ID J1AJ55_9FLAO Unreviewed; 686 AA.
AC J1AJ55;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=FF52_06600 {ECO:0000313|EMBL:EJG02329.1};
OS Flavobacterium sp. F52.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1202532 {ECO:0000313|EMBL:EJG02329.1, ECO:0000313|Proteomes:UP000002690};
RN [1] {ECO:0000313|EMBL:EJG02329.1, ECO:0000313|Proteomes:UP000002690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F52 {ECO:0000313|EMBL:EJG02329.1,
RC ECO:0000313|Proteomes:UP000002690};
RX PubMed=22965088; DOI=10.1128/JB.01249-12;
RA Kolton M., Green S.J., Harel Y.M., Sela N., Elad Y., Cytryn E.;
RT "Draft Genome Sequence of Flavobacterium sp. Strain F52, Isolated from the
RT Rhizosphere of Bell Pepper (Capsicum annuum L. cv. Maccabi).";
RL J. Bacteriol. 194:5462-5463(2012).
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:EJG02329.1}.
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DR EMBL; AKZQ01000019; EJG02329.1; -; Genomic_DNA.
DR RefSeq; WP_008464006.1; NZ_AKZQ01000019.1.
DR AlphaFoldDB; J1AJ55; -.
DR PATRIC; fig|1202532.3.peg.1360; -.
DR eggNOG; COG0308; Bacteria.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000002690; 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; 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; IPR016024; ARM-type_fold.
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; SSF48371; ARM repeat; 1.
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:EJG02329.1};
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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 28..187
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 227..425
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 686 AA; 80187 MW; 9438FD8B558092C1 CRC64;
MKYIFLLFTS FLFAQQTQYV DFKSVSGQLS INPKDKLISG AVDFQFEVLQ NTDTISLDAK
NMEFSNVKVN ENEIMFINTN KELKLAFPFK KGQNHLTFNY TAKPKQALYF VDMGNDEVQI
WTQGQGRYTS NWFPSFDDVN EKLIFNLGIS YDKDYQVVAN GVLKTKTANG NLNHWQFEME
KPMSSYLLML AIGKFDKKEF KSKSRILLEY YYEPKDADRF EPTYRYSKRI FDFLEKEIGV
KYPWKINRQI PVRDFLYAGM ENTTSTLFAT RYVVDSTGFC DRNYTNVDAH ELAHHWFGDL
ITAESSTHHW LQEGFATYFA LLAEKDIYGE HYFYSKLYDT AQQIKFASRT DTIPVLNAKA
SSLTFYEKGA WALFVLHESI GDKAFKKAIK SYLNKYAYQT VNTQNFFDEI KKVSDFDLEK
FQKTWLESTA FDTPTANALL SKNKAIQKRL EIDKLKKTPF AEKKDILKST LESDVYQSVK
EAVVDQLENE KYEDKKALLL LALQTNNIKV RQNLAGSLTQ IPEDFRTNYE TLLDDKSYQT
QEIALYWLWR NFPDHRTEYL DKSKSWIGFN DYNLRTLWLS LALSTPNYTN KKDDLINELI
AFSSSKYEAT TRQNALEKLI AFKIINDQVL SNLVGATTHH MWQFSKFGRD TVRLLLKNPE
MRASFNRILP NLTPDEQFQL NRLVKE
//
