ID A0A0A0JV36_9MICO Unreviewed; 512 AA.
AC A0A0A0JV36;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=N801_08700 {ECO:0000313|EMBL:KGN41295.1};
OS Knoellia aerolata DSM 18566.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Knoellia.
OX NCBI_TaxID=1385519 {ECO:0000313|EMBL:KGN41295.1, ECO:0000313|Proteomes:UP000030013};
RN [1] {ECO:0000313|EMBL:KGN41295.1, ECO:0000313|Proteomes:UP000030013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18566 {ECO:0000313|EMBL:KGN41295.1,
RC ECO:0000313|Proteomes:UP000030013};
RA Zhu W., Wang G.;
RT "The genome sequence of Knoellia aerolata.";
RL Submitted (AUG-2013) 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:KGN41295.1}.
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; AVPL01000020; KGN41295.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0JV36; -.
DR STRING; 1385519.N801_08700; -.
DR MEROPS; M01.032; -.
DR eggNOG; COG0308; Bacteria.
DR Proteomes; UP000030013; 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:UP000030013};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..512
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001964589"
FT DOMAIN 53..226
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 324..465
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 512 AA; 54965 MW; 53AE2F2B4CF7315E CRC64;
MAATAVTAAL AVGAPLAGAD DSGGKNGRFT AGTPGVGDVY YPLAGNGGYD VRHYDIAGSY
DPATDVWSAT STIEAVATAD LYRFNLDFDG MTITSLTVGG KPAGWTRDGA ELVVVPRQKV
RAGSPMTIVT SYSGVPKEFV IPLEGFELRT GFMATDDGAT VAGQPDVAAG WFPVNDHPRD
KAAYTFHVTV PDGLGVVANG FLVGERSANG RTTFDWDAPE PMASYLATID IGEWDVRQWS
TPSGLPVYDA VDPDLLDDPV LGPAIDSSLS RQGEVLDVLS AAFGPYPFST VGAIVDDQDD
LFFALETQTR PVYSKYFWPD GGDAVVAHEL AHQWYGDDVA LEQWQDIWLN EGWATYAEWL
WAEHEGFFTP QDALDFYLAV IPDDDPFWAF VIGEPPADDL FGEPVYLRGG LTLQVLRNRV
GDADFFEIAK QWASQRSGGT GTTAQFIALA ESVSGQQLDD LFDAWLFTGS KPEVTSLAGA
RSGSPDARSQ DAASAVESWG SAFGRRIAHG RY
//
