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Database: UniProt
Entry: A0A2S4YX34_9ACTN
LinkDB: A0A2S4YX34_9ACTN
Original site: A0A2S4YX34_9ACTN 
ID   A0A2S4YX34_9ACTN        Unreviewed;       348 AA.
AC   A0A2S4YX34;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:POX53304.1};
GN   ORFNames=C3489_15860 {ECO:0000313|EMBL:POX53304.1};
OS   Streptomyces sp. Ru71.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2080746 {ECO:0000313|EMBL:POX53304.1, ECO:0000313|Proteomes:UP000237414};
RN   [1] {ECO:0000313|EMBL:POX53304.1, ECO:0000313|Proteomes:UP000237414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ru71 {ECO:0000313|EMBL:POX53304.1,
RC   ECO:0000313|Proteomes:UP000237414};
RA   Suneja G., Sharma R.;
RT   "Genome sequencing of cellulose degrading bacteria.";
RL   Submitted (FEB-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:POX53304.1}.
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DR   EMBL; PQSS01000022; POX53304.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S4YX34; -.
DR   OrthoDB; 9807329at2; -.
DR   Proteomes; UP000237414; Unassembled WGS sequence.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   CDD; cd07062; Peptidase_S66_mccF_like; 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:SF4; CARBOXYPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR30237; MURAMOYLTETRAPEPTIDE CARBOXYPEPTIDASE; 1.
DR   Pfam; PF02016; Peptidase_S66; 1.
DR   Pfam; PF17676; Peptidase_S66C; 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:0000313|EMBL:POX53304.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000313|EMBL:POX53304.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237414}.
FT   DOMAIN          16..131
FT                   /note="LD-carboxypeptidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02016"
FT   DOMAIN          205..337
FT                   /note="LD-carboxypeptidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17676"
SQ   SEQUENCE   348 AA;  38606 MW;  BDBE1BD36D00E287 CRC64;
     MTTIAYPPKP CPGDRIAVLS PSAGLPALFP RPYELGLERL HKDYGLEPVE YPTTRTLDAS
     PRERADDINA AFADPDVRAV IASIGGDDQI TVLPLLDREL IRANPKPFFG MSDNSNLLAF
     LYNTGIVAYH GASVMVELGR PVAMHPQTAD SLRAALFTSG PYELRPAERW RDVDRDWADP
     ATFEAEPRTR PGTGWIWQNA DRVVEGRAWG GCLEVVGRLL MADREISHDL SVYDGGVLLL
     ETSEEMPIAR EVFRTVRSMG ERGLLQRFSA VLVGRAKSWS LENPTTPEEA ARYAAEQRQA
     VLRAMRLYAP DTLIVFDVDF GHTDPQFVLP YGGVVRVDGP ARRITVTY
//
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