ID A0A2I8DS39_9BURK Unreviewed; 311 AA.
AC A0A2I8DS39;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:AUT50206.1};
GN ORFNames=C2U31_20380 {ECO:0000313|EMBL:AUT50206.1};
OS Achromobacter sp. AONIH1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=1758194 {ECO:0000313|EMBL:AUT50206.1, ECO:0000313|Proteomes:UP000236176};
RN [1] {ECO:0000313|Proteomes:UP000236176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AONIH1 {ECO:0000313|Proteomes:UP000236176};
RX PubMed=29437920;
RG NISC Comparative Sequencing Program;
RA Weingarten R.A., Johnson R.C., Conlan S., Ramsburg A.M., Dekker J.P.,
RA Lau A.F., Khil P., Odom R.T., Deming C., Park M., Thomas P.J.,
RA Henderson D.K., Palmore T.N., Segre J.A., Frank K.M.;
RT "Genomic Analysis of Hospital Plumbing Reveals Diverse Reservoir of
RT Bacterial Plasmids Conferring Carbapenem Resistance.";
RL MBio 9:e02011-e02017(2018).
RN [2] {ECO:0000313|Proteomes:UP000236176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AONIH1 {ECO:0000313|Proteomes:UP000236176};
RA Segre J.A., Mullikin J.;
RL Submitted (JAN-2018) 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; CP026124; AUT50206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I8DS39; -.
DR KEGG; achr:C2U31_20380; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000236176; Chromosome.
DR GO; GO:0004180; F:carboxypeptidase activity; 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:AUT50206.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000236176};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 10..129
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 179..296
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 109
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 210
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 281
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 311 AA; 33432 MW; 1E82A35A08498F36 CRC64;
MPPLRPGGRV AIVAPASAAP NAADDAADWL LSRGYQPRIM PAARSRLDTP FDYLAGTDAE
RAADLHAAFT SADIDAVWCL QGGFGSWRLL DLLDYELLRR HAKPFIGYSD ITALHLAIQR
HAGFVTFHGP MLAQDLLNGR EEPTESALYA MVGGRMGQGA WIGAPDYALP TTLMPGTATG
RLAGGNLALI CAMQGSRHEI DTRDAILFIE DVNEAVPRVD RMLSQLAAAG KFESIKGVLA
GSFTRSGARD DAQFQYAFHP LLRERFGPLG IPVLAGWPSG HGDPNLTLPL GARVTLNATR
QGLRLEQAVT R
//