ID G9EPN8_9GAMM Unreviewed; 300 AA.
AC G9EPN8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=LD-carboxypeptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=LDG_7205 {ECO:0000313|EMBL:EHL30776.1};
OS Legionella drancourtii LLAP12.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=658187 {ECO:0000313|EMBL:EHL30776.1, ECO:0000313|Proteomes:UP000002770};
RN [1] {ECO:0000313|EMBL:EHL30776.1, ECO:0000313|Proteomes:UP000002770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LLAP12 {ECO:0000313|EMBL:EHL30776.1,
RC ECO:0000313|Proteomes:UP000002770};
RX PubMed=22047552; DOI=10.1186/1471-2164-12-542;
RA Gimenez G., Bertelli C., Moliner C., Robert C., Raoult D., Fournier P.E.,
RA Greub G.;
RT "Insight into cross-talk between intra-amoebal pathogens.";
RL BMC Genomics 12:542-542(2011).
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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DR EMBL; JH413824; EHL30776.1; -; Genomic_DNA.
DR RefSeq; WP_006871122.1; NZ_JH413824.1.
DR AlphaFoldDB; G9EPN8; -.
DR STRING; 658187.LDG_7205; -.
DR eggNOG; COG1619; Bacteria.
DR HOGENOM; CLU_034346_3_1_6; -.
DR InParanoid; G9EPN8; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000002770; Unassembled WGS sequence.
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:UP000002770};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 13..129
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 176..288
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 109
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 205
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 273
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 300 AA; 32652 MW; CB72458DF6A3FC6A CRC64;
MYSLPVLKPG DFVELIAPAS RCSEHELLGI KQLCEAWQLN CIVNEDIFGD DLLCANSDAA
RFNHLKNALQ NPQTKAVICV RGGYGAMRLI PQLAKIQPPV TPKVFVGMSD TTCLHLYLQQ
QWGWATIHGA ASPDKFSAQS IAALKTLLFV EAEAVNFSRL KPLNQAAKEQ GVLIAPVTGG
NLTLIQAGIG TNWQLNARDK FVLLEEVNER GYRVDRMLEH LQQAHILDGA TAILFGDFLG
GNEPNDTSLI PAVLQRFADA CAIPVVQIDG IGHGVTNFPI PCATKARLEL GNELGLTCFR
//
