ID   A0A1I4KX63_9MICO        Unreviewed;       857 AA.
AC   A0A1I4KX63;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
DE   AltName: Full=Alanine aminopeptidase {ECO:0000256|ARBA:ARBA00029811};
DE   AltName: Full=Lysyl aminopeptidase {ECO:0000256|ARBA:ARBA00031533};
GN   ORFNames=SAMN04515692_11413 {ECO:0000313|EMBL:SFL83193.1};
OS   Leifsonia sp. CL147.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leifsonia.
OX   NCBI_TaxID=1798215 {ECO:0000313|EMBL:SFL83193.1, ECO:0000313|Proteomes:UP000198997};
RN   [1] {ECO:0000313|Proteomes:UP000198997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL147 {ECO:0000313|Proteomes:UP000198997};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC         peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC         amino acids including Pro (slow action). When a terminal hydrophobic
CC         residue is followed by a prolyl residue, the two may be released as
CC         an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000098};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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DR   EMBL; FOTM01000014; SFL83193.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4KX63; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000198997; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09602; M1_APN; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR   InterPro; IPR045357; Aminopeptidase_N-like_N.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR024571; ERAP1-like_C_dom.
DR   InterPro; IPR012778; Pept_M1_aminopeptidase.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   NCBIfam; TIGR02412; pepN_strep_liv; 1.
DR   PANTHER; PTHR11533:SF304; AMINOPEPTIDASE N; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   Pfam; PF11838; ERAP1_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:SFL83193.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198997};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          21..189
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          231..445
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          532..842
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
SQ   SEQUENCE   857 AA;  94045 MW;  B096D2CB1B11686C CRC64;
     MPGENLTRTE AQERASLVRT RSYDVSLDLT TGPETFRSTT TVRFSAAEGA STFIDAITRT
     VHSVTLNGAE LDPVAVSDGV RIQLDGLKDE NELTVVADAI YTNTGEGLHR FVDPVDGEVY
     LYSQFEVPDS RRMFAVFEQP DLKAEFTFTV TAPAHWAVVS NSPTPEPQDA GEGKKVWSFA
     PTPVISSYIT ALIAGPYQSV HSRLTSSDGR VIPLGVYTRK SLSEFLDADY IFDKTREGFA
     FYEERFDYPY PFAKYDQLFV PEFNAGAMEN AGAVTFTETY VFRSKVTDAI KERRVVTILH
     ELAHMWFGDL VTMKWWNDLW LNESFAEYAS TLATAEATEW TEAWTTFAAM EKSWAYRQDQ
     LPSTHPIVAT INDLEDVQVN FDGITYAKGA SVLKQLVAWV GQEDFLAGVA QYFKKHAHGN
     TELKDLLVEL EATSGRDLSD WSTKWLETAG VNTLRPEIEV DADGVITSFA VLQSAAADYP
     TIRPHRLAIG LYNLTTDGDG KQSLVRDERL ELDVDGKRTE VPGLAGTRRP DLVLINDDDL
     AYAKIRLDEA SLTVAIEHLS DIESPLARSL VWGAAWDATR DAETSASDYV RLVLGNIASE
     TESTTIRTTL NQLVLAATAY VAPERQTETA QDAADALWEL ARAAEAGSDA QFQFVKFFAA
     LASTDEQLAT IAALRDGSIT LDGLTIDTDL SWELLIALVA GGAAGTAEID AALEADNTAN
     GGQFAAQARA SIPTLEGKQA AWDSVFGSDS LPNTIVRYTG IGFQRAKDKN VLAAFIEPYF
     TTLQDVWASR SYKIAEYLVG GMYPAPLAND ELRDATRAWL DANPEPAALR RMVVENLAGV
     ERALAAQQRD AQLVGVQ
//