ID   A0A0W0ZAH6_LEGSP        Unreviewed;       454 AA.
AC   A0A0W0ZAH6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Aminopeptidase {ECO:0000313|EMBL:KTD66124.1};
DE            EC=3.4.11.1 {ECO:0000313|EMBL:KTD66124.1};
GN   ORFNames=Lspi_0187 {ECO:0000313|EMBL:KTD66124.1};
OS   Legionella spiritensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=452 {ECO:0000313|EMBL:KTD66124.1, ECO:0000313|Proteomes:UP000054877};
RN   [1] {ECO:0000313|EMBL:KTD66124.1, ECO:0000313|Proteomes:UP000054877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mt.St.Helens-9 {ECO:0000313|EMBL:KTD66124.1,
RC   ECO:0000313|Proteomes:UP000054877};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
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:KTD66124.1}.
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DR   EMBL; LNYX01000002; KTD66124.1; -; Genomic_DNA.
DR   RefSeq; WP_058482129.1; NZ_LT906457.1.
DR   AlphaFoldDB; A0A0W0ZAH6; -.
DR   STRING; 452.Lspi_0187; -.
DR   PATRIC; fig|452.5.peg.203; -.
DR   OrthoDB; 9809354at2; -.
DR   Proteomes; UP000054877; 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:KTD66124.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KTD66124.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054877}.
FT   DOMAIN          302..309
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
SQ   SEQUENCE   454 AA;  49799 MW;  2DCE81D06A8BCD8C CRC64;
     MQTERFYRCQ SDHAIPLYLI TRAQWDNQDI EISPREQNIL DNQQFKGQAG KTGIIYDDNG
     QIRTVFVGQG DATDARAMAH AATLLPPGTY RVQQELSFFA QINWTLAQYA FDRYKKRDAS
     PRYLMVTKDK LPALKAMCDA IFMVRDLINT PTNDMGPEQL ALVASDLAKV HQAELKQWCG
     DELLSDNFPA IHAVGRASAS VPRLLQLTWG KEHQPRVTLV GKGVCFDSGG LDIKPAANMR
     LMKKDMGGAA HVLGLAHWIM ATGLPVRLQV LIPAVENAVG PESFRPGDVL TMRNGITVEV
     DNTDAEGRLV LADALVKACE DSPDLLIDFA TLTGAARVAV GTDIAAMFTA DDELATDLTR
     LSVAINDPVW RLPLFDDYEA LLDSSVADLV NCSTSPYAGA TTAALFLKRF ISTDVSWVHF
     DIMAWNVAGK PGKPEGGEAM AIRTIAQYLQ DRFA
//