ID   AAXB_CHLCV              Reviewed;         195 AA.
AC   Q822F3;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Pyruvoyl-dependent arginine decarboxylase AaxB;
DE            Short=PvlArgDC;
DE            EC=4.1.1.19;
DE   AltName: Full=Biodegradative arginine decarboxylase;
DE   Contains:
DE     RecName: Full=Pyruvoyl-dependent arginine decarboxylase subunit beta;
DE   Contains:
DE     RecName: Full=Pyruvoyl-dependent arginine decarboxylase subunit alpha;
GN   Name=aaxB; OrderedLocusNames=CCA_00730;
OS   Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC)
OS   (Chlamydophila caviae).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=227941;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-813 / DSM 19441 / 03DC25 / GPIC;
RX   PubMed=12682364; DOI=10.1093/nar/gkg321;
RA   Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T.,
RA   Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A.,
RA   Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O.,
RA   Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G., Bavoil P.M.,
RA   Fraser C.M.;
RT   "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC):
RT   examining the role of niche-specific genes in the evolution of the
RT   Chlamydiaceae.";
RL   Nucleic Acids Res. 31:2134-2147(2003).
CC   -!- FUNCTION: Part of the AaxABC system, catalyzes the decarboxylation of
CC       L-arginine. The arginine uptake by the bacterium in the macrophage may
CC       be a virulence factor against the host innate immune response (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-arginine = agmatine + CO2; Xref=Rhea:RHEA:17641,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:58145; EC=4.1.1.19;
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000250};
CC       Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Trimer of an alpha-beta dimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the pyruvoyl-dependent arginine decarboxylase
CC       family. {ECO:0000305}.
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DR   EMBL; AE015925; AAP05471.1; -; Genomic_DNA.
DR   RefSeq; WP_011006685.1; NC_003361.3.
DR   AlphaFoldDB; Q822F3; -.
DR   SMR; Q822F3; -.
DR   STRING; 227941.CCA_00730; -.
DR   EnsemblBacteria; AAP05471; AAP05471; CCA_00730.
DR   KEGG; cca:CCA_00730; -.
DR   eggNOG; COG1945; Bacteria.
DR   HOGENOM; CLU_1313366_0_0_0; -.
DR   OMA; KKKFGFC; -.
DR   OrthoDB; 1265324at2; -.
DR   Proteomes; UP000002193; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR   Gene3D; 3.50.20.10; -; 1.
DR   InterPro; IPR016104; Pyr-dep_his/arg-deCO2ase.
DR   InterPro; IPR016105; Pyr-dep_his/arg-deCO2ase_sand.
DR   InterPro; IPR002724; Pyruvoyl-dep_arg_deCO2ase.
DR   PANTHER; PTHR40438; PTHR40438; 1.
DR   Pfam; PF01862; PvlArgDC; 1.
DR   SFLD; SFLDG01170; Pyruvoyl-dependent_arginine_de; 1.
DR   SUPFAM; SSF56271; SSF56271; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Decarboxylase; Lyase; Pyruvate; Virulence.
FT   CHAIN           1..52
FT                   /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT                   beta"
FT                   /id="PRO_0000364039"
FT   CHAIN           53..195
FT                   /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT                   alpha"
FT                   /id="PRO_0000364040"
FT   SITE            52..53
FT                   /note="Cleavage (non-hydrolytic)"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         53
FT                   /note="Pyruvic acid (Ser)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   195 AA;  21775 MW;  BD1D5CDC01D351C5 CRC64;
     MPYGTRYPTL AFHTGGIGES DDGMPPQPFE TFCYDSALLQ AKIENFNIVP YTSVLPKELF
     GNIVPVDQCI KFFKHGAVLE VIMAGRGAST SDGTHAIATG VGICWGQDKN GELIGGWAAE
     YVEFFPTWIN DEIAESHAKM WLKKSLQHEL DLRSVVKHSE FQYFHNYINI KQKYGFSLTA
     LGFLNFENAD PATIK