ID A0A1D9P8V8_9FLAO Unreviewed; 330 AA.
AC A0A1D9P8V8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:AOZ98996.1};
GN ORFNames=BIW12_05845 {ECO:0000313|EMBL:AOZ98996.1};
OS Flavobacterium commune.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1306519 {ECO:0000313|EMBL:AOZ98996.1, ECO:0000313|Proteomes:UP000178198};
RN [1] {ECO:0000313|EMBL:AOZ98996.1, ECO:0000313|Proteomes:UP000178198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PK15 {ECO:0000313|EMBL:AOZ98996.1,
RC ECO:0000313|Proteomes:UP000178198};
RA Ekwe A., Kim S.B.;
RT "Complete Genome Sequence of Flavobacterium sp. PK15.";
RL Submitted (OCT-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; CP017774; AOZ98996.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D9P8V8; -.
DR STRING; 1306519.BIW12_05845; -.
DR KEGG; fcm:BIW12_05845; -.
DR Proteomes; UP000178198; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:AOZ98996.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000178198};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 44..159
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 201..316
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 140
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 232
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; 36918 MW; 7DE9F64D85FF1EC3 CRC64;
MPTPRFLVLN RTISVFLIII FQSFNSQAQK QMITPAALQK GDTIAIVATA RKYTDNHLQP
AIDLMRSWGL EVVLGKSIGL DNNQLAGTDE ERTADFQAQL DNPNIKAIWC VKGGYGTVRI
IDTLDFTKFK QNPKWIVGFS DITVLHNHLN TLGYKTIHGI MPVTAPRATK EAIETLRQAL
FNEALSYEIP SDPMNRIGSA KGELVGGNLS ILYSLFGSPS AIDCNDKILF IEDLDEYLYH
IDRMMMNLKR NGCLESIRGI VVGSMTKMKD NEIPWGKNAV QIIEDVTKKY HIPVIYNFPA
GHIQDNRALI LGSTVSMEVT PEKSTLKFED
//
