ID A0A0Q7K6H5_9BACL Unreviewed; 307 AA.
AC A0A0Q7K6H5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:KQX69085.1};
GN ORFNames=ASD40_00875 {ECO:0000313|EMBL:KQX69085.1};
OS Paenibacillus sp. Root444D2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736538 {ECO:0000313|EMBL:KQX69085.1, ECO:0000313|Proteomes:UP000051657};
RN [1] {ECO:0000313|EMBL:KQX69085.1, ECO:0000313|Proteomes:UP000051657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root444D2 {ECO:0000313|EMBL:KQX69085.1,
RC ECO:0000313|Proteomes:UP000051657};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX69085.1, ECO:0000313|Proteomes:UP000051657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root444D2 {ECO:0000313|EMBL:KQX69085.1,
RC ECO:0000313|Proteomes:UP000051657};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQX69085.1}.
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DR EMBL; LMEO01000001; KQX69085.1; -; Genomic_DNA.
DR RefSeq; WP_057301469.1; NZ_LMEO01000001.1.
DR AlphaFoldDB; A0A0Q7K6H5; -.
DR STRING; 1736538.ASD40_00875; -.
DR Proteomes; UP000051657; 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:KQX69085.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000051657};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 14..129
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 178..291
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 110
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 209
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 276
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 307 AA; 33520 MW; 23358B4F736D2ECF CRC64;
MAIRPPILQR GDTIGIVTLG SPLDATIIDE RIKTIENMGF NVVVGKYAYA YGGIVASTAQ
QRAEDLMSMF ENRSVKMILP TRGGTGVKDI LPFLNYTIIK NNPKIVTGYS DITILLNVLY
QFSDLITFQS LLLIDFSAST PTYNFNQFYS ATSTLSSPRV IQNPPGMLQT SLIAGNVRGP
IVGGNLTSFV DTLGTPYEIN TVGKILVIEE THEATNVIYR YLTRLIMARK IQDCIGVVMG
QCTNCTISYS TTYNDLITDV IAPLGKPLMT NVSTAHGLYK AAIPIGANVN LDTYNNRLTV
LEPTVKA
//
