ID A0A0W1AD28_9GAMM Unreviewed; 454 AA.
AC A0A0W1AD28;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Leucine aminopeptidase {ECO:0000313|EMBL:KTD79229.1};
GN Name=pepA {ECO:0000313|EMBL:KTD79229.1};
GN ORFNames=Lwal_1301 {ECO:0000313|EMBL:KTD79229.1};
OS Legionella waltersii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=66969 {ECO:0000313|EMBL:KTD79229.1, ECO:0000313|Proteomes:UP000054729};
RN [1] {ECO:0000313|EMBL:KTD79229.1, ECO:0000313|Proteomes:UP000054729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51914 {ECO:0000313|EMBL:KTD79229.1,
RC ECO:0000313|Proteomes:UP000054729};
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:KTD79229.1}.
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DR EMBL; LNZB01000036; KTD79229.1; -; Genomic_DNA.
DR RefSeq; WP_058480010.1; NZ_LT906442.1.
DR AlphaFoldDB; A0A0W1AD28; -.
DR STRING; 66969.Lwal_1301; -.
DR PATRIC; fig|66969.6.peg.1430; -.
DR OrthoDB; 9809354at2; -.
DR Proteomes; UP000054729; 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:KTD79229.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000054729}.
FT DOMAIN 302..309
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 454 AA; 49159 MW; 8ADF8A4E32C67ED2 CRC64;
MQADLFYNTR GDRVVPISLI SQSEWEEGQD NYSSLESNCF FARQFKGKLG DYTFIPNSDG
VVEKAYIGSG TGNQESALAN AALVLPPGCY RLQGPLSKEA AVNWSLAQYR FDAYKKWDTP
IKTLIVDPNE LDSILALSKS IYLVRDLINR PASDMGPAEL AQAVEQLATA HKAEFTQWIG
DDLVKENFPA IHAVGRASIS APRLLSLTWG NAKHPKITLI GKGVCFDSGG LDIKPSSGMR
LMKKDMGGAA HVIGLAQWIM LQKLPIRLQV LIPAVENSIG PNAFRPGDVL TMRNGLTVEI
ENTDAEGRLV LADAVVKACE DNPELVIDFA TLTGAARVAV GTEIAAMFSN DDQLAQAIVD
AADKVSDPVW RLPLFTPYEE LLNSNAADIA NSSPSAYAGA IVAALFLRRF VTASTPWVHF
DVMAWNISSK PGKPEGGEAM GLRAVAEYLL QNYG
//
