ID A0A1W1ZML8_9FLAO Unreviewed; 307 AA.
AC A0A1W1ZML8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase {ECO:0000313|EMBL:SMC49634.1};
GN ORFNames=SAMN06296427_10390 {ECO:0000313|EMBL:SMC49634.1};
OS Moheibacter sediminis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Moheibacter.
OX NCBI_TaxID=1434700 {ECO:0000313|EMBL:SMC49634.1, ECO:0000313|Proteomes:UP000192393};
RN [1] {ECO:0000313|EMBL:SMC49634.1, ECO:0000313|Proteomes:UP000192393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12708 {ECO:0000313|EMBL:SMC49634.1,
RC ECO:0000313|Proteomes:UP000192393};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FWXS01000003; SMC49634.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1ZML8; -.
DR STRING; 1434700.SAMN06296427_10390; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000192393; 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:SMC49634.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000192393};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 12..130
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 173..295
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 111
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 204
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 280
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 307 AA; 34879 MW; 90DE15F2ED7CE1CF CRC64;
MKPEFLKPND KIAIVAPSGR IFPEEIEDGL NLIKSWGLTP ILGKNLFQDH YNGYHFAGTD
EQRISDFQNV LDDDKIKAIW CARGGYGAVK LLDNLNWDKF LKNPKWIIGY SDITAIHNHI
NNSGIETVHG ITTKKLNTEY NNETFLTLEK ALFGKNLNYE IPAHLYNQRG NAKGKLAGGN
LSIIYSLAGS KSFIDGNDLI LFIEDWNENW YHIDRMMTNL KRSGLLNKIK GMIVGSFTQM
DVEAENPEFH SNFDQTTYEV IKKIMNEFQI PIAYQFPAGH IGDNRALIFG SEVSLEVNEN
SVILKFN
//
