ID   M2YAV1_9MICC            Unreviewed;       865 AA.
AC   M2YAV1;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
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=C884_01324 {ECO:0000313|EMBL:EME35774.1};
OS   Kocuria palustris PEL.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=1236550 {ECO:0000313|EMBL:EME35774.1, ECO:0000313|Proteomes:UP000009877};
RN   [1] {ECO:0000313|EMBL:EME35774.1, ECO:0000313|Proteomes:UP000009877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEL {ECO:0000313|EMBL:EME35774.1,
RC   ECO:0000313|Proteomes:UP000009877};
RX   PubMed=24504000;
RA   Sharma G., Khatri I., Subramanian S.;
RT   "Draft Genome Sequence of Kocuria palustris PEL.";
RL   Genome Announc. 2:e01261-13(2014).
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}.
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:EME35774.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ANHZ02000021; EME35774.1; -; Genomic_DNA.
DR   RefSeq; WP_006215550.1; NZ_ANHZ02000021.1.
DR   AlphaFoldDB; M2YAV1; -.
DR   STRING; 71999.KPaMU14_06650; -.
DR   MEROPS; M01.012; -.
DR   Proteomes; UP000009877; 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:EME35774.1};
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:UP000009877};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          115..199
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          247..458
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          538..854
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
SQ   SEQUENCE   865 AA;  96161 MW;  FA03901774DA9AAF CRC64;
     MPTPSLTRQE AADRTERVHP HRCEVDLDLT GAPDAARRTF PVEVAWTFSF DRADGPDETF
     LDFTGEVLEL EINGRSLSAE EIAAAFAEDR LRLEGLQPQN RVRVRGEALY SRSGEGMHRY
     TDPQDGEVYL YTQYEPADAH RVMPCFDQPD LRAEWVFRLT APQQWAARSN GTPISTPAQD
     GSAATRHEFS PTLPIPAYLT SVLAGPYVSA ESSWESSAPQ RPQHLPLHLW CRASMAEHLD
     AEEIFTITRQ GLDFFTDLFD MAYPFDTYEQ AFVPEYNLGA MENPGLVTFT EDYLFPDGAS
     RQQLAGRANT ILHEMAHMWF GDLVAIHWWE DLWLKESFAE FMGAHASVSA TQFTEAWAGF
     AVGRKAWAYR QDALSTTHPI VADVPDVAAA KQNFDGITYA KGAAALKQLV AFVGLEDFTR
     ACRVYFRRHA FGSARLEDFL AVLQESSERD TASWARDWLA TTGATVLRLQ THRDPDGALV
     SASLTPEGTV HDPASERDHQ LAVSVWGAAQ QPQRTVELTL SGRTAHELPH LAGADGVLVV
     NDRDLDFAEI VVDQPTREDQ LARLSSIPDP MARAVVWSAL WTDVRQARLD PEDFVAAVIE
     HLFVESDEAV FTTVLGQAEE ALESYLPARR RPQIRGRLME RVIGQLQAAE PGSDRQRSLA
     SSLARLSHRD GAAHGLTQDL LSGEVVIPGL HLGPALRWSL LTGLVATNHA VDSSILRESE
     RDASRISQIG RARTNAARPT ARAKDLAWAE ILGHELTNDL LSATIEGFQL GSPDLLAPYR
     TRYFEVIEPE WSQRSIGMAT RLVRGLFPAA ADLSPRADPE QDPILRRSGQ WLDEHAQADP
     ALRRIVIECR DELARRLRAQ AAARP
//