ID A0A2P8CSN9_9BACT Unreviewed; 344 AA.
AC A0A2P8CSN9;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase LdcA involved in peptidoglycan recycling {ECO:0000313|EMBL:PSK87978.1};
GN ORFNames=B0I18_1168 {ECO:0000313|EMBL:PSK87978.1};
OS Taibaiella chishuiensis.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Taibaiella.
OX NCBI_TaxID=1434707 {ECO:0000313|EMBL:PSK87978.1, ECO:0000313|Proteomes:UP000240572};
RN [1] {ECO:0000313|EMBL:PSK87978.1, ECO:0000313|Proteomes:UP000240572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12700 {ECO:0000313|EMBL:PSK87978.1,
RC ECO:0000313|Proteomes:UP000240572};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-2018) 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:PSK87978.1}.
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DR EMBL; PYGD01000016; PSK87978.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8CSN9; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000240572; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR CDD; cd07062; Peptidase_S66_mccF_like; 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:SF4; CARBOXYPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR30237; MURAMOYLTETRAPEPTIDE 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:0000313|EMBL:PSK87978.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:PSK87978.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000240572}.
FT DOMAIN 15..134
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 210..329
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 115
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 244
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 314
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 344 AA; 38509 MW; 330F21FF52DB37B7 CRC64;
MELITPQGLQ PGDKIATVSL SWGAAGELPH RYATGKERLE KIFGLEVIAT THALEPADWI
YNNPQARAAD LMEAFADPTV KAIIANIGGE DSVRMLPYID LGIIRNNPKI FLGFSDSTIT
HFICMKAGLG SFYGPALLTG FAENVAMHDY QVADIKRTLF SREVIGQVKA NEAGWTSEFV
DWFDPSLQHT QRKLEPATGW RFVSGSGVVQ GRLIGGCMEV MEMLKGTEYW PELSVWEDSI
LFFETSEDKP WPGFVRYWIR NYASLGILQR AKGIILGRPY DNLYALEYET ELLKVLNEEG
LTDMPVITRM DFGHTAPVFT IPYGRLAEIN CDQQSFSILE PGVR
//
