ID   A0A1L3JMA0_9FLAO        Unreviewed;       853 AA.
AC   A0A1L3JMA0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN   ORFNames=LPB136_13175 {ECO:0000313|EMBL:APG66267.1};
OS   Tenacibaculum todarodis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tenacibaculum.
OX   NCBI_TaxID=1850252 {ECO:0000313|EMBL:APG66267.1, ECO:0000313|Proteomes:UP000181898};
RN   [1] {ECO:0000313|EMBL:APG66267.1, ECO:0000313|Proteomes:UP000181898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0136 {ECO:0000313|EMBL:APG66267.1,
RC   ECO:0000313|Proteomes:UP000181898};
RA   Kim E., Yi H.;
RT   "Tenacibaculum sp. LPB0136, isolated from marine environment.";
RL   Submitted (NOV-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}.
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DR   EMBL; CP018155; APG66267.1; -; Genomic_DNA.
DR   RefSeq; WP_072556791.1; NZ_CP018155.1.
DR   AlphaFoldDB; A0A1L3JMA0; -.
DR   STRING; 1850252.LPB136_13175; -.
DR   KEGG; ten:LPB136_13175; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000181898; Chromosome.
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:SF304; 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.
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:UP000181898};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          135..208
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          248..462
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
SQ   SEQUENCE   853 AA;  98572 MW;  FE568DAF03FA727B CRC64;
     MKYFFSFLLS LLILISCNNN KEEKLVLEKG VSFELAKYRK QQISDVVYKL DFNIPKEKTT
     SIASKLVLNL TIHDLKHAIF LDFNEDTSNL KSLKVNDVDS EIKHQNEHLV IDRSKLKLGK
     NSIEILFDAG ELSLNRNEEF LYTLLVPDRA STLFPCFDQP DIKANYKLTI TAPKDWEVLC
     GGFEESSTSK GDFIEHVFEK TDLMSTYLFS FVAGKFTTET KNPGAFDMRF LYRENNKEKI
     SESVGEVFNI HQKSIDFLEE YTQVKFPFQK MDFAAIPPFQ YGGMEHVGAI QYRASSLFLD
     KNATQKQKLN RAKLIAHETS HMWFGDLVTM KWFNDVWMKE VFANFMADKI MNPVFPEVNH
     ELNFMMSHYP SAYSEDRTKG TNAIRQELGN LKNAGSLYGR IIYNKAPIMM RQLEYLLGEE
     AFKNGIQEYI KTYANSNADW GELVSILDEN SSKDIKNWSD VWVNSSGRPV FSEEIQLDEN
     EKVTSFAIHQ KAEDGSDKIW PQSFKIQLVY GDEVNEVNVS ISEGKVIIPE ANDLPKPTQI
     LYNTNGFGYG VFPVDKDVIN SYKNITDDVS RGYQFINLYE NMLNGEVAPL NVYQVMFNAI
     QQEKNELIVS YLSGKIQNIF WTFLNEEAQN KLQYYVNNDL YKLLEKDLPA NIKKTLFGLY
     QSIAISEEGT ANLYAIWSKK KTIKNLFLNE NNFTSLAMKL AIYKHPKTPE VLQKQQTRIS
     NSDRLERFKW MLPSLYSDKT VRDNFMKSLL EKENREKESW VQTALSNIHH PLRQDSSTKH
     LKSVLEKLEE VQLTGDIFFP KGWLASSIGN YSSKEANIIL QEFFAENPNY NPVLMKKLLQ
     TTDNLTRAQE IKK
//