKPTL
     VLAHNKILAA QLCSEFQQFF PENAVEYFVS YYDYYQPEAY IPTTDTYIEK DALINDEIDK
     LRHSATMALF ERRDVIIVAS VSCIYGLGSP EDYRDLAVSL RVGNQVDRDY ILRRLVDIQY
     ERNDHNFVRN KFRVRGDVVE IFPAGATDRA IRCEWWGDEI ERISEFDPLT GEITGTMTHV
     AIYPASHYVV ADEKREQALR SIEEELEERL KELRAQGKLL EAQRLEQRTR NDLEMIREIG
     FCSGIENYSR HLTGRKPGEP PYTLLDFFPD DWLLVIDESH VTIPQVAAMY NGDRSRKETL
     IEYGFRLPSA ADNRPLKFAE FEERINQVIY VSATPGPYEL ERVPPSLVVE QIVRPTGLLD
     PEVEVRPTKG QIDDLYAEIR ARVKKNQRVL VTTLTKRMAE DLTEYLKELG VKVRYMHSDV
     ETIERMQIVR DLRLGVFDVL VGINLLREGL DIPEVSLVAI LDADKEGFLR AERSLIQTIG
     RAARNAEGKV IMYADRITQS MQKAINETNR RRAIQEAYNR KHGIVPKTIV KPVRDVIQAV
     KPVAEAGPAN ILDTPPHEIP KVVAKLRKEM MQAAKDLDFE RAAEIRDIIF ELEKKKRGA
//
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