ID   Y402_RICPR              Reviewed;         317 AA.
AC   Q9ZDC9;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Putative carboxypeptidase RP402;
DE            EC=3.4.16.-;
GN   OrderedLocusNames=RP402;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
CC   -!- SIMILARITY: Belongs to the peptidase S66 family. {ECO:0000305}.
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DR   EMBL; AJ235271; CAA14859.1; -; Genomic_DNA.
DR   PIR; A71698; A71698.
DR   RefSeq; NP_220783.1; NC_000963.1.
DR   RefSeq; WP_004599449.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZDC9; -.
DR   SMR; Q9ZDC9; -.
DR   STRING; 272947.RP402; -.
DR   EnsemblBacteria; CAA14859; CAA14859; CAA14859.
DR   GeneID; 57569527; -.
DR   KEGG; rpr:RP402; -.
DR   PATRIC; fig|272947.5.peg.415; -.
DR   eggNOG; COG1619; Bacteria.
DR   HOGENOM; CLU_034346_3_0_5; -.
DR   OMA; GFIFGQC; -.
DR   Proteomes; UP000002480; 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   Gene3D; 3.40.50.10740; -; 1.
DR   Gene3D; 3.50.30.60; -; 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; PTHR30237; 1.
DR   Pfam; PF02016; Peptidase_S66; 1.
DR   Pfam; PF17676; Peptidase_S66C; 1.
DR   PIRSF; PIRSF028757; LD-carboxypeptidase; 1.
DR   SUPFAM; SSF141986; SSF141986; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Hydrolase; Protease; Reference proteome; Serine protease.
FT   CHAIN           1..317
FT                   /note="Putative carboxypeptidase RP402"
FT                   /id="PRO_0000172844"
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   317 AA;  35493 MW;  7A3B5DE05DD527AC CRC64;
     MVLKNLSLLI ILFFSTSVFS VSNNLINIPI TVVATATGAD SKTLSDLKNI NGLNLQIPAK
     CFTKGKLPFL ASSDEVRFNC LRDALFDKSD NVVWSLRGGY GSARIIPDLL KLSKPNKEKF
     FIGYSDITAL HLFLSQEWGW RTIHGSNIAD LLKTEKDQGN FTKLGEILKG KVKQVTIDNL
     IPLNDIAKSS DLVKGNLTGG NLTMVQTSIG TRWQIKTKGK ILFLEDTNVA PFRLDRELLH
     LKQSMLLEGV KAIIFGSFGK DLDATMLVLR NFAYSLNIPV FKTNRFGHER INDPIIYNTN
     SKIIMSKHKE FKLIMEL