ID A0A0T0PTU7_9SPHN Unreviewed; 460 AA.
AC A0A0T0PTU7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Aminopeptidase {ECO:0000313|EMBL:KQT32246.1};
GN ORFNames=ASG29_10525 {ECO:0000313|EMBL:KQT32246.1};
OS Sphingomonas sp. Leaf412.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736370 {ECO:0000313|EMBL:KQT32246.1, ECO:0000313|Proteomes:UP000051178};
RN [1] {ECO:0000313|EMBL:KQT32246.1, ECO:0000313|Proteomes:UP000051178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf412 {ECO:0000313|EMBL:KQT32246.1,
RC ECO:0000313|Proteomes:UP000051178};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT32246.1, ECO:0000313|Proteomes:UP000051178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf412 {ECO:0000313|EMBL:KQT32246.1,
RC ECO:0000313|Proteomes:UP000051178};
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:KQT32246.1}.
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DR EMBL; LMQP01000003; KQT32246.1; -; Genomic_DNA.
DR RefSeq; WP_055983510.1; NZ_LMQP01000003.1.
DR AlphaFoldDB; A0A0T0PTU7; -.
DR STRING; 1736370.ASG29_10525; -.
DR OrthoDB; 9809354at2; -.
DR Proteomes; UP000051178; 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; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR048816; Peptidase_M17_N_1.
DR PANTHER; PTHR11963:SF53; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF21337; Peptidase_M17_N_1; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:KQT32246.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000051178}.
FT DOMAIN 308..315
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 460 AA; 48528 MW; 01A16AAEE8A251B9 CRC64;
MIDFSTLLAP DRGQPARDIH VVHPDAFGDW LARQPPRIRT AVAANRVSGK AGNRAVLPGE
GAEDWSMLLV CDEDAASPWR IASLGDGLPE GTYRLAGGEP GAAMLGWCLA QHRFTRYKAT
EPVGARVLLT GEPARIEEVV RLAHATALVR TLVDTAAADM GPAELEAEAD RLALAHDAKV
TVTRGDALAT GYPMIHAVGQ AATRERGPRL IELEWGDPAH PRIAIVGKGV CFDTGGLDLK
PSAGMRLMKK DMGGAAHALA LAGLVMAARL KVRLHLLIPA VENAVSAAAF RPGDVLATRL
GLTVENTNTD AEGRLVLGDA LTKAVEGAPD LILDFATLTG AARVALGPDL PATFANDEAL
AAELLAAGDA VRDPLWRLPL WDGYDDMLKS DVADMVNAPD GGFAGAITAA LFLRRFVPAG
IPWAHLDTFA WRPVGKPGRP KGGDAYGLRA TWALLKGRFS
//
