ID A0A0T1WDH8_9MYCO Unreviewed; 241 AA.
AC A0A0T1WDH8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:KQY07010.1};
GN ORFNames=ASD37_12980 {ECO:0000313|EMBL:KQY07010.1};
OS Mycobacterium sp. Root135.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1736457 {ECO:0000313|EMBL:KQY07010.1, ECO:0000313|Proteomes:UP000051127};
RN [1] {ECO:0000313|EMBL:KQY07010.1, ECO:0000313|Proteomes:UP000051127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root135 {ECO:0000313|EMBL:KQY07010.1,
RC ECO:0000313|Proteomes:UP000051127};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY07010.1, ECO:0000313|Proteomes:UP000051127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root135 {ECO:0000313|EMBL:KQY07010.1,
RC ECO:0000313|Proteomes:UP000051127};
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 S51 family.
CC {ECO:0000256|ARBA:ARBA00006534}.
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:KQY07010.1}.
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DR EMBL; LMEZ01000005; KQY07010.1; -; Genomic_DNA.
DR RefSeq; WP_056551526.1; NZ_LMEZ01000005.1.
DR AlphaFoldDB; A0A0T1WDH8; -.
DR STRING; 1736457.ASD37_12980; -.
DR OrthoDB; 9778515at2; -.
DR Proteomes; UP000051127; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03146; GAT1_Peptidase_E; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR005320; Peptidase_S51.
DR PANTHER; PTHR20842:SF0; ALPHA-ASPARTYL DIPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR20842; PROTEASE S51 ALPHA-ASPARTYL DIPEPTIDASE; 1.
DR Pfam; PF03575; Peptidase_S51; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000051127};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
SQ SEQUENCE 241 AA; 25330 MW; 8A281A5CAD5C86E0 CRC64;
MPADAPTILA TSGGIGAGKR TRFTFTALTD FAVELSGVNG RAPRMCLLAT AMGDDKTVLH
YLTEAAQSRG FVASHLSLFP MPNVDDVAAH LLEQDVVWVF GGSVAGLLAM WRLHGVDVAL
RDAWQAGVVL TGISAGSICW HAGGTTDSFG PQLRPVTNGL GFLPYANGVH YDSEAERRPL
LHSLVRDGVL PAAYATDDGV GLLYRGTELV EAVGETGSAG AYFVEECDGA AVETALDVRR
L
//
