ID A0A2N8Z9I9_9VIBR Unreviewed; 868 AA.
AC A0A2N8Z9I9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN Name=pepN {ECO:0000313|EMBL:SON48585.1};
GN ORFNames=VTAP4600_A0606 {ECO:0000313|EMBL:SON48585.1};
OS Vibrio tapetis subsp. tapetis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1671868 {ECO:0000313|EMBL:SON48585.1, ECO:0000313|Proteomes:UP000235828};
RN [1] {ECO:0000313|EMBL:SON48585.1, ECO:0000313|Proteomes:UP000235828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vibrio tapetis CECT4600 {ECO:0000313|EMBL:SON48585.1};
RA Banno H., Chua N.-H.;
RL Submitted (OCT-2017) 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 ---------------------------------------------------------------------------
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; LT960611; SON48585.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N8Z9I9; -.
DR KEGG; vta:A0606; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000235828; Chromosome a.
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; cd09600; M1_APN; 1.
DR Gene3D; 2.60.40.1840; -; 1.
DR Gene3D; 3.30.2010.30; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 1.25.50.10; Peptidase M1, alanyl aminopeptidase, C-terminal domain; 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; IPR038438; PepN_Ig-like_sf.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR012779; Peptidase_M1_pepN.
DR InterPro; IPR024601; Peptidase_M1_pepN_C.
DR InterPro; IPR037144; Peptidase_M1_pepN_C_sf.
DR InterPro; IPR035414; Peptidase_M1_pepN_Ig-like.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR NCBIfam; TIGR02414; pepN_proteo; 1.
DR PANTHER; PTHR46322; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46322:SF1; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR Pfam; PF11940; DUF3458; 1.
DR Pfam; PF17432; DUF3458_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:SON48585.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SON48585.1};
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:UP000235828};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 23..185
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 225..435
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 443..543
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 547..867
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 868 AA; 98084 MW; 3C7595BC35259453 CRC64;
MAQNPQAKYR KDYQSPEFTI SHLDLTFDLY DTETIVTAIS NVKKLKQSST LLLDGDDLVL
KAVKVNGEDW KDYQELTSQL EINNLPDEFE LTIETQIDPT ANTVLEGLYK SGGAFCTQCE
AEGFRRITYY LDRPDVLAIF TTTVIADKKE NPFLLSNGNR VEEGEADNGR HWVKWNDPHP
KPAYLFALVA GDFDVLSDSY TTSSGRNVAL EIFVDKGNLD RAPHAMTSLI NSMKWDEERF
GLEYDLDIYM IVAVDFFNMG AMENKGLNVF NSKFVLANEK TATDTDYLGI EAVIGHEYFH
NWTGNRVTCR DWFQLSLKEG LTVFRDQEFS SDLGSRSVNR ISNVRTIRGP QFAEDASPMS
HPIRPEKVIE MNNFYTLTVY EKGSEVIRMM HTLLGEDKFQ KGMKLYFERH DGTAATCEDF
VLAMEEASGV DLKQFRLWYS QSGTPLVKAT SQYNESDSTF SLTLTQSTPA TPDQSDKQPL
HIPMNVELYA QSGDVFELRR NGLVSGNVLD FTEQEQTFVF EGISSEPVVS LLREFSAPVK
LEYSYQDADL MFLMVNAKND FARWDAGQML LAKYIKLNVA REQAGENFEL PSSVVDAFRG
VLLDASLEQA FIAEVLTLPS ENEVAGWFKP VDVDAINHVL HSIKKTFATE MVEELSATYH
SLKQNGYSID HDSIGRRALR NKCLGYLALT EIGNQTVVDQ FAQATNMTDT MAALASANQA
QLPCRAEMMQ SFSDEWEHDG LVMDKWFMLQ GTNPAHDALP VIKQTMSHKA FDLKNPNRTR
NLVGSFFANN PVHFHAKDGS GYAFAGEILA QLNKSNPQVA SRLIDPLLKY RNYDESRQQL
MRTELENIAK LDNLAKDLFE KVTKALEQ
//
