ID A0A0P0GE28_9BACE Unreviewed; 320 AA.
AC A0A0P0GE28;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:KAA5420402.1};
DE SubName: Full=Putative murein peptide carboxypeptidase {ECO:0000313|EMBL:ALJ60522.1};
DE EC=3.4.16.- {ECO:0000313|EMBL:ALJ60522.1};
GN Name=ykfA {ECO:0000313|EMBL:ALJ60522.1};
GN ORFNames=BcellWH2_03288 {ECO:0000313|EMBL:ALJ60522.1}, DWX97_10070
GN {ECO:0000313|EMBL:RGS37468.1}, F2Y53_07875
GN {ECO:0000313|EMBL:KAA5458454.1}, F2Y70_23030
GN {ECO:0000313|EMBL:KAA5420402.1}, F2Y81_03505
GN {ECO:0000313|EMBL:KAA5423151.1}, F2Y87_02580
GN {ECO:0000313|EMBL:KAA5422018.1};
OS Bacteroides cellulosilyticus.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=246787 {ECO:0000313|EMBL:ALJ60522.1, ECO:0000313|Proteomes:UP000061809};
RN [1] {ECO:0000313|EMBL:ALJ60522.1, ECO:0000313|Proteomes:UP000061809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH2 {ECO:0000313|EMBL:ALJ60522.1,
RC ECO:0000313|Proteomes:UP000061809};
RX PubMed=26430127;
RA Wu M., McNulty N.P., Rodionov D.A., Khoroshkin M.S., Griffin N.W.,
RA Cheng J., Latreille P., Kerstetter R.A., Terrapon N., Henrissat B.,
RA Osterman A.L., Gordon J.I.;
RT "Genetic determinants of in vivo fitness and diet responsiveness in
RT multiple human gut Bacteroides.";
RL Science 350:AAC5992-AAC5992(2015).
RN [2] {ECO:0000313|EMBL:RGS37468.1, ECO:0000313|Proteomes:UP000283341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF22-3AC {ECO:0000313|EMBL:RGS37468.1,
RC ECO:0000313|Proteomes:UP000283341};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000425249, ECO:0000313|Proteomes:UP000448877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIOML-A2 {ECO:0000313|EMBL:KAA5458454.1,
RC ECO:0000313|Proteomes:UP000425249}, BIOML-A3
RC {ECO:0000313|EMBL:KAA5420402.1, ECO:0000313|Proteomes:UP000475645},
RC BIOML-A6 {ECO:0000313|EMBL:KAA5423151.1,
RC ECO:0000313|Proteomes:UP000448877}, and BIOML-A8
RC {ECO:0000313|EMBL:KAA5422018.1, ECO:0000313|Proteomes:UP000482653};
RX PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA Xavier R.J., Alm E.J.;
RT "A library of human gut bacterial isolates paired with longitudinal
RT multiomics data enables mechanistic microbiome research.";
RL Nat. Med. 25:1442-1452(2019).
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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DR EMBL; CP012801; ALJ60522.1; -; Genomic_DNA.
DR EMBL; VVYT01000109; KAA5420402.1; -; Genomic_DNA.
DR EMBL; VVYX01000003; KAA5422018.1; -; Genomic_DNA.
DR EMBL; VVYV01000003; KAA5423151.1; -; Genomic_DNA.
DR EMBL; VVYS01000138; KAA5458454.1; -; Genomic_DNA.
DR EMBL; QRVJ01000006; RGS37468.1; -; Genomic_DNA.
DR RefSeq; WP_007211932.1; NZ_VVYX01000003.1.
DR AlphaFoldDB; A0A0P0GE28; -.
DR STRING; 246787.BcellWH2_03288; -.
DR GeneID; 66305377; -.
DR KEGG; bcel:BcellWH2_03288; -.
DR PATRIC; fig|246787.4.peg.3404; -.
DR eggNOG; COG1619; Bacteria.
DR Proteomes; UP000061809; Chromosome.
DR Proteomes; UP000283341; Unassembled WGS sequence.
DR Proteomes; UP000425249; Unassembled WGS sequence.
DR Proteomes; UP000448877; Unassembled WGS sequence.
DR Proteomes; UP000475645; Unassembled WGS sequence.
DR Proteomes; UP000482653; 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:ALJ60522.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ALJ60522.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 16..131
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 189..304
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 112
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 220
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 289
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 320 AA; 35436 MW; E607FDC15B6B9EB1 CRC64;
MNSLIFPSYV QKGDRVIILS PSSKIDKSFL KGAKKRLKSW GLEVVMAKHA GSSHGTYGGS
IKQRVEDLQN ALDDEKAKVI LCSRGGYGAV HLLGKLDFTR FREHPKWLIG FSDITALHNV
LQKEGFASLH ALMARHLTVE SEDDFCTLAL KDILFGHFNP ETAESVEISE NGFSYICPGH
KLNHKGTASG ILRGGNLSVF YGLRGTPYDI PAEGTILFIE DVGERPHAVE RMIYNLKLGG
ILEKLSGLII GQFTEYEENK SLGKELYGAI ADLVKEYDYP VCFNFPVGHV SMNLPMINGA
EVTLETGRKE VKLSFNLDKE
//
