ID A0A0Q5TP37_9BACT Unreviewed; 462 AA.
AC A0A0Q5TP37;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Leucyl aminopeptidase {ECO:0000313|EMBL:KQS31370.1};
GN ORFNames=ASG33_13705 {ECO:0000313|EMBL:KQS31370.1};
OS Dyadobacter sp. Leaf189.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=1736295 {ECO:0000313|EMBL:KQS31370.1, ECO:0000313|Proteomes:UP000051810};
RN [1] {ECO:0000313|EMBL:KQS31370.1, ECO:0000313|Proteomes:UP000051810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf189 {ECO:0000313|EMBL:KQS31370.1,
RC ECO:0000313|Proteomes:UP000051810};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS31370.1, ECO:0000313|Proteomes:UP000051810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf189 {ECO:0000313|EMBL:KQS31370.1,
RC ECO:0000313|Proteomes:UP000051810};
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 M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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:KQS31370.1}.
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DR EMBL; LMPS01000004; KQS31370.1; -; Genomic_DNA.
DR RefSeq; WP_056285889.1; NZ_LMPS01000004.1.
DR AlphaFoldDB; A0A0Q5TP37; -.
DR STRING; 1736295.ASG33_13705; -.
DR OrthoDB; 9809354at2; -.
DR Proteomes; UP000051810; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR000819; Peptidase_M17_C.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11963:SF23; ZGC:152830; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:KQS31370.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000051810}.
FT DOMAIN 152..454
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF00883"
SQ SEQUENCE 462 AA; 50020 MW; DB8950F28D154943 CRC64;
MRIEQVFGGD EAVLVVRSFE QGAGPENQSM FRGEKGELWW FSSNELWLGL GKEPKLPSII
RIFRSLFFKR KDRWPEHIIL DAKGRSPEWI ENAIIGMILG GYNLQLYKSE PKPSSKFFSD
GLLQILTEDG VSIGAVISSG QKTALVQLRI MDLMNAPGNY KTPTILGEWA IKSGKENGYN
VSVFDKQKLE ALGMHALLAV SKGSAEPPVM IVSEYVPASY TKTVALVGKG VTFDTGGISI
KPSANMHLMK SDMGGAAAVL GIVELAAQLQ LPVRIIGIIP STENAVDGAA MKPGDVISSY
SRKTIEVIDT DAEGRLILAD GLSYAVRNFQ PDILIDLATL TGSVIQTLGY EAAGLFTPND
NLAADLANAG EATGERLWRL PVWDEYKEEI SSDIADVKNY HGKPLAGAIV AAKFLEAFTD
SHNAWAHLDI AGMAFGDTEY APGRAGTAYG IRLLRHYLAA LS
//
