ID   G7Z3Q8_AZOL4            Unreviewed;       459 AA.
AC   G7Z3Q8;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Leucine aminopeptidase {ECO:0000313|EMBL:CBS88070.1};
DE            EC=3.4.11.1 {ECO:0000313|EMBL:CBS88070.1};
GN   Name=pepA2 {ECO:0000313|EMBL:CBS88070.1};
GN   OrderedLocusNames=AZOLI_2894 {ECO:0000313|EMBL:CBS88070.1};
OS   Azospirillum lipoferum (strain 4B).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS88070.1, ECO:0000313|Proteomes:UP000005667};
RN   [1] {ECO:0000313|Proteomes:UP000005667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RX   PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA   Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA   Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA   Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA   Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA   Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA   Zhulin I.B.;
RT   "Azospirillum genomes reveal transition of bacteria from aquatic to
RT   terrestrial environments.";
RL   PLoS Genet. 7:E1002430-E1002430(2011).
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC       {ECO:0000256|ARBA:ARBA00009528}.
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DR   EMBL; FQ311868; CBS88070.1; -; Genomic_DNA.
DR   RefSeq; WP_014249049.1; NC_016622.1.
DR   AlphaFoldDB; G7Z3Q8; -.
DR   STRING; 862719.AZOLI_2894; -.
DR   KEGG; ali:AZOLI_2894; -.
DR   HOGENOM; CLU_013734_2_1_5; -.
DR   OrthoDB; 9809354at2; -.
DR   Proteomes; UP000005667; Chromosome.
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; SSF52949; Macro domain-like; 1.
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:CBS88070.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CBS88070.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   DOMAIN          307..314
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
SQ   SEQUENCE   459 AA;  48062 MW;  4787ED7EB2A8E9DC CRC64;
     MLATLLAVDG PDTVALTPVT KAGLADWLAA QSPAVASWVK AVGFTGEAGS TVFLPGPDGG
     VAHVLAGVSA IDDLWAFAGL PASLPAGSYK IDATLDARTA TRAALGWALG SYRFSRYKKP
     PEKGFANLVW PAAADRGEVE RAATATWLVR DLVNTPACDM GPAELAQAAQ DLAAEFDAAV
     EVIVGQDLLD RDYPAIHAVG RASPRAPRLI DLRWGNPQHP KVTIVGKGVC FDTGGLDLKP
     SSAMLIMKKD MGGAAHALAL GRMIMMAGLP VRLRVLVPAV ENVVSGDSFK PQDVLKTRKG
     PTVEVGNTDA EGRLILCDAL AEADSEKPEL LIDFATLTGA ARVALGPDLP ALMCNDDALA
     NDLTEAGTAV DDPMWRLPLW APYRKGLDSK VADINNVTTN GFAGAITAGL FLQEFVSKGT
     PWAHLDTYAW NGSARPGRPE GGEALGLRAA YAVIAKRFG
//