ID A0A1H7M189_9LACT Unreviewed; 358 AA.
AC A0A1H7M189;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase LdcA (Peptidoglycan recycling) {ECO:0000313|EMBL:SEL04954.1};
GN ORFNames=SAMN04488099_11076 {ECO:0000313|EMBL:SEL04954.1};
OS Alkalibacterium pelagium.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Alkalibacterium.
OX NCBI_TaxID=426702 {ECO:0000313|EMBL:SEL04954.1, ECO:0000313|Proteomes:UP000199081};
RN [1] {ECO:0000313|Proteomes:UP000199081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19183 {ECO:0000313|Proteomes:UP000199081};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNZU01000010; SEL04954.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7M189; -.
DR STRING; 426702.SAMN04488099_11076; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000199081; 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:SEL04954.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:SEL04954.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199081}.
FT DOMAIN 13..138
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 213..342
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 119
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 260
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 327
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 358 AA; 40395 MW; 84AD1F9A254F6596 CRC64;
MKKPKGLQMG DKVAVVSLSS GILGESFAEH QLKLGSDRLT ELGLVPVFMP HALKGMDALD
KYPEWRAEDL KEAFRDTSIK GIICAIGGDD TYRLLPYLME DDEFIENVKS SPKLFTGFSD
TTVNHLMFHR LGMTSFYGPN FLNDFAELGS ELLPYTRTIV KGLFAGHELD GVPKSDTWYE
ERIDFSEGAL GKDRKSHVEE NGFEVLQGEG HVTGKLLGGC LESLVECLTG ERYKEQADVI
KTFNVFPSLD EWKNALLFIE TSEERPTPDK FKEMLNVLKK YGLFEVINGI LVGKPQNEVH
YEEYKSVLVE ILQDKTIPIL YNLPFGHAYP RCLLPYGIET TLDTEDKSVK FDESYFSG
//
