ID I0LBW9_9ACTN Unreviewed; 474 AA.
AC I0LBW9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
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:CCH21316.1};
GN ORFNames=MILUP08_46211 {ECO:0000313|EMBL:CCH21316.1};
OS Micromonospora lupini str. Lupac 08.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1150864 {ECO:0000313|EMBL:CCH21316.1, ECO:0000313|Proteomes:UP000003448};
RN [1] {ECO:0000313|Proteomes:UP000003448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lupac 08 {ECO:0000313|Proteomes:UP000003448};
RX PubMed=22815450; DOI=10.1128/jb.00628-12;
RA Alonso-Vega P., Normand P., Bacigalupe R., Pujic P., Lajus A., Vallenet D.,
RA Carro L., Coll P., Trujillo M.E.;
RT "Genome Sequence of Micromonospora lupini Lupac 08, Isolated from Root
RT Nodules of Lupinus angustifolius.";
RL J. Bacteriol. 194:4135-4135(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:CCH21316.1}.
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DR EMBL; CAIE01000040; CCH21316.1; -; Genomic_DNA.
DR RefSeq; WP_007465084.1; NZ_HF570108.1.
DR AlphaFoldDB; I0LBW9; -.
DR STRING; 1150864.MILUP08_46211; -.
DR MEROPS; M01.032; -.
DR eggNOG; COG0308; Bacteria.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000003448; 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:SF174; ALANINE/ARGININE AMINOPEPTIDASE-RELATED; 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 Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:CCH21316.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCH21316.1};
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:UP000003448};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..474
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003631222"
FT DOMAIN 62..233
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 276..464
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 474 AA; 50691 MW; 6964316146A048C7 CRC64;
MVLSGRAPSR RRLAAALTVL SCAVTLTAAG CTGDDDGGFR PGAADVGDPY VPGRGNGGYD
VTHYGLDVRY DPTTDRLTGR ATITATATQD LSRFNLDLVG LDVGAVTVAD RRAKHRREEG
ELVVTPRDRL PRGGSFTVAV DYAGVPTAVA DGELGSGGFL HTDDGAVALG QPDSAATWFP
VNDHPSDKAS YDIAVTVPDG LSALSNGVPG PRSSADGWTT WRWSERTPMA SYLSTLVIGN
YRVVTGEHAG RPLVTAVAAS LPASGGAAGS LARTGEIVDF LASRFGPYPF DSYGGIVVAD
DRIGYALETQ SRPVYGPAFF SDDRPNPGVV AHELAHQWFG DSVSLHRWSD IWLNEGFASY
AEWLWEEHDG GRTAQRNFEL QYASTDWSQP SVEPGRERMF GTAVYKRGAL AVHALRRTVG
DDTFFRILRT WTTERAAGTA TTSDFVALAE RVANRQLRPL FDAWLVGGAA PTPP
//