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Database: UniProt
Entry: G6XGL1_9PROT
LinkDB: G6XGL1_9PROT
Original site: G6XGL1_9PROT 
ID   G6XGL1_9PROT            Unreviewed;       487 AA.
AC   G6XGL1;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Leucine aminopeptidase {ECO:0000313|EMBL:EHH69319.1};
GN   ORFNames=GMO_06260 {ECO:0000313|EMBL:EHH69319.1};
OS   Gluconobacter morbifer G707.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=1088869 {ECO:0000313|EMBL:EHH69319.1, ECO:0000313|Proteomes:UP000004949};
RN   [1] {ECO:0000313|EMBL:EHH69319.1, ECO:0000313|Proteomes:UP000004949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G707 {ECO:0000313|EMBL:EHH69319.1,
RC   ECO:0000313|Proteomes:UP000004949};
RA   Lee W.-J., Kim E.-K.;
RT   "Genome sequence of Gluconobacter morbifer G707, isolated from Drosophila
RT   gut.";
RL   Submitted (OCT-2011) 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:EHH69319.1}.
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DR   EMBL; AGQV01000001; EHH69319.1; -; Genomic_DNA.
DR   AlphaFoldDB; G6XGL1; -.
DR   STRING; 1088869.GMO_06260; -.
DR   PATRIC; fig|1088869.3.peg.636; -.
DR   eggNOG; COG0260; Bacteria.
DR   Proteomes; UP000004949; 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   PANTHER; PTHR11963:SF53; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR   Pfam; PF00883; Peptidase_M17; 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:EHH69319.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004949}.
FT   DOMAIN          333..340
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
SQ   SEQUENCE   487 AA;  51590 MW;  72F4FBF14D9792DB CRC64;
     MVGCLRSKSK RSKPSGFIFS GKKDMSAHIQ LPFATSAEAP AARQVHLVAA DDATTVSALL
     GDHAGFLTGQ GFKPEDGAFT LIPSGESVGA ALLCVSRDRS HDPMAFGLLG TKLLAGDWVP
     VLHGLEESAR ESAILGFCMG AYSYRVGERK AGKARMVVPD DAAKLVALAK ANWLGRDLIN
     MPANLLGPQD LANAASKALS HRGATTTVIS GDELMASYPC LAQVGEGSER KPAVVVARWK
     AREGAPRVSL IGKGVCFDTG GYDLKPPAGM LRMKKDMGGA ALMLALMCAA IDARLDVDLE
     LRLGCVENSV SGHAMRPGDV LQTRSGLTVE IGNTDAEGRL VLCDLITEAA ETKPDYILDA
     ATLTGAARVA LGPDLPALFT NDDQWGSVFL ESGKKTADAL WRMPLWHGYD AWLDSKVADL
     GNITSRPMAG AITAALYLQR FVPEGQKWAH LDTYAWNDAT SPGRPEGGET LGLRGLFEML
     TALNKNT
//
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