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Database: UniProt
Entry: Q9Z7A5
LinkDB: Q9Z7A5
Original site: Q9Z7A5 
ID   UVRB_CHLPN              Reviewed;         657 AA.
AC   Q9Z7A5; Q9JQE7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   31-JUL-2019, entry version 131.
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=CPn_0801, CP_1070, CpB0830;
OS   Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=83558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CWL029;
RX   PubMed=10192388; DOI=10.1038/7716;
RA   Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA   Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT   "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL   Nat. Genet. 21:385-389(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR39;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F.,
RA   White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J.,
RA   Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C.,
RA   Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F.,
RA   McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia
RT   pneumoniae AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J138;
RX   PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA   Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA   Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT   "Comparison of whole genome sequences of Chlamydia pneumoniae J138
RT   from Japan and CWL029 from USA.";
RL   Nucleic Acids Res. 28:2311-2314(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW-183;
RA   Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA   Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT   "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT   other Chlamydia strains based on whole genome sequence analysis.";
RL   Submitted (MAY-2002) 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
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; AE001363; AAD18939.1; -; Genomic_DNA.
DR   EMBL; AE002161; AAF38842.1; -; Genomic_DNA.
DR   EMBL; BA000008; BAA99009.1; -; Genomic_DNA.
DR   EMBL; AE009440; AAP98759.1; -; Genomic_DNA.
DR   PIR; B72034; B72034.
DR   PIR; G86590; G86590.
DR   RefSeq; NP_224996.1; NC_000922.1.
DR   RefSeq; WP_010883438.1; NZ_LN847257.1.
DR   SMR; Q9Z7A5; -.
DR   STRING; 115713.CPn_0801; -.
DR   EnsemblBacteria; AAD18939; AAD18939; CPn_0801.
DR   EnsemblBacteria; AAF38842; AAF38842; CP_1070.
DR   EnsemblBacteria; AAP98759; AAP98759; CpB0830.
DR   EnsemblBacteria; BAA99009; BAA99009; BAA99009.
DR   GeneID; 894666; -.
DR   KEGG; cpa:CP_1070; -.
DR   KEGG; cpj:uvrB; -.
DR   KEGG; cpn:CPn0801; -.
DR   KEGG; cpt:CpB0830; -.
DR   PATRIC; fig|115713.3.peg.880; -.
DR   eggNOG; ENOG4105CCW; Bacteria.
DR   eggNOG; COG0556; LUCA.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OrthoDB; 95696at2; -.
DR   BioCyc; CPNE115713:G1G19-809-MONOMER; -.
DR   Proteomes; UP000000583; Chromosome.
DR   Proteomes; UP000000801; 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; SOS response.
FT   CHAIN         1    657       UvrABC system protein B.
FT                                /FTId=PRO_0000138386.
FT   DOMAIN       24    409       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      426    589       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      617    652       UVR. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   NP_BIND      37     44       ATP. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   MOTIF        90    113       Beta-hairpin.
SQ   SEQUENCE   657 AA;  74830 MW;  177267D65748492E CRC64;
     MTFQLHAPFA PCGDQPEAIA RLSAGVRNQV KSQVLLGTTG SGKTFTIANV VANVNLPTLV
     LAHNKTLAAQ LYQEFREFFP NNAVEYFISY YDYYQPEAYI ARSDTYIEKS LLINDEIDKL
     RLSATRSILE RRDTLIVSSV SCIYGIGSPE NYTSMALVLE VGKEYPRNIL TAQLVKMHYQ
     ASPIPQRSAF RERGSVIDIF PAYESELALR LEFLNDTLTS IEYSDPLTMI PKESVPSATL
     YPGSHYVIPE AIREQAIRTI QEELEERMAF FDDRPIEKDR IFHRTTHDIE MIKEIGFCKG
     IENYSRHFTG APPGAPPTCL LDYFPEDFLL IIDESHQTLP QIRAMYRGDQ SRKQSLVEYG
     FRLPSAFDNR PLTYEEAQKY FRKVIYVSAT PGDTEVQESS GHIVQQIIRP TGIPDPMPEI
     RPATGQVDDL LEEIRLRLSQ KHEKILVISI TKKLAEDMAG FLSELEIPAA YLHSGIETAE
     RTQILTDLRS GVIDVLIGVN LLREGLDLPE VSLVAILDAD KEGFLRSTSS LIQFCGRAAR
     NINGKVIFYA DQKTRSIEET LRETERRRQI QLDYNKEHNI VPKPIIKAIF ANPILQTSKD
     SESPKESQRP LSKEDLEEQI KKYEALMQRA AKEFRFNEAA KYRDAMQACK EQLLYLF
//
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