ID A0A1I5G9L7_9BURK Unreviewed; 337 AA.
AC A0A1I5G9L7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase {ECO:0000313|EMBL:SFO32657.1};
GN ORFNames=SAMN05443579_102427 {ECO:0000313|EMBL:SFO32657.1};
OS Variovorax sp. PDC80.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1882827 {ECO:0000313|EMBL:SFO32657.1, ECO:0000313|Proteomes:UP000199369};
RN [1] {ECO:0000313|Proteomes:UP000199369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PDC80 {ECO:0000313|Proteomes:UP000199369};
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}.
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DR EMBL; FOWG01000002; SFO32657.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5G9L7; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000199369; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
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:SFO32657.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000199369};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 6..125
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 177..293
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT REGION 308..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 105
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 206
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 278
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 337 AA; 36188 MW; 2BE0D3F0D005A1EA CRC64;
MSNKHIYIYS PSSAVRDKAA FRRGVARLKA LGHEVEVDEA ALSFHQRFAG DDATRLAAIG
RAAASGADIA LIARGGYGLT RILDGVPFKK VAKAIERGTE FVGLSDFTAL QNALLAKTGA
VTWAGPAVGE DFGAEAGPDD IMEACFDDLA SGQGEGTGWR MPVRDAGIKL KPVHDAVLWG
GNLCVLTSLL GTPYFPAVDQ GVLFIEDINE HPYRIERMLE QLRMAGVLGR QRAIVFGQFT
GMRKVPGYDR GFGLDTVIDR LRAQLRKVQV IAGLPFGHVP TKVLLPVGAK VELAADGRDV
FMVWGHHPHG SARPHGHAHG HDHGHAHGDH ADHGHAH
//
