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Database: UniProt
Entry: O84590
LinkDB: O84590
Original site: O84590 
ID   UVRB_CHLTR              Reviewed;         668 AA.
AC   O84590;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-OCT-2019, entry version 117.
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=CT_586;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V.,
RA   Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans:
RT   Chlamydia trachomatis.";
RL   Science 282:754-759(1998).
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; AE001273; AAC68188.1; -; Genomic_DNA.
DR   PIR; C71496; C71496.
DR   RefSeq; NP_220101.1; NC_000117.1.
DR   RefSeq; WP_010725260.1; NC_000117.1.
DR   SMR; O84590; -.
DR   EnsemblBacteria; AAC68188; AAC68188; CT_586.
DR   GeneID; 884370; -.
DR   KEGG; ctr:CT_586; -.
DR   PATRIC; fig|272561.5.peg.638; -.
DR   eggNOG; ENOG4105CCW; Bacteria.
DR   eggNOG; COG0556; LUCA.
DR   InParanoid; O84590; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   BioCyc; CTRA272561:G1G18-622-MONOMER; -.
DR   Proteomes; UP000000431; 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    668       UvrABC system protein B.
FT                                /FTId=PRO_0000138387.
FT   DOMAIN       31    416       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      433    596       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      621    656       UVR. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   NP_BIND      44     51       ATP. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   MOTIF        97    120       Beta-hairpin.
SQ   SEQUENCE   668 AA;  75867 MW;  FBF80B06FA34E281 CRC64;
     MGGGVLKQQF VLHAPFLPCG DQPEAIRRLS QGITDGVPAQ VLLGTTGSGK TFTMANVIAN
     VNVPTLVLAH NKTLAAQLYQ EFKAFFPENA VEYFISYYDY YQPEAYIARS DTYIEKSLLI
     NDEIDKLRLS ATRSILERRD TLIVSSISCI YGIGSPDNYS SMALTLEVGK EYPRSQLSSQ
     LVRMHYQASS TPQRSAFRER GSVIDIFLAY ESDLAVRLEF MNDTLISIEY VDPLTMIPSH
     TTSSITLYPG SHYVTPEAVR EQAIRTIREE LEQRMLFFEG RPVEQERLFQ RTTHDIEMIK
     EIGFCKGIEN YSRHFTGAAP GEPPTCLLDY FPDDFLLIID ESHQTLPQLR AMYRGDQSRK
     QSLVEYGFRL PSAFDNRPLT YEEARRYFHR VIYVSATPGD LEIQESRGHI IEQIIRPTGI
     PDPLPEIRPA KGQIDDLLEE IRQRLRKDQE KILVISVTKK LAEDIAAFLA ELGIAATYLH
     SGIETAERTQ ILTDLRLGNI DVLIGVNLLR EGIDLPEVSL VAILDADKEG FLRSSASLIQ
     FCGRAARNIH GKVICYADRI TPSMDHMLKE TERRRKIQLD YNQQHKITPQ PIIKPILANP
     ITKEAGQEET RLKMQSSKEL EASIKTYEEA MYQAAQEFQF DEAAKYRDLM NAAKKQLLFQ
     KGEEENGD
//
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