ID A0A0T2KWX3_9MICO Unreviewed; 518 AA.
AC A0A0T2KWX3;
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:KRA24159.1};
GN ORFNames=ASD65_06775 {ECO:0000313|EMBL:KRA24159.1};
OS Microbacterium sp. Root61.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736570 {ECO:0000313|EMBL:KRA24159.1, ECO:0000313|Proteomes:UP000051216};
RN [1] {ECO:0000313|EMBL:KRA24159.1, ECO:0000313|Proteomes:UP000051216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root61 {ECO:0000313|EMBL:KRA24159.1,
RC ECO:0000313|Proteomes:UP000051216};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA24159.1, ECO:0000313|Proteomes:UP000051216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root61 {ECO:0000313|EMBL:KRA24159.1,
RC ECO:0000313|Proteomes:UP000051216};
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 S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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:KRA24159.1}.
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DR EMBL; LMGU01000001; KRA24159.1; -; Genomic_DNA.
DR RefSeq; WP_056220223.1; NZ_LMGU01000001.1.
DR AlphaFoldDB; A0A0T2KWX3; -.
DR STRING; 1736570.ASD65_06775; -.
DR Proteomes; UP000051216; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013595; Pept_S33_TAP-like_C.
DR PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000051216};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 425..517
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
SQ SEQUENCE 518 AA; 54531 MW; 18917AAD8A95FB3C CRC64;
MRTESARRVR RISAVVAGLV AASLALSGCL YAMIPESGPT STASAAPDTE GVSAELLPFY
EQTLTWTDCG SGFDCTTVTA PLDWSDPSSG SIDLSVIRHR ATGGDVIGSL LTNPGGPGAS
GVALIRDSLS FAVGDALQQR YDVIGFDPRG VGESTAVRCY DAADMDAYLF DIPQNPRGSD
AWTAELNANS LAFAQACDAG SDGILPFITT DNAARDMDLL RAVLGDKKLN YLGYSYGTFL
GATYAKIYPE RVGRLVLDGA IDPAVSGLDV STTQAVGFES ALRAYMAACL TESDCPFRGS
VDEGMADLGT LLASVDRAPI EASDGRMLGA DSLMTAIIAA LYSQDSWPYL TVALSDVLQG
DADVAFQLAD FYYGREGGTY SDNSTEAFRA YNCMDYPDDS TQEQKDASDA KIKAEAPTVA
PYWSGPDPCA QWPYPPTGVR EPISADGAAP ILVVGTTNDP ATPYEWSVSL AEQLSSGILI
TRVGEGHTGF NKGNACVDNA VEAYLLEGTV PDGDVRCE
//
