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CADD_CHLPN
ID   CADD_CHLPN              Reviewed;         224 AA.
AC   Q9Z7E5;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Probable oxidoreductase CPn_0761/CP_1111/CPj0761/CpB0789;
DE            EC=1.-.-.-;
DE   AltName: Full=Chlamydia protein associating with death domains;
DE            Short=CADD;
GN   OrderedLocusNames=CPn_0761, CP_1111, CPj0761, CpB0789;
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., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   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 from
RT   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: Chlamydia specific toxin that associates with death domains
CC       of tumor necrosis factor family (TNF) receptors and induces apoptosis
CC       in mammalian cell lines through a Caspase-dependent mechanism. Probably
CC       functions as an oxidoreductase. {ECO:0000250|UniProtKB:O84616}.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:O84616};
CC       Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:O84616};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O84616}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O84616}. Host
CC       cytoplasm {ECO:0000250|UniProtKB:O84616}. Note=Secreted into the host
CC       cytoplasm, where it co-localizes with Fas in the proximity of the
CC       inclusion body. {ECO:0000250|UniProtKB:O84616}.
CC   -!- SIMILARITY: Belongs to the CADD family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP98718.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE001363; AAD18899.1; -; Genomic_DNA.
DR   EMBL; AE002161; AAF38878.1; -; Genomic_DNA.
DR   EMBL; BA000008; BAA98969.1; -; Genomic_DNA.
DR   EMBL; AE009440; AAP98718.1; ALT_INIT; Genomic_DNA.
DR   PIR; B72040; B72040.
DR   PIR; G86585; G86585.
DR   RefSeq; NP_224956.1; NC_000922.1.
DR   RefSeq; WP_010883398.1; NZ_LN847257.1.
DR   AlphaFoldDB; Q9Z7E5; -.
DR   SMR; Q9Z7E5; -.
DR   STRING; 115711.CP_1111; -.
DR   PRIDE; Q9Z7E5; -.
DR   EnsemblBacteria; AAD18899; AAD18899; CPn_0761.
DR   EnsemblBacteria; AAF38878; AAF38878; CP_1111.
DR   GeneID; 45050816; -.
DR   KEGG; cpa:CP_1111; -.
DR   KEGG; cpj:CPj0761; -.
DR   KEGG; cpn:CPn_0761; -.
DR   KEGG; cpt:CpB0789; -.
DR   PATRIC; fig|115713.3.peg.838; -.
DR   eggNOG; COG5424; Bacteria.
DR   HOGENOM; CLU_088144_0_0_0; -.
DR   OrthoDB; 1571811at2; -.
DR   Proteomes; UP000000583; Chromosome.
DR   Proteomes; UP000000801; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:UniProt.
DR   GO; GO:0034641; P:cellular nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0046483; P:heterocycle metabolic process; IEA:UniProt.
DR   GO; GO:1901360; P:organic cyclic compound metabolic process; IEA:UniProt.
DR   GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR   Gene3D; 1.20.910.10; -; 1.
DR   InterPro; IPR027572; Fol-rel_CADD.
DR   InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR   InterPro; IPR039068; PqqC-like.
DR   InterPro; IPR004305; Thiaminase-2/PQQC.
DR   PANTHER; PTHR40279; PTHR40279; 1.
DR   Pfam; PF03070; TENA_THI-4; 1.
DR   SUPFAM; SSF48613; SSF48613; 1.
DR   TIGRFAMs; TIGR04305; fol_rel_CADD; 1.
PE   3: Inferred from homology;
KW   Host cytoplasm; Iron; Metal-binding; Oxidoreductase; Secreted; Toxin;
KW   Virulence.
FT   CHAIN           1..224
FT                   /note="Probable oxidoreductase
FT                   CPn_0761/CP_1111/CPj0761/CpB0789"
FT                   /id="PRO_0000219993"
FT   BINDING         77
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:O84616"
FT   BINDING         77
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O84616"
FT   BINDING         84
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:O84616"
FT   BINDING         138
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O84616"
FT   BINDING         169
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:O84616"
FT   BINDING         173
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O84616"
FT   BINDING         176
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O84616"
SQ   SEQUENCE   224 AA;  25971 MW;  063D7DECCBABF8D0 CRC64;
     MTSWIELLDK QIEDQHMLKH EFYQRWSEGK LEKQQLQAYA KDYYLHIKAF PCYLSALHAR
     CDDLQIRRQI LENLMDEEAG NPNHIDLWRQ FALSLGVSEE ELANHEFSQA AQDMVATFRR
     LCDMPQLAVG LGALYTYEIQ IPQVCVEKIR GLKEYFGVSA RGYAYFTVHQ EADIKHASEE
     KEMLQTLVGR ENPDAVLQGS QEVLDTLWNF LSSFINSTEP CSCK
 
 
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