ID   Y688_TREPA              Reviewed;         337 AA.
AC   P96129;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Putative carboxypeptidase TP_0688;
DE            EC=3.4.16.-;
GN   OrderedLocusNames=TP_0688;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Nichols;
RA   Stamm L.V., Barnes N.Y.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
CC   -!- SIMILARITY: Belongs to the peptidase S66 family. {ECO:0000305}.
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DR   EMBL; U70661; AAB38706.1; -; Genomic_DNA.
DR   EMBL; AE000520; AAC65657.1; -; Genomic_DNA.
DR   PIR; E71292; E71292.
DR   RefSeq; WP_010882133.1; NC_021490.2.
DR   AlphaFoldDB; P96129; -.
DR   SMR; P96129; -.
DR   IntAct; P96129; 12.
DR   STRING; 243276.TPANIC_0688; -.
DR   MEROPS; S66.003; -.
DR   EnsemblBacteria; AAC65657; AAC65657; TP_0688.
DR   GeneID; 57879213; -.
DR   KEGG; tpa:TP_0688; -.
DR   eggNOG; COG1619; Bacteria.
DR   HOGENOM; CLU_034346_1_1_12; -.
DR   OMA; MLTQWRL; -.
DR   OrthoDB; 952832at2; -.
DR   Proteomes; UP000000811; 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..337
FT                   /note="Putative carboxypeptidase TP_0688"
FT                   /id="PRO_0000172847"
FT   ACT_SITE        118
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        234
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        302
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   337 AA;  37958 MW;  959513EDCECE4993 CRC64;
     MQDEGVDMKK LLLRSSDEVR VIAPSCSMRK IDSSVIERAQ ERFRCLGLNV AFGDHVYDED
     FLGSASVDKR VADLHAAFAD KKVKLILTAI GGFNSNQLLQ HIDYALLKKN PKLLCGFSDV
     TALLNAIHAK TGMPVFYGPH FSTFGMEKGI EFTIECFKNT FFYGRCDILA SETWSDDMWF
     KDQEHRQFIT NPGYEIIHRG DMVGMGVGGN ISTFNLLAGT EYEPSLKKSI LFIEDTSRMS
     ITDFDRHLEA LTQRDDFCTV RGILIGRFQK DSGIDMDMLR KIISRKKALD AIPLFANVDF
     GHTTPHCILP IGGMIRVNVD RKCITVQLHS SVEQLPE