ID   A0A1Q5PDQ3_9BACT        Unreviewed;       863 AA.
AC   A0A1Q5PDQ3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-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=A3841_18870 {ECO:0000313|EMBL:OKL40378.1};
OS   Pontibacter flavimaris.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Pontibacter.
OX   NCBI_TaxID=1797110 {ECO:0000313|EMBL:OKL40378.1, ECO:0000313|Proteomes:UP000186551};
RN   [1] {ECO:0000313|EMBL:OKL40378.1, ECO:0000313|Proteomes:UP000186551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S10-8 {ECO:0000313|EMBL:OKL40378.1,
RC   ECO:0000313|Proteomes:UP000186551};
RA   Zhang G., Zhang R.;
RT   "Genome sequence of Pontibacter sp. nov., of the family cytophagaceae,
RT   isolated from marine sediment of the Yellow Sea, China.";
RL   Submitted (MAR-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:OKL40378.1}.
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DR   EMBL; LVWA01000005; OKL40378.1; -; Genomic_DNA.
DR   RefSeq; WP_073852481.1; NZ_LVWA01000005.1.
DR   AlphaFoldDB; A0A1Q5PDQ3; -.
DR   STRING; 1797110.A3841_18870; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000186551; 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; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 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   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:OKL40378.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..863
FT                   /note="Aminopeptidase N"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012818459"
FT   DOMAIN          145..218
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          262..468
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
SQ   SEQUENCE   863 AA;  98742 MW;  31FF79332E07FEA1 CRC64;
     MKKRNRNLLL ASIALLSAGT LASCSSSAPA TSEAIPVETG VSKELADYRK QVLSHIAYDI
     SLQIPEQKQQ PILGEETITF RLSDNSRPMQ LDFKEAPDHL KQVWLNGKQL EVRLENEHIL
     LPAKELIVGE NEVRLEFIAG DLSLNRNEEY LYTLLVPDRA RTVLPVFDQP NLKATFKLSL
     TLPKDWKALA NGSLVDSAVT ENSKSYTFAT SDTIPTYLFS FAAGKFKHVQ RDMKGTTMHF
     YHRETDPAKI RESINPIFQL HSDALRFMEA YTQIPYPFQK FDFVAIPDFQ YGGMEHVGAI
     QYKASTLFLD ETATKDEKIS RSNLIAHETA HMWFGDLVTM QWFDDVWMKE VFANFMADKV
     TQVALENTNY DMKFLVDHFP AAYSIDRTTG ANPIRQPLDN LQDAGSLYGS IIYHKAPIMM
     RQLERLMGEE ELRKGLQEYL KAYAYQNATW PDLINILDAR TPVDLEEWNQ VWVNEPGRPV
     FSHELKTSNG KIEQLRVMQQ GEDGSERVWS QFFEIALVYP DRLEELTVDM TNKEVVVGKA
     ASKEVPQFIL FNSTGQGYGV FPVEEAMLER LYTLQDPVQR ASAYINLYEN MLNGRNLTPA
     QLIRFYQKGL AQEQEELNIK LISGQLSDVY WTFISPAQRR QLAAQLEQEV WQALQQQQAP
     NVKKLLFKTY QSIATSKDAQ DRLYQVWQKQ QPPTGVKLNE DDYTSLALAL AVRDYPDQRI
     LGEQLTRIQN PDRKKRLEFL MPALSSDAQV RNAFFASLKE AENREKEAWV ASALGYLHHP
     LRAQTSADYL PQSLELLAEI QRTGDIFFPF NWLRATFGSY QTAEAAEVVR NFLAANPDYN
     PKLKAKILQA ADDLFRAEKL VQE
//