ID A0A1W1W2S0_9BACT Unreviewed; 823 AA.
AC A0A1W1W2S0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=SAMN00120144_3189 {ECO:0000313|EMBL:SMB99922.1};
OS Hymenobacter roseosalivarius DSM 11622.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=645990 {ECO:0000313|EMBL:SMB99922.1, ECO:0000313|Proteomes:UP000192266};
RN [1] {ECO:0000313|EMBL:SMB99922.1, ECO:0000313|Proteomes:UP000192266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11622 {ECO:0000313|EMBL:SMB99922.1,
RC ECO:0000313|Proteomes:UP000192266};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FWWW01000096; SMB99922.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1W2S0; -.
DR STRING; 645990.SAMN00120144_3189; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000192266; 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; 1.25.10.10; Leucine-rich Repeat Variant; 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; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
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; PF13646; HEAT_2; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:SMB99922.1};
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:UP000192266};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..823
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012348172"
FT DOMAIN 42..231
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 269..477
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 823 AA; 91615 MW; C49054DD0DC4C843 CRC64;
MRSLHKFLPV ILTLTVINSA GAQQPDATTY RATERQVNDL VHTRLDLQFD YAKRYAYGKE
WLTLKPHAYP TDSLRLDAKG MDIKMVALVN GSSLQPLKYS YDQQHLRVSL GQKKAPGTDY
TVYIEYMAKP DEANVKGSAA ISEAKGLYFI NPDSAVAGKP VQIWTQGETE ASSVWFPTID
RPNQKMTSEI SLTVPSKYVT LSNGALTSQQ PAGPGLRRDT WKMEQPHAPY LFMLAVGDFR
ITKDTWRGKE VSYYLEPKFA PQARAIFGKT PKMLEFFSQK LGVDYPWNKY AQIVARDYVS
GAMENTTASL FGEQAQGSVR ELLDWEYAGV EREIAHELFH HWFGDYVTAE SWSNLTMNES
FANFSEVLWA EHAYGPDAGA AQADRSLRNY LRTPANYEKP LVRFQYADKE DLFDGVSYQK
GGSILNMLRA TLGEEVFFQG LKRYLTQNAF GTGESHQLRL ALEEASGQDL NWFFNQWYYR
VGHPIVTIDY QWDAARQRQA VVVRQTQAGG LFVLPLLVDV YTGGKAQRYS ATLRKAVDTL
YFPAATKPEL VDVDAAKVLV WQKQDNKSLA EYAYQYRHAP HYLDRREALT AAQAKATDPL
ARKILLAGLT DKSSALRQLA VEVLDLKNAP QRKATAPVLA KLAATDSSVQ VRAAALTALG
TLEEKRYAKL FTKALDSKSY RVQGAALQAL LPLQPKQALA RATAFEADNK GPLTVALVSV
YGQAGGPAQW PLVLSKYDAA SPSGRFDMLP GIVPLLGRLE DPTALTEGIT RMKDLAVKFK
AFGVAEPIIG GLQQIQQQQA ARLSAPQARM LVESAVKEIQ NAK
//
