GenomeNet

Database: UniProt
Entry: I0LBW9_9ACTN
LinkDB: I0LBW9_9ACTN
Original site: I0LBW9_9ACTN 
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}.
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; 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
//
DBGET integrated database retrieval system