ID A0A0W0R3V8_9GAMM Unreviewed; 298 AA.
AC A0A0W0R3V8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:KTC65761.1};
GN ORFNames=Lade_0419 {ECO:0000313|EMBL:KTC65761.1};
OS Legionella adelaidensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45056 {ECO:0000313|EMBL:KTC65761.1, ECO:0000313|Proteomes:UP000054859};
RN [1] {ECO:0000313|EMBL:KTC65761.1, ECO:0000313|Proteomes:UP000054859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1762-AUS-E {ECO:0000313|EMBL:KTC65761.1,
RC ECO:0000313|Proteomes:UP000054859};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Identification of large and diverse effector repertoires of 38 Legionella
RT species.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTC65761.1}.
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DR EMBL; LNKA01000001; KTC65761.1; -; Genomic_DNA.
DR RefSeq; WP_058461496.1; NZ_LNKA01000001.1.
DR AlphaFoldDB; A0A0W0R3V8; -.
DR STRING; 45056.Lade_0419; -.
DR PATRIC; fig|45056.6.peg.434; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000054859; 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 ECO:0000313|EMBL:KTC65761.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000054859};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 13..128
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 174..286
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 108
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 271
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 298 AA; 33265 MW; C44290F4EB35D400 CRC64;
MFTIPVLKPN DQVELIAPAS RCSEERLQLT QQMLTSWGLQ CIVNPSLFGS DLLCANSDFM
RSQLLIEALT NPDNKAIICL RGGYGSMRLI PELHKIKQME FKLFIGMSDI TALNLFFMQK
WKWPVLHGGI APDYYTLESL ARYKSYLFGE INQLEFQGSA LNQHALKNNT ISSTITGGNL
CLLQASIGTT WEIDTQNKFV FIEEVGERGY RIDRMLEHLT QTGIFSKAQG IILGDFTGGN
EPDGSSLIQP VLERFAQAQS IPVFQIKGVG HDSTNFPLPL GIPAHIHLGD TINLTVFR
//
