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Database: UniProt
Entry: A0A2S5X6F0_9MICO
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ID   A0A2S5X6F0_9MICO        Unreviewed;       851 AA.
AC   A0A2S5X6F0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
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   Name=pepN {ECO:0000313|EMBL:PPG40059.1};
GN   ORFNames=C5C17_09395 {ECO:0000313|EMBL:PPG40059.1};
OS   Pseudoclavibacter sp. RFBA6.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Pseudoclavibacter.
OX   NCBI_TaxID=2080573 {ECO:0000313|EMBL:PPG40059.1, ECO:0000313|Proteomes:UP000237697};
RN   [1] {ECO:0000313|EMBL:PPG40059.1, ECO:0000313|Proteomes:UP000237697}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RFBA6 {ECO:0000313|EMBL:PPG40059.1,
RC   ECO:0000313|Proteomes:UP000237697};
RA   Davis E.W.II., Tabima J.F., Weisberg A.J., Lopes L.D., Wiseman M.S.,
RA   Wiseman M.S., Pupko T., Belcher M.S., Sechler A.J., Tancos M.A.,
RA   Schroeder B.K., Murray T.D., Luster D.G., Schneider W.L., Rogers E.,
RA   Andreote F.D., Grunwald N.J., Putnam M.L., Chang J.H.;
RT   "Bacteriophage NCPPB3778 and a type I-E CRISPR drive the evolution of the
RT   US Biological Select Agent, Rathayibacter toxicus.";
RL   Submitted (FEB-2018) 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}.
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:PPG40059.1}.
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DR   EMBL; PSUA01000011; PPG40059.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S5X6F0; -.
DR   Proteomes; UP000237697; 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:PPG40059.1};
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:UP000237697};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          22..190
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          235..446
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          528..837
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
SQ   SEQUENCE   851 AA;  94130 MW;  C284E8EB111F4E07 CRC64;
     MPGENLTRAE SVERRGVVLG VEHYDVALDL TTGPETFRSI TTVTFSAVPG ASTFIDAITR
     QVHSVVLNGE ALDVAAVNDG VRIQLPNLAE RNTLTVDADA IYMNTGEGLH RFVDPADGEV
     YLYSQFEVPD SRRMFAVFEQ PDLKANFTFH VTAPAAWQVV SNEPSQTPQP IDAERAVWHF
     DKTPRISSYI TALVAGPYTV VRDELTSIDG RTIPLAVYCR ASLAPNLDAD NIFRTTKQGF
     EYYEKAFGVP YPFTKYDQLF VPEFNAGAME NAGCVTFTET YVFRSKVADA VRERRVVTIL
     HELAHMWFGD LVTMKWWNDL WLNESFAEFI STLATAEATE WTENWVTFNA SEKSWAYRQD
     QLPSTHPIVA EIRDLDDVQV NFDGITYAKG GSVLKQLFAW VGRDAFFAGI NAYFSKHAWG
     NTELRDLLAE LEVTSGRDLT EWSAKWLETA GVNTLRPVYE LDEHGNFTSF AIEQTATAEH
     PTIRPHRLAI GLYNVQGDEL VRIHRFELDV DGERTEVPSF VGGALPDLII VNDDDLAYAK
     IRLDAHSVTT VQQHLPKLRA PLSRSLVVSS LWDATRDAEL RARDFIRAVL GVIGTETEST
     TRRTVLGQLI SAAKFYTAPE DRAEIVEVVT DELFELAKRA EAGSDAQFSF VKAFASLAET
     GPQLDAVAAL FDGTFALEGL EIDTDLGWEL LYALVAGGRA GEAEIAARLE TDRTADGERS
     AAHARAALPT PEGKEAAWAS VMERSDATNA IVRATVAGFD RVNDEALLEP FVDRYFGHIS
     TIWADRSFQI AETLIEGFFP AGLATARIGD AADDWLANNE AAAPAFRRMI IEGRAGVVRA
     LAAQERDAQP E
//
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