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Database: UniProt
Entry: B9K844
LinkDB: B9K844
Original site: B9K844 
ID   UVRB_THENN              Reviewed;         664 AA.
AC   B9K844;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   11-DEC-2019, entry version 66.
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=CTN_0951;
OS   Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NS-E).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=309803;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49049 / DSM 4359 / NS-E;
RA   Lim S.K., Kim J.S., Cha S.H., Park B.C., Lee D.S., Tae H.S., Kim S.-J.,
RA   Kim J.J., Park K.J., Lee S.Y.;
RT   "The genome sequence of the hyperthermophilic bacterium Thermotoga
RT   neapolitana.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; CP000916; ACM23127.1; -; Genomic_DNA.
DR   RefSeq; WP_015919444.1; NC_011978.1.
DR   SMR; B9K844; -.
DR   STRING; 309803.CTN_0951; -.
DR   EnsemblBacteria; ACM23127; ACM23127; CTN_0951.
DR   KEGG; tna:CTN_0951; -.
DR   eggNOG; ENOG4105CCW; Bacteria.
DR   eggNOG; COG0556; LUCA.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   BioCyc; TNEA309803:G1GAR-946-MONOMER; -.
DR   Proteomes; UP000000445; 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; Cytoplasm; DNA damage; DNA excision; DNA repair;
KW   Excision nuclease; Helicase; Hydrolase; Nucleotide-binding; SOS response.
FT   CHAIN           1..664
FT                   /note="UvrABC system protein B"
FT                   /id="PRO_1000200561"
FT   DOMAIN          23..180
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   DOMAIN          426..588
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   DOMAIN          622..657
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   NP_BIND         36..43
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   MOTIF           89..112
FT                   /note="Beta-hairpin"
SQ   SEQUENCE   664 AA;  76581 MW;  E57E674C5F621523 CRC64;
     MFKLVSEFEP TGDQPQAIEK LVEGLNRGMR FQTLLGVTGS GKTFTMANVI ARVNRPALVI
     SPNKTLAAQL YQEFKTFFPE NRVEFFISYY DYYQPEAYIP TKDLYIEKNA DINDVIVRMR
     MSTLKSVRTR RDVIVVASVS CIYATGDPND FDRMNIKLSV GERLDVFELA EKLAKIGYQR
     TEDVSLSGCF RIRGDTLEIY PTYQDEGIRV EFFGDEIDAI SLIDRFNRTT LERLDKVIIY
     PAVEFVTTEE KLRRAIESIK EELRERLAEL KKQGKVLEYE RLKQRTLNDI ELLETMGYCP
     GIENYSRHFD GRKPGEPPYT LLDYFDDDFV VFIDESHITV PQLRAMYNGD RSRKKNLVEY
     GFRLPSAYDN RPLTFEEFLK KVGQIVFVSA TPGDFELSVS EQVVEQIIRP TGLVDPEVEV
     RPTRGQVDDL INEIVKVKQR GERALVTVLT KKTAELLSEH LTELGIKSLY LHSELDAIER
     VEVLKKLRRG DVDVVVGVNL LREGLDLPEV SLVAIMDADT EGFLRSETTL IQIIGRTARN
     VNGKVIMYAD RITNAMKRAI EETNRRRRIQ LEYNKKHGIT PRSIVKPLEI EVFEQFMVKE
     EPAEYGDTIK NIFSMKESLS LEEYVALLEE EMYRAASELR YEDAAALRDE LFRVKETLKK
     KKGR
//
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