ID A0A2C9ZU10_9BACT Unreviewed; 302 AA.
AC A0A2C9ZU10;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:OUJ70158.1};
GN ORFNames=BXP70_25240 {ECO:0000313|EMBL:OUJ70158.1};
OS Hymenobacter crusticola.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1770526 {ECO:0000313|EMBL:OUJ70158.1, ECO:0000313|Proteomes:UP000194873};
RN [1] {ECO:0000313|EMBL:OUJ70158.1, ECO:0000313|Proteomes:UP000194873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIMBbqt21 {ECO:0000313|EMBL:OUJ70158.1};
RA Liang Y., Feng F.;
RT "A new Hymenobacter.";
RL Submitted (JAN-2017) 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:OUJ70158.1}.
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DR EMBL; MTSE01000026; OUJ70158.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9ZU10; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000194873; 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:OUJ70158.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000194873};
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 172..288
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 110
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 273
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 302 AA; 32899 MW; E82331AD9BE3B129 CRC64;
MPTTAPSLRP GDRVAIVCPA RKVSHAEVAA AVAILASWGL EVMLGDTVTA EYHQFAGTDE
LRRADFQRML DAPDIRAILC ARGGYGTSRI IDQLDFSRFA ENPKWIAGFS DVTVLNCHLL
ALEHESIHGV MPLLFDQAGG EESLESLRHV LFGEEVSYAA PAHPLNRLGT ATGELVGGNL
SLLQNLSGTR SDCPTTGRIL FLEDIDEYLY NIDRMMVHLD RTGKLQNLAG LLVGHFTDPH
DNSVPFGQTP YEIIQTYAGK YNFPVAYGFP VGHEPQNMAL VCGRTAQMIV DAAGVRVAYS
TT
//
