ID A0A0Q7GT56_9FLAO Unreviewed; 724 AA.
AC A0A0Q7GT56;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=ASC72_02610 {ECO:0000313|EMBL:KQX15785.1};
OS Flavobacterium sp. Root420.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1736533 {ECO:0000313|EMBL:KQX15785.1, ECO:0000313|Proteomes:UP000051729};
RN [1] {ECO:0000313|EMBL:KQX15785.1, ECO:0000313|Proteomes:UP000051729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root420 {ECO:0000313|EMBL:KQX15785.1,
RC ECO:0000313|Proteomes:UP000051729};
RX PubMed=26633631; DOI=.1038/nature16192;
RA Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL Nature 528:364-369(2015).
RN [2] {ECO:0000313|Proteomes:UP000051729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root420 {ECO:0000313|Proteomes:UP000051729};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000051729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root420 {ECO:0000313|Proteomes:UP000051729};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQX15785.1}.
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DR EMBL; LMEF01000001; KQX15785.1; -; Genomic_DNA.
DR RefSeq; WP_056186257.1; NZ_LMEF01000001.1.
DR AlphaFoldDB; A0A0Q7GT56; -.
DR STRING; 1736533.ASC72_02610; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000051729; 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 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 48..236
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 275..480
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 724 AA; 82728 MW; 0CBF41B7F9CB6F5C CRC64;
MKKLFLKYII FNLIAIMGQK IEAQTTDQKT DELTVYRVTA LKVHDLVHTK LDVSFDYAKR
HLNGKAWITL KPHFYETDQL TLDAKGMEFK EIAIIDGKKS IPLKYTQDSE QVFITLNRKY
KSTEKYVVYI DYIAKPNELK TKGGESITDS KGLYFVNPDG KENKPVQIWT QGETEASSAW
FPTIDKPNQK TTSEIAMTVD SKYTTLSNGK LTSQKDNKNG TRTDVWKMDQ PNAPYLFMMA
VGDFKIYKDT YNGKEVSYYL EPKYAPYAKQ IFWKTPDMMN FYSKMLGVEY PWAKYSQIVV
TDFFGGAMEN TSATVHGGYV QKTERELLDD NEESTVAHEL FHQWFGDYVT AESWSNLTMN
ESFATFGEVL WHGHDEGQDA EDRSRYGKLQ NYLSSQKNGD SPILARFHYK NKDDMFDNIS
YSKGSIILYA IKNQMGDEAF FKSLNHYLTT NAYKSGETHQ LRLSMEEVTG KDWSPYFNQW
YYQGGNPILN IEYGYANGKA TIAVKQVQQS SVQTFSLPLK VDYYVNGTKI RKEILIDQRE
QNFSFDIPSQ PTFVDLDPDK ILVGQVIDNK KIADYLFQYK NVPTYYNRIE AIKYAAKDKS
HDAQLVLLAG LKDKQDDLRT LSIKAIDLGD NQIKEEAIKT LLDIAKNDKK TISRANAIIK
LAATGDVSYK ALMQESIKNQ SYNVIAGGII GLTKYVPAEG EKALASLDDD TKKHVTALIK
KLSK
//
