ID   Q5NIH0_FRATT            Unreviewed;       337 AA.
AC   Q5NIH0; A0A0G2RPC4;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=LD-carboxypeptidase {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=FTT_0101 {ECO:0000313|EMBL:CAG44734.1};
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416 {ECO:0000313|EMBL:CAG44734.1, ECO:0000313|Proteomes:UP000001174};
RN   [1] {ECO:0000313|EMBL:CAG44734.1, ECO:0000313|Proteomes:UP000001174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 / Schu 4 {ECO:0000313|Proteomes:UP000001174};
RX   PubMed=15640799; DOI=10.1038/ng1499;
RA   Larsson P., Oyston P.C.F., Chain P., Chu M., Duffield M., Fuxelius H.H.,
RA   Garcia E., Halltorp G., Johansson D., Isherwood K., Karp P., Larsson E.,
RA   Lui Y., Michell S., Prior J., Prior R., Sjostedt A., Svensson K.,
RA   Thompson N., Vergez L., Wagg J., Wren B., Lindler L.E., Andersson S.G.,
RA   Forsman M., Titball R.W.;
RT   "The complete genome sequence of Francisella tularensis, the causative
RT   agent of tularemia.";
RL   Nat. Genet. 37:153-159(2005).
CC   -!- SIMILARITY: Belongs to the peptidase S66 family.
CC       {ECO:0000256|ARBA:ARBA00010233}.
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DR   EMBL; AJ749949; CAG44734.1; -; Genomic_DNA.
DR   RefSeq; WP_003019840.1; NZ_CP010290.1.
DR   RefSeq; YP_169172.1; NC_006570.2.
DR   AlphaFoldDB; Q5NIH0; -.
DR   DNASU; 3192163; -.
DR   EnsemblBacteria; CAG44734; CAG44734; FTT_0101.
DR   KEGG; ftu:FTT_0101; -.
DR   PATRIC; fig|177416.18.peg.111; -.
DR   OrthoDB; 9807329at2; -.
DR   Proteomes; UP000001174; 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 {ECO:0000256|ARBA:ARBA00022645};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001174};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..337
FT                   /note="LD-carboxypeptidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5030175913"
FT   DOMAIN          34..154
FT                   /note="LD-carboxypeptidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02016"
FT   DOMAIN          209..322
FT                   /note="LD-carboxypeptidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17676"
FT   ACT_SITE        134
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT   ACT_SITE        239
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT   ACT_SITE        308
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ   SEQUENCE   337 AA;  38399 MW;  22CAD8D4B4066C9D CRC64;
     MLLKNNYLVS IILVVLIMIV TKSFACAATD YNKVALINVS TQYYPNDIKQ AEKALKDTGY
     NTTYKYLDIY PSDFGYSNPD SIRAKILLDA LLDKNIDIIW FLKGGGGAFN LLPYLYDHIN
     ELKKAKPKIL VGFSDVTAIH FFVNNVLGWK SLHGVVAAYN KNAYSSQKIG KIRINDLERI
     PNITEIINNG ISYDKLMPMN KMAYNGIDGS IVGGNMTLIY SYFSTVYQQD ISTKILFLED
     TGISFRQLDR SLHQLLYLPE NKKPEAIIFG QFYPLDPTDD QRLIYKTVIK KFAKTFNRPV
     YYFPFIGHGQ YNKPLLLGVT SNIKCSKETI FCTLKQK
//