ID A0A3N6EWU1_9ACTN Unreviewed; 321 AA.
AC A0A3N6EWU1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Putative murein peptide carboxypeptidase {ECO:0000313|EMBL:RPK55670.1};
DE EC=3.4.16.- {ECO:0000313|EMBL:RPK55670.1};
GN Name=ykfA {ECO:0000313|EMBL:RPK55670.1};
GN ORFNames=EES43_25780 {ECO:0000313|EMBL:RPK55670.1};
OS Streptomyces sp. ADI96-02.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1522760 {ECO:0000313|EMBL:RPK55670.1, ECO:0000313|Proteomes:UP000273170};
RN [1] {ECO:0000313|EMBL:RPK55670.1, ECO:0000313|Proteomes:UP000273170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ADI96-02 {ECO:0000313|EMBL:RPK55670.1,
RC ECO:0000313|Proteomes:UP000273170};
RA Guerrero-Garzon J.F., Zehl M., Urban E., Schneider O., Ruckert C.,
RA Busche T., Kalinowski J., Zotchev S.B.;
RT "Streptomyces spp. from the marine sponge Antho dichothoma: analyses of
RT secondary metabolite biosynthesis gene clusters and some of their
RT products.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RPK55670.1}.
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DR EMBL; RPGW01000170; RPK55670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N6EWU1; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000273170; 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:RPK55670.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:RPK55670.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000273170};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 25..145
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 190..301
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 222
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 287
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 321 AA; 33115 MW; 7610C8406274ED08 CRC64;
MTHRDRGRAG GRPVRPPRLR PGARVAVVAP SGPVPAGRLA AGVAVLRAWG LDPVVAPHAR
DTHPELDHLA GADADRAADL QAAWCDPSVD AVICARGGYG AHRVVDLLDW SAIRAAGPKA
FVGYSDATVL HEAFALRAGY ATLHGPMPAT ESFLADPATR EHLRATLFAP ETVRTLASDS
AAALVPGRAR GILFGGCLSL LAADAGTPHA RTHARGGLLV IEDVGEAPYR IDGALTRLLR
SGALDGPAGV VCGSWQDCGP YARVRAVLAD RFGPLGIPVV EELGFGHGPG PLTIPLGVPA
VLDAPADGGR CTLTVEEPAL R
//
