ID   Y549_RICCN              Reviewed;         315 AA.
AC   Q92I71;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2002, sequence version 2.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Putative carboxypeptidase RC0549;
DE            EC=3.4.16.-;
GN   OrderedLocusNames=RC0549;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
CC   -!- SIMILARITY: Belongs to the peptidase S66 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL03087.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE006914; AAL03087.1; ALT_INIT; Genomic_DNA.
DR   PIR; E97768; E97768.
DR   RefSeq; WP_041471720.1; NC_003103.1.
DR   AlphaFoldDB; Q92I71; -.
DR   SMR; Q92I71; -.
DR   GeneID; 927661; -.
DR   KEGG; rco:RC0549; -.
DR   PATRIC; fig|272944.4.peg.628; -.
DR   HOGENOM; CLU_034346_3_0_5; -.
DR   Proteomes; UP000000816; Chromosome.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07025; Peptidase_S66; 1.
DR   Gene3D; 3.40.50.10740; Class I glutamine amidotransferase-like; 1.
DR   Gene3D; 3.50.30.60; LD-carboxypeptidase A C-terminal domain-like; 1.
DR   InterPro; IPR027461; Carboxypeptidase_A_C_sf.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR027478; LdcA_N.
DR   InterPro; IPR040449; Peptidase_S66_N.
DR   InterPro; IPR040921; Peptidase_S66C.
DR   InterPro; IPR003507; S66_fam.
DR   PANTHER; PTHR30237; MURAMOYLTETRAPEPTIDE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR30237:SF2; MUREIN TETRAPEPTIDE CARBOXYPEPTIDASE; 1.
DR   Pfam; PF02016; Peptidase_S66; 1.
DR   Pfam; PF17676; Peptidase_S66C; 1.
DR   PIRSF; PIRSF028757; LD-carboxypeptidase; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF141986; LD-carboxypeptidase A C-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Hydrolase; Protease; Serine protease.
FT   CHAIN           1..315
FT                   /note="Putative carboxypeptidase RC0549"
FT                   /id="PRO_0000172843"
FT   ACT_SITE        125
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        225
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        288
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   315 AA;  34928 MW;  8C651913F808D947 CRC64;
     MILKNISLLI ILFFSISTFS AGHSLKNISI TVVAPATGAD NKTLSDLKNI NGLNLQISSK
     CFAKGKLPFL ASSDEVRFNC LRDALFDESD NIVWSLRGGY GSARIIPDLL KLSKPNKEKF
     FIGYSDITAL HLFLSQEWGW KTIHGSNIAD LLKPEQDQGN FTKLAEILKG KVKQVTIDNL
     VPLNDIAKSS DLVNGKLTGG NLTMVQTSIG TSWQIKTKGK ILFLEDVNVV PFRLDRELLH
     LKQAGLLEDV KAIIFGSFGK DLDATMLVLR NFADSLDIPV FKTNRFGHEK INDPIIYNTN
     SKIIKSKEFK LVMGV
//