ID A0A142EIN9_9BACT Unreviewed; 527 AA.
AC A0A142EIN9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=AO498_01230 {ECO:0000313|EMBL:AMQ54994.1};
OS Algoriphagus sanaruensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=1727163 {ECO:0000313|EMBL:AMQ54994.1, ECO:0000313|Proteomes:UP000073816};
RN [1] {ECO:0000313|Proteomes:UP000073816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8-2 {ECO:0000313|Proteomes:UP000073816};
RA Shintani M.;
RT "Complete sequence of Algoriphagus sp. M8-2.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMQ54994.1, ECO:0000313|Proteomes:UP000073816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8-2 {ECO:0000313|EMBL:AMQ54994.1,
RC ECO:0000313|Proteomes:UP000073816};
RX PubMed=27174266;
RA Muraguchi Y., Kushimoto K., Ohtsubo Y., Suzuki T., Dohra H., Kimbara K.,
RA Shintani M.;
RT "Complete Genome Sequence of Algoriphagus sp. Strain M8-2, Isolated from a
RT Brackish Lake.";
RL Genome Announc. 4:0-0(2016).
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; CP012836; AMQ54994.1; -; Genomic_DNA.
DR RefSeq; WP_067542618.1; NZ_CP012836.1.
DR AlphaFoldDB; A0A142EIN9; -.
DR STRING; 1727163.AO498_01230; -.
DR KEGG; alm:AO498_01230; -.
DR PATRIC; fig|1727163.4.peg.254; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000073816; Chromosome.
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; cd09603; M1_APN_like; 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; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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 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:UP000073816};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..527
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007494384"
FT DOMAIN 41..214
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 263..457
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 527 AA; 60076 MW; 87CF7206BB326A5A CRC64;
MKTRISISLL CLLFLVTFPA FSQNWDWGGP IDPIQAKMKI LHYRLDLEIF PETQRISGSN
TITFSTAEKL DLLRFQLINQ YEVSKVLMDG KEVRFTHEND LIDITPIDCT CDQVQIFYGG
KTPIAQNPPW TGGFTWEKDQ LENHWMGLSS QGEGAKIFMP ALDHPSSEPS EGVDLHFTVP
QPYFVASNGR LIETEESSEK VTYHWRTTYP INNYNINFTL GIFHEVKHDF TSVSGQSIPM
HAWVLQENKA KARELLEVLR ISTETQEKYF GPFPFPQDKI SVVETPYLGM EHQTINAYGN
NFQFVPMGKV KYDWLLHHEL GHEWFGNKVS VGDWADMWIH EGLTAYGDWL FYWEHGGPDA
YFAKAKAEAR HLPHAKPVVS PPNSTEEEAY HGEIYSKGAM VIHSLRGVLG DELFFPALKA
FVMDDRFTYL NQVTTRDFTD FIQSYTGKDL QGFFDLYLYT TDIPTLKISK KGKSGYALSL
EGITFELLVE VLTSEGLNKI NLGPKPVTIT SNTPPQVDPN GWLMLGK
//
