ID A0A068YU13_9BURK Unreviewed; 320 AA.
AC A0A068YU13;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase {ECO:0000313|EMBL:CDS55192.1};
DE EC=3.4.17.13 {ECO:0000313|EMBL:CDS55192.1};
OS Polaromonas sp. CG9_12.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1504672 {ECO:0000313|EMBL:CDS55192.1, ECO:0000313|Proteomes:UP000043372};
RN [1] {ECO:0000313|EMBL:CDS55192.1, ECO:0000313|Proteomes:UP000043372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Smith H.J., Foreman C.M., Ramaraj T.;
RT "Draft Genome Sequence of a Metabolically Diverse Antarctic Supraglacial
RT Stream Organism, Polaromonas sp. Strain CG9_12, Determined Using Pacific
RT Biosciences Single-Molecule Real-Time Sequencing Technology.";
RL Genome Announc. 2:1-2(2014).
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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DR EMBL; CCJP01000005; CDS55192.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068YU13; -.
DR STRING; 1504672.gene:199034459; -.
DR eggNOG; COG1619; Bacteria.
DR Proteomes; UP000043372; Unassembled WGS sequence.
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:CDS55192.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CDS55192.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000043372};
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 191..305
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 220
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 290
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 320 AA; 34915 MW; 4A106FBEB7CBC9D5 CRC64;
MNKHIYIYSP SSAVRDKFAF KRGVKRLTAL GYEVEVDEAA LRNHGRFAGN DETRLAAIHR
ASASRADVAL ISRGGYGLTR ILPGIDYKAV TNAVDRGTRF VGFSDFTAFQ MALLAQTGAI
SWAGPALGED FGAKEGADDI MEACFDDLIT GQGEGSGWRL PKKTPNKKIT EVMDPSCAKA
TNDIYSIHDS VLWGGNLAML TSLVGTPYFP VVKNGILFIE DVGEHPYRVE RMLAQLIQAG
VLAHQKAIVF GHFSDYKLVP HDNGYKIGSV IDWLKSQVTA QVLTGLPFGH VATKVILPVG
LRVTLDVEGR DAFLLWGHQH
//
