ID A0A1W6EDV8_9BACT Unreviewed; 343 AA.
AC A0A1W6EDV8;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:ARK13592.1};
GN ORFNames=A6C57_10355 {ECO:0000313|EMBL:ARK13592.1};
OS Fibrella sp. ES10-3-2-2.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Fibrella.
OX NCBI_TaxID=1834519 {ECO:0000313|EMBL:ARK13592.1, ECO:0000313|Proteomes:UP000193660};
RN [1] {ECO:0000313|Proteomes:UP000193660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES10-3-2-2 {ECO:0000313|Proteomes:UP000193660};
RA Kim M.K., Srinivasan S., Kim E.B., Kim K.S.;
RL Submitted (APR-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; CP015317; ARK13592.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6EDV8; -.
DR STRING; 1834519.A6C57_10355; -.
DR KEGG; fib:A6C57_10355; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000193660; Chromosome.
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:ARK13592.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000193660};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 42..159
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 212..328
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 139
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 243
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 313
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 343 AA; 37517 MW; 0F1DD242E05EB3C9 CRC64;
MIPRRIWLKS ALLAPFATRL SVQQSSLVPV SKPPRLKPGD TIGLFCPAAP AYSRETVQIT
IESLRALGFK TKLSAHFYDR YGYLAGSDAD RAADLNAFFA DPSVHAVMAM HGGWGCARIL
PLINYDQIRR TPKIILGYSD ITALLLAITA KTGLVTMHGP VGAVTWNRFT SDWLKRVLVD
GEAVQFRNPA DENATLAPTR DRITTIRPGI ARGRLIGGNL TVLSHLIGTP YVPDWKGAIL
FLEDVQEEPY RIDRMMAQLK LAGILDQVAG VVFGKCTKCD SENSYGSLTL EDILTTYLEP
LNVPVFTGSM IGHITDKFTI PVGLNAEIDA TNGTIQLLEP AVR
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