ID A0A0K9XJX7_9ACTN Unreviewed; 475 AA.
AC A0A0K9XJX7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, 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=AC230_03255 {ECO:0000313|EMBL:KNB53654.1};
OS Streptomyces caatingaensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1678637 {ECO:0000313|EMBL:KNB53654.1, ECO:0000313|Proteomes:UP000037288};
RN [1] {ECO:0000313|Proteomes:UP000037288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMAA 1322 {ECO:0000313|Proteomes:UP000037288};
RA Santos S.N., Gacesa R., Taketani R.G., Long P.F., Melo I.S.;
RT "Draft genome sequence of Streptomyces sp. CMAA 1322, a bacterium isolated
RT from Caatinga biome, from dry forest semiarid of Brazil.";
RL Submitted (JUL-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:KNB53654.1}.
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; LFXA01000002; KNB53654.1; -; Genomic_DNA.
DR RefSeq; WP_049714377.1; NZ_LFXA01000002.1.
DR AlphaFoldDB; A0A0K9XJX7; -.
DR STRING; 1678637.AC230_03255; -.
DR PATRIC; fig|1678637.3.peg.716; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000037288; 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.
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:UP000037288};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..475
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039163509"
FT DOMAIN 56..228
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 271..463
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT REGION 26..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 52511 MW; EB28F034B96A88F9 CRC64;
MGSGRSACSR RALLAGAVLP LTAAAAAASG PRRRPRRERP QPYFPGHGSY GHRTVAYDLE
LGYDPGAGWL DGHARIEAVA NGAVDRVALD LARLEVHEAR LDDRPVAFRR KGGKLLISTP
RTLEAGRPFA LDIRYGGRPR PVPSQFGPIG WDRTGDDHDG TLVASQPVGA PSWFPCNDRP
DDKASYTFGI TVPVGHQALA NGSLVEHRRN GASARWTYHH PGPMASYLAA VYTGRFARET
WTPRDTGAPV PVHIACPAGT AKEVRHDLAR QGRILRVFTD LFGDYPFESY GVVVVDAELA
APVENQTLSV FGTNHMDGRR TWETLVAHET AHQWFGNSVG LGDWQHIWLN EGFATYAEWL
WSEHLDEDDA DTLARRARDE LAGRRQNLRI ADPGRRHLFD DRVYVRGACA LHALRLAVGD
TRFFRVLRTW HEARRGGFAD TDAFLAHAAR VTGRDVADVL GPWLFEPRVP KYAPA
//
