ID D8MQY6_ERWBE Unreviewed; 306 AA.
AC D8MQY6;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase A {ECO:0000313|EMBL:CAX59243.1};
DE EC=3.4.17.13 {ECO:0000313|EMBL:CAX59243.1};
GN Name=ldcA {ECO:0000313|EMBL:CAX59243.1};
GN OrderedLocusNames=EbC_17120 {ECO:0000313|EMBL:CAX59243.1};
OS Erwinia billingiae (strain Eb661).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793};
RN [1] {ECO:0000313|EMBL:CAX59243.1, ECO:0000313|Proteomes:UP000008793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX59243.1,
RC ECO:0000313|Proteomes:UP000008793};
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(2010).
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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DR EMBL; FP236843; CAX59243.1; -; Genomic_DNA.
DR RefSeq; WP_013201736.1; NC_014306.1.
DR AlphaFoldDB; D8MQY6; -.
DR STRING; 634500.EbC_17120; -.
DR MEROPS; S66.002; -.
DR KEGG; ebi:EbC_17120; -.
DR eggNOG; COG1619; Bacteria.
DR HOGENOM; CLU_034346_0_1_6; -.
DR Proteomes; UP000008793; Chromosome.
DR GO; GO:0106415; F:muramoyltetrapeptide carboxypeptidase activity; IEA:UniProtKB-EC.
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:CAX59243.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAX59243.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000008793};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 9..129
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 172..287
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 110
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 273
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 306 AA; 33429 MW; 3F9C4038176A8023 CRC64;
MSVTPRTFHL IAPSGYCHNQ PAAQLAVKRL QDQGHHVVNT EVIARRHQRF AGDDAERLQD
INGLAQMEDL PDILLAVRGG YGATRLLPQI DFAAVAARLK DQPVALCGHS DFTAIQLPLL
KQGAISFSGP MLTGNFGAEV LSDFTVDHFW RALTSPKLTL SWETQPQDID VQGTVWGGNL
AMIASMMGTP WLPEIEDGIL VIEDVNEHPF RVERMLLQLA QSGILPRQKA IVTGSFTGAT
LTDYDNGYDF DSVWTLIRQV TGVPLVTGLE FGHHWNTVTL PLGAQGHLQV KGSSSTLTLS
GHPTLR
//
