ID A0A222VWP3_9PSEU Unreviewed; 481 AA.
AC A0A222VWP3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=DES30_104168 {ECO:0000313|EMBL:PWV78434.1},
GN SAMN05421630_104168 {ECO:0000313|EMBL:SDC85904.1};
OS Prauserella marina.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Prauserella.
OX NCBI_TaxID=530584 {ECO:0000313|EMBL:SDC85904.1, ECO:0000313|Proteomes:UP000199494};
RN [1] {ECO:0000313|EMBL:SDC85904.1, ECO:0000313|Proteomes:UP000199494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5506 {ECO:0000313|EMBL:SDC85904.1,
RC ECO:0000313|Proteomes:UP000199494};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PWV78434.1, ECO:0000313|Proteomes:UP000246674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45268 {ECO:0000313|EMBL:PWV78434.1,
RC ECO:0000313|Proteomes:UP000246674};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-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}.
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DR EMBL; QGTN01000004; PWV78434.1; -; Genomic_DNA.
DR EMBL; FMZE01000004; SDC85904.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A222VWP3; -.
DR STRING; 530584.SAMN05421630_104168; -.
DR KEGG; pmad:BAY61_28845; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000199494; Unassembled WGS sequence.
DR Proteomes; UP000246674; 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; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000199494};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..481
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038222787"
FT DOMAIN 64..236
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 320..462
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT REGION 25..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 481 AA; 52034 MW; 5213276AF4939B1A CRC64;
MFSRRVRTVL LGGLICTCTL TACSSPEPPR EDAAPAPSQP GEGADGIGDP YYPADGNGGY
DALDYAVTID YNPGNGILDG DTTVTAKATE DLERFNLDLR GFTVASVEVD GEEAEFAREG
DAELVITPDQ PLAGGDEFTT RVRYTGEPVA AAEGQLGGNG WHRTASGGAF VIGEPQSASY
WYPVNEHPSD KAAFHLTATV PEEWTAVSIG RKESESTKAG KTTTTWAEPD PIASYLTVLA
IDRFTVDESR LADGTPVLDA YAPGAEGIKE DAARVGEIID FLSGKFGEYP ANAAGGIYLG
EHVGYSLETQ GRPIYTRSAD LETIVHELAH QWYGNSVSVE SWADICLNEC LASYSQWLWA
EGKEGADLDA RYRATVEQLR ADSGFWGQQL YDMGSGKEFE GVYDKGILAM HALRRAIGEE
AFDKVLTGWP EEHRNSNASW LDFEAYVSEV AGTDLTAFFQ AWFHGTELPG DEHLYPGSLS
R
//
