ID A0A0J6CVC0_9BACI Unreviewed; 339 AA.
AC A0A0J6CVC0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Peptidase S66 {ECO:0000313|EMBL:KMM37098.1};
GN ORFNames=AB986_14535 {ECO:0000313|EMBL:KMM37098.1};
OS Alkalihalobacillus macyae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=157733 {ECO:0000313|EMBL:KMM37098.1, ECO:0000313|Proteomes:UP000035996};
RN [1] {ECO:0000313|EMBL:KMM37098.1, ECO:0000313|Proteomes:UP000035996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16346 {ECO:0000313|EMBL:KMM37098.1,
RC ECO:0000313|Proteomes:UP000035996};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Zheng C., Che J., Ge C., Shi H.,
RA Pan Z., Liu X.;
RL Submitted (JUN-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:KMM37098.1}.
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DR EMBL; LELK01000004; KMM37098.1; -; Genomic_DNA.
DR RefSeq; WP_048311887.1; NZ_LELK01000004.1.
DR AlphaFoldDB; A0A0J6CVC0; -.
DR STRING; 157733.AB986_14535; -.
DR PATRIC; fig|157733.3.peg.973; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000035996; 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; 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:UP000035996}.
FT DOMAIN 15..132
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 203..325
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 243
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 310
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 339 AA; 37915 MW; 122CED8206E2B99B CRC64;
MNKIKYPFLN QGATIGVTAP SSGAPTELHK LLTTARDRLE SKSYEVLFGD TSWTQDKAKS
ASAKIRAAEF NKMMSDEQIQ LIIPPWGGEL LIEALEYIDF DHMKTKWVLG YSDVSLLLLA
ITLNTGIATA HGTNLVDLRG EYSDDTTDMW ESVLSTEAGG SVIQYSSEKY QKEWQFDSPT
ACVFDLTEQT EWKSVSSKNA KVQGRILGGC IDVVRHLIGT PFGNVTHFRE HFITNEPIVW
YFENCGMSTT DLRRTLVHMK LAGWFTNCAG ILFGRSPANT PVGNYEIEDV YNDLYEEIQV
PILYDIDCGH VPPQNTFING SYAEVELTNG KGTVVQHFI
//
