CADD_CHLMU
ID CADD_CHLMU Reviewed; 236 AA.
AC Q9PJC9;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Probable oxidoreductase TC_0900;
DE EC=1.-.-.-;
DE AltName: Full=Chlamydia protein associating with death domains;
DE Short=CADD;
GN OrderedLocusNames=TC_0900;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
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).
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}.
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DR EMBL; AE002160; AAF39693.1; -; Genomic_DNA.
DR PIR; D81652; D81652.
DR AlphaFoldDB; Q9PJC9; -.
DR SMR; Q9PJC9; -.
DR STRING; 243161.TC_0900; -.
DR PRIDE; Q9PJC9; -.
DR EnsemblBacteria; AAF39693; AAF39693; TC_0900.
DR KEGG; cmu:TC_0900; -.
DR eggNOG; COG5424; Bacteria.
DR HOGENOM; CLU_088144_0_0_0; -.
DR OMA; ICEIGAQ; -.
DR Proteomes; UP000000800; 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..236
FT /note="Probable oxidoreductase TC_0900"
FT /id="PRO_0000219992"
FT BINDING 87
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O84616"
FT BINDING 87
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O84616"
FT BINDING 94
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O84616"
FT BINDING 148
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O84616"
FT BINDING 180
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O84616"
FT BINDING 184
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O84616"
FT BINDING 187
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O84616"
SQ SEQUENCE 236 AA; 27166 MW; 32A4A9427E1C3231 CRC64;
MESRKGIKEV SMNFLDQLDA IIQNKHMLEH PFYMKWSKGE LTKEQLQAYA KDYYLHIKAF
PKYLSAIHSR CDDLEARKLL LDNLMDEENG YPNHIDLWKQ FVFALGVSSE ELEAHEPSEA
AKAKVATFMR WCTGDSLAAG VAALYSYESQ IPCVAKEKIR GLIEYFGFSN PEDYAYFTEH
EEADVRHARE EKALIEMLSR DDSDKVLEAS REVTQSLYGF LDSFLEPATC CHCHKA
