ID   A0A2S7WPM3_9FLAO        Unreviewed;       852 AA.
AC   A0A2S7WPM3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN   ORFNames=BTO18_09580 {ECO:0000313|EMBL:PQJ79406.1};
OS   Polaribacter porphyrae.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1137780 {ECO:0000313|EMBL:PQJ79406.1, ECO:0000313|Proteomes:UP000238882};
RN   [1] {ECO:0000313|EMBL:PQJ79406.1, ECO:0000313|Proteomes:UP000238882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 108759 {ECO:0000313|EMBL:PQJ79406.1,
RC   ECO:0000313|Proteomes:UP000238882};
RA   Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT   "Trade-off between light-utilization and light-protection in marine
RT   flavobacteria.";
RL   Submitted (DEC-2016) 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:PQJ79406.1}.
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DR   EMBL; MSCN01000001; PQJ79406.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S7WPM3; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000238882; 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; cd09602; M1_APN; 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:SF257; PEPTIDASE_M1 DOMAIN-CONTAINING PROTEIN; 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   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:UP000238882};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          116..206
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          247..460
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
SQ   SEQUENCE   852 AA;  100136 MW;  A3F18972E8BE9F83 CRC64;
     MKNFIFTACF FIIFSCDKKQ EIQKLEGGVS YELAQYRKKQ ITDVVYNIHF KIPKEKEKPI
     NTRLKIFFTV NDLSKDVIVD FNEDKSRLNS MNVNDVLSNI NHENEHIIID KKLLSLGSNN
     IEIFFDAGET SLNRNEEFLY TLLVPDRAST LFPCFDQPDM KAKYNLRITA PKDWNVLASS
     HKESSLEVNN FIEHTFEESD LMSTYLFSFV AGKFTTKTKN PGAFDMQFLY RENNKEKIKE
     SVDKVFQIHQ NSLDFLEEYT QVKFPFQKMD FAAIPPFQYG GMEHVGAIQY RQSSLFLDKN
     ATQNQKLRRA KLIAHETSHM WFGDLVTMKW FNDVWMKEVF ANFMADKIVN PVYPEVNHNL
     SFMMSHYPSA YSEDRTKGTN AIRQNLDNLK NAGSLYGRII YNKAPIMMRQ LEYLLGEDLF
     QEGIKEYINT YENSNADWSE LVSIFDKKTT GNIKNWSDVW VNSAGRPIFY EEIETNEKGN
     VTKFIIHQKA EDNSNKIWTQ SFKIQLKDKR GYIKNINIKN IGKSFDITSA TKDFKPGQVL
     YNTNGFGYGV FPIYKNNIYS YKDIKDEVSR GYQFINLYEN MLIGKVDAFE IYKVFLEAIL
     YEKNELILNY LTSRLNTIFW TFLSEQQREN WLPTTEQTLK EILEKNNPKN VKKIAFKLLT
     QIGYDTKALR TLYAVWKKQK VYKNLFLNES DYTDLAMKLV IFKHPYSSII LDKQQDSISN
     KDRLVRFRWL LPSLSESSPE RDDFMESLFL KENREKESWV QTALNNIHHP LRQKSASKHL
     RPILDKLQEV QVTGDIFFPK RWLTSSFGNY SSREAYNIVQ EFLKDNPNYN KNLLQKLHQT
     TDNLVRAQKI KN
//