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
//