CADD_CHLTR
ID CADD_CHLTR Reviewed; 231 AA.
AC O84616;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Probable oxidoreductase CT_610 {ECO:0000305|PubMed:15087448};
DE EC=1.-.-.- {ECO:0000305|PubMed:15087448};
DE AltName: Full=Chlamydia protein associating with death domains {ECO:0000303|PubMed:11805081, ECO:0000303|PubMed:15087448};
DE Short=CADD {ECO:0000303|PubMed:11805081, ECO:0000303|PubMed:15087448};
GN OrderedLocusNames=CT_610;
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., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
RN [2]
RP FUNCTION, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=11805081; DOI=10.1074/jbc.c100693200;
RA Stenner-Liewen F., Liewen H., Zapata J.M., Pawlowski K., Godzik A.,
RA Reed J.C.;
RT "CADD, a Chlamydia protein that interacts with death receptors.";
RL J. Biol. Chem. 277:9633-9636(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH IRON, SUBUNIT,
RP FUNCTION, COFACTOR, IRON-BINDING SITES, AND MUTAGENESIS OF GLU-81; HIS-88;
RP TYR-170 AND HIS-174.
RX PubMed=15087448; DOI=10.1074/jbc.m401268200;
RA Schwarzenbacher R., Stenner-Liewen F., Liewen H., Robinson H., Yuan H.,
RA Bossy-Wetzel E., Reed J.C., Liddington R.C.;
RT "Structure of the Chlamydia protein CADD reveals a redox enzyme that
RT modulates host cell apoptosis.";
RL J. Biol. Chem. 279:29320-29324(2004).
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
CC (PubMed:11805081, PubMed:15087448). Probably functions as an
CC oxidoreductase (PubMed:15087448). {ECO:0000269|PubMed:11805081,
CC ECO:0000269|PubMed:15087448}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000305|PubMed:15087448};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000269|PubMed:15087448};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15087448}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11805081}. Host
CC cytoplasm {ECO:0000269|PubMed:11805081}. Note=Secreted into the host
CC cytoplasm, where it co-localizes with Fas in the proximity of the
CC inclusion body. {ECO:0000269|PubMed:11805081}.
CC -!- DEVELOPMENTAL STAGE: Expressed late in the infectious cycle.
CC {ECO:0000269|PubMed:11805081}.
CC -!- SIMILARITY: Belongs to the CADD family. {ECO:0000305}.
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DR EMBL; AE001273; AAC68213.1; -; Genomic_DNA.
DR PIR; F71493; F71493.
DR RefSeq; NP_220127.1; NC_000117.1.
DR RefSeq; WP_009871978.1; NC_000117.1.
DR PDB; 1RCW; X-ray; 2.50 A; A/B/C=1-231.
DR PDBsum; 1RCW; -.
DR AlphaFoldDB; O84616; -.
DR SMR; O84616; -.
DR STRING; 813.O172_03335; -.
DR EnsemblBacteria; AAC68213; AAC68213; CT_610.
DR GeneID; 884390; -.
DR KEGG; ctr:CT_610; -.
DR PATRIC; fig|272561.5.peg.667; -.
DR HOGENOM; CLU_088144_0_0_0; -.
DR InParanoid; O84616; -.
DR OMA; ICEIGAQ; -.
DR BioCyc; MetaCyc:CT_610-MON; -.
DR EvolutionaryTrace; O84616; -.
DR Proteomes; UP000000431; 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 1: Evidence at protein level;
KW 3D-structure; Host cytoplasm; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; Secreted; Toxin; Virulence.
FT CHAIN 1..231
FT /note="Probable oxidoreductase CT_610"
FT /id="PRO_0000219994"
FT BINDING 81
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15087448"
FT BINDING 81
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15087448"
FT BINDING 88
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15087448"
FT BINDING 142
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15087448"
FT BINDING 174
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15087448"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15087448"
FT BINDING 181
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15087448"
FT MUTAGEN 81
FT /note="E->A: Apoptotic activity is decreased by more than
FT 60%, but the mutant still binds to death receptors; when
FT associated with A-88; F-170 and A-174."
FT /evidence="ECO:0000269|PubMed:15087448"
FT MUTAGEN 88
FT /note="H->A: Apoptotic activity is decreased by more than
FT 60%, but the mutant still binds to death receptors; when
FT associated with A-81; F-170 and A-174."
FT /evidence="ECO:0000269|PubMed:15087448"
FT MUTAGEN 170
FT /note="Y->F: Apoptotic activity is decreased by 15%, but
FT the mutant still binds to death receptors. Apoptotic
FT activity is decreased by more than 60%, but the mutant
FT still binds to death receptors; when associated with A-81;
FT A-88 and A-174."
FT /evidence="ECO:0000269|PubMed:15087448"
FT MUTAGEN 174
FT /note="H->A: Apoptotic activity is decreased by more than
FT 60%, but the mutant still binds to death receptors; when
FT associated with A-81; A-88 and F-170."
FT /evidence="ECO:0000269|PubMed:15087448"
FT HELIX 8..18
FT /evidence="ECO:0007829|PDB:1RCW"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:1RCW"
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:1RCW"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:1RCW"
FT HELIX 48..62
FT /evidence="ECO:0007829|PDB:1RCW"
FT HELIX 68..82
FT /evidence="ECO:0007829|PDB:1RCW"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:1RCW"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:1RCW"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:1RCW"
FT HELIX 113..126
FT /evidence="ECO:0007829|PDB:1RCW"
FT HELIX 131..142
FT /evidence="ECO:0007829|PDB:1RCW"
FT HELIX 145..159
FT /evidence="ECO:0007829|PDB:1RCW"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:1RCW"
FT HELIX 169..192
FT /evidence="ECO:0007829|PDB:1RCW"
FT HELIX 197..216
FT /evidence="ECO:0007829|PDB:1RCW"
SQ SEQUENCE 231 AA; 26734 MW; 8AED7D2592A7FF24 CRC64;
MMEVFMNFLD QLDLIIQNKH MLEHTFYVKW SKGELTKEQL QAYAKDYYLH IKAFPKYLSA
IHSRCDDLEA RKLLLDNLMD EENGYPNHID LWKQFVFALG VTPEELEAHE PSEAAKAKVA
TFMRWCTGDS LAAGVAALYS YESQIPRIAR EKIRGLTEYF GFSNPEDYAY FTEHEEADVR
HAREEKALIE MLLKDDADKV LEASQEVTQS LYGFLDSFLD PGTCCSCHQS Y
