ID A0A1C0Y620_9BACL Unreviewed; 321 AA.
AC A0A1C0Y620;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Peptidase S66 {ECO:0000313|EMBL:OCS82622.1};
GN ORFNames=A6M13_07040 {ECO:0000313|EMBL:OCS82622.1};
OS Caryophanon tenue.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Caryophanon.
OX NCBI_TaxID=33978 {ECO:0000313|EMBL:OCS82622.1, ECO:0000313|Proteomes:UP000093199};
RN [1] {ECO:0000313|EMBL:OCS82622.1, ECO:0000313|Proteomes:UP000093199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14152 {ECO:0000313|EMBL:OCS82622.1,
RC ECO:0000313|Proteomes:UP000093199};
RA Verma A., Pal Y., Krishnamurthi S.;
RT "Caryophanon tenue genome sequencing.";
RL Submitted (JUL-2016) 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:OCS82622.1}.
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DR EMBL; MASJ01000040; OCS82622.1; -; Genomic_DNA.
DR RefSeq; WP_066548365.1; NZ_MASJ01000040.1.
DR AlphaFoldDB; A0A1C0Y620; -.
DR STRING; 33978.A6M13_07040; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000093199; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase 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:SF5; CARBOXYPEPTIDASE YOCD-RELATED; 1.
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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000093199}.
FT DOMAIN 13..132
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 197..309
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 112
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 228
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 294
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 321 AA; 36070 MW; E544492312624372 CRC64;
MEAMYKLQRG DEVRVIAPSR SAAILSTDGI ALATASLQEL GLHVTFGKHI FDCDMQQSSS
IDARIDDLHE AFRDPNVKAI LTVIGGFNSN ELLPYIDYEL LRQHPKILCG YSDITALAHA
ITAKSGLMTY IGPHFSSFQL RGLHTYQQDA FMQMMMQAEP FSLTASPQWS DDEWYIENAP
RTYYEGQWHV YTEGVAEGRV FGGNLCTLNL LQGTPYMPNI SDCILFVEDD ELSIPETFAR
DLTSLLQAIG PIRGLMIGRF QRKSGMTEEL LHFILQKHPQ LADIPVMYNV DIGHTQPLLT
LPIGGRARMD TASRMLTFIE F
//
