ID Q12AS5_POLSJ Unreviewed; 316 AA.
AC Q12AS5;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase {ECO:0000313|EMBL:ABE44367.1};
DE EC=3.4.17.13 {ECO:0000313|EMBL:ABE44367.1};
GN OrderedLocusNames=Bpro_2448 {ECO:0000313|EMBL:ABE44367.1};
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE44367.1, ECO:0000313|Proteomes:UP000001983};
RN [1] {ECO:0000313|Proteomes:UP000001983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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DR EMBL; CP000316; ABE44367.1; -; Genomic_DNA.
DR AlphaFoldDB; Q12AS5; -.
DR STRING; 296591.Bpro_2448; -.
DR MEROPS; S66.002; -.
DR KEGG; pol:Bpro_2448; -.
DR eggNOG; COG1619; Bacteria.
DR HOGENOM; CLU_034346_0_0_4; -.
DR Proteomes; UP000001983; 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:ABE44367.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABE44367.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001983};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 5..124
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 187..301
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 104
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 216
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 286
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 316 AA; 34071 MW; B455B934FD990C7E CRC64;
MKKHIYIYSP SSAVRDKASF KRGVRRLTAL GHEVEIDEAA LARHQRFAGD DETRLAAIHR
AAASGADVAL ITRGGYGLTR ILPGINYKAV AKAIDKGTQF VGLSDFTAFQ SAVLAKTGAV
TWAGPALGED FGTEVPPDDI MEACFDDLIT GQGEGTGWQL PKSAMNSIAD NPDLKGAETQ
FSIKNAVLWG GNLAILSSLV GTPYLPIVKG GILFVEDVGE HPYRVERMFT QLLYAGVLAQ
QKAVIFGQFT NYRLVPHDKG FKLPSVAAWL QSQIKAPVLT GLPFGHVATK VLLPVGYKTT
LAVEGRDAFL LWGHQH
//
