ID A0A0Q1BFD3_9SPHI Unreviewed; 299 AA.
AC A0A0Q1BFD3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:KQB98817.1};
GN ORFNames=AQF98_20965 {ECO:0000313|EMBL:KQB98817.1};
OS Pedobacter sp. Hv1.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1740090 {ECO:0000313|EMBL:KQB98817.1, ECO:0000313|Proteomes:UP000050543};
RN [1] {ECO:0000313|EMBL:KQB98817.1, ECO:0000313|Proteomes:UP000050543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hv1 {ECO:0000313|EMBL:KQB98817.1,
RC ECO:0000313|Proteomes:UP000050543};
RA Ott B.M., Beka L., Graf J., Rio R.;
RT "Draft Genome Sequence of a Pedobacter sp. Strain Hv1, an Isolate From
RT Medicinal Leech Mucosal Castings.";
RL Submitted (OCT-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:KQB98817.1}.
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DR EMBL; LLWP01000012; KQB98817.1; -; Genomic_DNA.
DR RefSeq; WP_055133927.1; NZ_LLWP01000012.1.
DR AlphaFoldDB; A0A0Q1BFD3; -.
DR STRING; 1740090.AQF98_20965; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000050543; 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:KQB98817.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000050543};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 14..129
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 171..287
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 202
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 272
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 299 AA; 33219 MW; 07A47640E4C412DE CRC64;
MIKQPPYLKK GDKIAIVCPA KKLPKPIDAA IETLKAWGLE VVLGQTLTST YHQFAGTDEL
RAADLQHYLD DPSIKAIIAA RGGYGTIRII DRLDFSAFEQ NPKWLIGFSD ITILLSHALA
TLNTQSIHGQ MPYTFDSSTP EALDSLRKAL FGEEISYTYQ SEFTNCEGTA EGILIGGNLS
LLIAVEGSVS EMDYEGKILF LEDVGEHEYS IDRMMRLLKR NGKLAQLKGL IVGAFNEISE
ETIPFGQTPE EIILELVKDY GYPVCFNFPT GHIDDNRAMI LGKNVSLQVA KHNVQFKFL
//
