ID A0A0M2GH43_9ACTN Unreviewed; 341 AA.
AC A0A0M2GH43;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase {ECO:0000313|EMBL:KJK34239.1};
GN ORFNames=UK15_36980 {ECO:0000313|EMBL:KJK34239.1};
OS Streptomyces variegatus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=284040 {ECO:0000313|EMBL:KJK34239.1, ECO:0000313|Proteomes:UP000034786};
RN [1] {ECO:0000313|Proteomes:UP000034786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16380 {ECO:0000313|Proteomes:UP000034786};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) 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:KJK34239.1}.
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DR EMBL; JYJH01000054; KJK34239.1; -; Genomic_DNA.
DR RefSeq; WP_031144345.1; NZ_JYJH01000054.1.
DR AlphaFoldDB; A0A0M2GH43; -.
DR STRING; 284040.UK15_36980; -.
DR PATRIC; fig|284040.3.peg.6945; -.
DR Proteomes; UP000034786; 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; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR003507; S66_fam.
DR PANTHER; PTHR30237; MURAMOYLTETRAPEPTIDE 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.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:KJK34239.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:KJK34239.1}.
FT DOMAIN 39..74
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT ACT_SITE 122
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 230
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 301
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 341 AA; 36901 MW; 5DD4CCA4C9B9A053 CRC64;
MTLTALPQPL RPRALRPGDL VVIASLSGPL HAVYEPDLEQ AVVVLERMGF RVRRAPLLEG
GRHRWWSAAR PTEIAEELNA LLRDPEVRAI IAHDGGQTAL GYLDLIDFEA ITADPKPILG
FSDISLLHLV LYARTGLVGF HTDLATPGLG GHWQRATAAR QAELEKLYST LLTGTEPIGA
LPTTPTWECW RAGRTEGRLI GGVINRIVLN QATPYALPLE WFDGAVLFWE EAGGLAAYVW
SYLQVLRHAG ILDRISGMVV GIPDGIDGLD SPDASPTLRE IVLDVLGDRD IPVLGNVEFG
HAGPNLPMPV GIRVALDAQQ RTLSLLEPAV RPLALTGQPG V
//
