ID A0A2H1ED26_9FLAO Unreviewed; 330 AA.
AC A0A2H1ED26;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:SFZ84568.1};
GN ORFNames=MARIT_2808 {ECO:0000313|EMBL:SFZ84568.1};
OS Tenacibaculum maritimum NCIMB 2154.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=1349785 {ECO:0000313|EMBL:SFZ84568.1, ECO:0000313|Proteomes:UP000231564};
RN [1] {ECO:0000313|EMBL:SFZ84568.1, ECO:0000313|Proteomes:UP000231564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 2154T {ECO:0000313|EMBL:SFZ84568.1};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; LT634361; SFZ84568.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H1ED26; -.
DR STRING; 1349785.GCA_000509405_01848; -.
DR KEGG; tmar:MARIT_2808; -.
DR Proteomes; UP000231564; Chromosome MARIT.
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:SFZ84568.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000231564};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 40..157
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 202..316
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 138
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 233
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 302
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 330 AA; 36832 MW; 659FFAF4C464C2FB CRC64;
MNTNKNILVL ILFMIASSLL GQSISLKKIK PPYLQKGDTI IILAPAGILK NRALVIDKAK
ILAEKWGLKV LYGKHMFEQG NHFAGTDEQR CEDFQKALDD PTIKAIWSAR GGYGSVRILD
RLDFTIFKKQ PKWIIGYSDL TAFHNHINNV GVETLHAMMG VSLEDKAAMI TETIATFKKA
LFGEQLKYEV GASRYNRKGK VSGELVGGNI AVLASMLGSE SQLDTDGKIL FIEEIGEYKY
SIDRMLQSLR RAGYFRKLKG VIVGGMTKIK KNTTPWGSSI EQLILDIIPE NIPVMFNFPA
GHDSDNRALI LGRKVVLEVE ENKALLLFEE
//
