ID A0A1V9F5P4_9BACT Unreviewed; 302 AA.
AC A0A1V9F5P4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:OQP53713.1};
GN ORFNames=A4R26_07035 {ECO:0000313|EMBL:OQP53713.1};
OS Niastella populi.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niastella.
OX NCBI_TaxID=550983 {ECO:0000313|EMBL:OQP53713.1, ECO:0000313|Proteomes:UP000192276};
RN [1] {ECO:0000313|Proteomes:UP000192276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=208 {ECO:0000313|Proteomes:UP000192276};
RA Chen L., Zhuang W., Wang G.;
RL Submitted (APR-2016) 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:OQP53713.1}.
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DR EMBL; LWBP01000210; OQP53713.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9F5P4; -.
DR STRING; 550983.A4R26_07035; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000192276; 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:OQP53713.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000192276};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 14..130
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 176..289
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 111
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 206
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 276
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 302 AA; 33615 MW; C6C205B8CE085BFA CRC64;
MVKIPPYLQP GNTIALVCPS GYMAIEKAQT CIDVLQQWGY KVKVGTTVGS HSATYFSGTD
EERLINFQQI LDDEEVHAVL CARGGYGLSR IIDHISFKKF KKQPKWVIGF SDITVLHSHI
YSNYGIATLH SPMAGAFNDG GFNNEYVLSL KNALEGKRIK YECAAHEFNK KGEAVGELVG
GNLALLAHMV GTPSDIKTKG RILFLEDVGE YLYNIDRMMR QLQRSGKLSK LAGLIIGGFS
DTKDTERPFG QTAYEIIHDI VKEYDYPVCF GFPVSHEKEN YALKVGEGYK LKVGKGKVML
EE
//
