ID A0A1Q2M3N7_9GAMM Unreviewed; 358 AA.
AC A0A1Q2M3N7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:AQQ67269.1};
GN ORFNames=Mag101_06185 {ECO:0000313|EMBL:AQQ67269.1};
OS Microbulbifer agarilyticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Microbulbiferaceae; Microbulbifer.
OX NCBI_TaxID=260552 {ECO:0000313|EMBL:AQQ67269.1, ECO:0000313|Proteomes:UP000188219};
RN [1] {ECO:0000313|EMBL:AQQ67269.1, ECO:0000313|Proteomes:UP000188219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GP101 {ECO:0000313|EMBL:AQQ67269.1,
RC ECO:0000313|Proteomes:UP000188219};
RA Jung J., Bae S.S., Baek K.;
RT "Genome of Microbulbifer agarilyticus GP101.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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DR EMBL; CP019650; AQQ67269.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2M3N7; -.
DR STRING; 260552.Mag101_06185; -.
DR KEGG; maga:Mag101_06185; -.
DR eggNOG; COG1619; Bacteria.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000188219; 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 ECO:0000313|EMBL:AQQ67269.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000188219};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..358
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012298054"
FT DOMAIN 56..173
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 229..343
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 153
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 260
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 328
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 358 AA; 38700 MW; 72FFBF7FAF4F257B CRC64;
MQRRKLIQSL VSAPLLAAGV SAASAGEADT VSAGYSSQME GEGLLRSKRL KSGMTVGLVT
PASNAWEDED IRFAGDVVRS LGFKVKEAAN LYRRSQYLAG PDEARAQDLN AMFADPDVDA
VFCLRGGYGT PRILPMLDYG LIRRNPKILL GYSDITALLN AIYHRSGVMT YHGPIAAQNF
TDYTLSEYQK VLVNAQSRVP LGTPPVFEAS PGRVENRNRI TRFAGGNARG RLIGGNLSLM
ASLVGTPFEP DYQGKILFLE DVGEAPYRVD RMLTQLWLAG KLQQVAGIVF GKFTETGTDG
NTFSIEHVLR ERTASLGIPV VRGLMIGHVD DQTVVPVGAL AELDGDEGVL TLLERPVA
//
