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Database: UniProt
Entry: A0A1D9H768_9BURK
LinkDB: A0A1D9H768_9BURK
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ID   A0A1D9H768_9BURK        Unreviewed;       485 AA.
AC   A0A1D9H768;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Leucyl aminopeptidase {ECO:0000313|EMBL:AOY95560.1};
GN   ORFNames=BKK79_27880 {ECO:0000313|EMBL:AOY95560.1};
OS   Cupriavidus sp. USMAA2-4.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=876364 {ECO:0000313|EMBL:AOY95560.1, ECO:0000313|Proteomes:UP000178101};
RN   [1] {ECO:0000313|EMBL:AOY95560.1, ECO:0000313|Proteomes:UP000178101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USMAA2-4 {ECO:0000313|EMBL:AOY95560.1,
RC   ECO:0000313|Proteomes:UP000178101};
RA   Abdullah A.A.-A., Shafie N.A.H., Lau N.S.;
RT   "Complete genome sequences of three Cupriavidus strains isolated from
RT   various Malaysian environments.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC       {ECO:0000256|ARBA:ARBA00009528}.
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DR   EMBL; CP017749; AOY95560.1; -; Genomic_DNA.
DR   RefSeq; WP_071039428.1; NZ_CP017749.1.
DR   AlphaFoldDB; A0A1D9H768; -.
DR   STRING; 876364.BKK79_27880; -.
DR   KEGG; cuu:BKK79_27880; -.
DR   Proteomes; UP000178101; Chromosome 2.
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:AOY95560.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000178101}.
FT   DOMAIN          322..329
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
SQ   SEQUENCE   485 AA;  49526 MW;  6958410933B15098 CRC64;
     MSTASAPIPP PRGLTGTADD ALPLYVVTPA GLAALLDVLP AAQARWVRAT GFAAEAGTTL
     LLPAPDGALA GAVASADPAQ PLWQLAGLPA QLPARRYALA AVPGTVAPER PLAALGWAIG
     ALPGGWEAGT PDTPDAPDSA VAELVSDAAE RAAVAPLAAA TGLVRRLVNT PANVLGPQQL
     ADEVRTLARA HGARYEQWTG EALPGAGFPL VHAVGRAAAQ APRVAALHWG EPGAPRLVLV
     GKGVCFDSGG LDLKPAAGMR WMKKDMGGAA HAIALAQLLM QARLPVQLTL LVPAVENAVG
     AGALRPGDVV RAGNGLSVEI ENTDAEGRLV LADALAHALD ARHGATALVI DFATLTGAAR
     VALGPELPAL FCHDDALAAS LLEQARRVAD PLWRLPLWQP YQAMLKSSSA DLQNAAANPH
     AGAITAALFL SRFVPAGTPW LHLDLFAWNP EARPGRPRGG EAQGLRALAA WLCERFGGAG
     GTPGD
//
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