ID   AMPN_HAEIN              Reviewed;         869 AA.
AC   P45274;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=Aminopeptidase N;
DE            EC=3.4.11.2;
DE   AltName: Full=Alpha-aminoacylpeptide hydrolase;
GN   Name=pepN; OrderedLocusNames=HI_1614;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-129.
RC   STRAIN=Eagan / Serotype B;
RX   PubMed=7927773; DOI=10.1128/iai.62.11.4922-4928.1994;
RA   McCrea K.W., Watson W.J., Gilsdorf J.R., Marrs C.F.;
RT   "Identification of hifD and hifE in the pilus gene cluster of Haemophilus
RT   influenzae type b strain Eagan.";
RL   Infect. Immun. 62:4922-4928(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RC   STRAIN=AM30 (770235) / Serotype B;
RX   PubMed=7997179; DOI=10.1111/j.1365-2958.1994.tb00461.x;
RA   van Ham M.S., van Alphen L., Mooi F.R., van Putten J.P.M.;
RT   "The fimbrial gene cluster of Haemophilus influenzae type b.";
RL   Mol. Microbiol. 13:673-684(1994).
CC   -!- FUNCTION: Aminopeptidase N is involved in the degradation of
CC       intracellular peptides generated by protein breakdown during normal
CC       growth as well as in response to nutrient starvation. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR   EMBL; L42023; AAC23262.1; -; Genomic_DNA.
DR   EMBL; Z33502; CAA83910.1; -; Genomic_DNA.
DR   EMBL; U58657; AAB70877.1; -; Genomic_DNA.
DR   PIR; F64132; F64132.
DR   RefSeq; NP_439756.1; NC_000907.1.
DR   AlphaFoldDB; P45274; -.
DR   SMR; P45274; -.
DR   STRING; 71421.HI_1614; -.
DR   MEROPS; M01.005; -.
DR   EnsemblBacteria; AAC23262; AAC23262; HI_1614.
DR   KEGG; hin:HI_1614; -.
DR   PATRIC; fig|71421.8.peg.1687; -.
DR   eggNOG; COG0308; Bacteria.
DR   HOGENOM; CLU_007993_2_0_6; -.
DR   OrthoDB; 100605at2; -.
DR   PhylomeDB; P45274; -.
DR   BioCyc; HINF71421:G1GJ1-1627-MONOMER; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; cd09600; M1_APN; 1.
DR   Gene3D; 2.60.40.1840; -; 1.
DR   Gene3D; 3.30.2010.30; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 1.25.50.10; Peptidase M1, alanyl aminopeptidase, C-terminal domain; 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; IPR038438; PepN_Ig-like_sf.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR012779; Peptidase_M1_pepN.
DR   InterPro; IPR024601; Peptidase_M1_pepN_C.
DR   InterPro; IPR037144; Peptidase_M1_pepN_C_sf.
DR   InterPro; IPR035414; Peptidase_M1_pepN_Ig-like.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   NCBIfam; TIGR02414; pepN_proteo; 1.
DR   PANTHER; PTHR46322; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR46322:SF1; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR   Pfam; PF11940; DUF3458; 1.
DR   Pfam; PF17432; DUF3458_C; 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; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW   Metal-binding; Metalloprotease; Protease; Reference proteome; Zinc.
FT   CHAIN           1..869
FT                   /note="Aminopeptidase N"
FT                   /id="PRO_0000095070"
FT   ACT_SITE        299
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         262..266
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         298
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         302
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         321
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   SITE            382
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        58
FT                   /note="Q -> G (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        93
FT                   /note="I -> L (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        121
FT                   /note="C -> T (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   869 AA;  99786 MW;  A00381DC6FB725D1 CRC64;
     MLAKAKYRKD YKQPDFTVTD IYLDFQLDPK HTVVTAITKF QRLNNEATSL CLDGHSFQFS
     SIKFNGEPFS DYQQDGESLT LDLKDKSADE FEIEIVTFLV PAENTSLQGL YQSGEGICTQ
     CEAEGFRQIT YMLDRPDVLA RYITKITADK TKYPFLLSNG NRIASGELED GRHWVEWNDP
     FPKPSYLFAL VAGDFDLLQD KFITKSGREV ALELYVDRGN LNRATWAMES LKKAMKWDED
     RFNLEYDLDI YMIVAVDFFN MGAMENKGLN IFNSKFVLAN PQTATDDDYL AIESVIAHEY
     FHNWTGNRVT CRDWFQLSLK EGLTVFRDQE FSSDTGSRAV NRINNVKFLR TVQFAEDASP
     MSHPIRPEKV IEMNNFYTVT VYEKGAEVIR MLHTLLGEQG FQKGMQLYIA ENDGKAATCE
     DFVSAMERAN NLDLNQFRRW YSQSGTPELL ISDAYDEKTH TYRLTVSQST PPTADQMEKV
     NLHIPLKVAL YDANGTKQML QHNGELLSDV LNVTEKDQVF EFHGIYGRPI PALLCDFSAP
     VKLDYDYKTE QLLGLLKFAD NQFIRWDAAQ MLFAQELRRN VVRFQQGEAL EISPEILTAL
     SYVLNHYEKD IELATLILTL PKEMEFAESF KTIDPDGISA ARAFMQAQIA ESLKDDFLRV
     YTHIRLNDYQ VTQQDIALRV MRNLCLTYLA YTNLGNNLVQ KHYNNANNMT DTLAALSVAT
     KAALLCRDVL LADFEQKWQH DGLVMDKWFA LQATRPDDNV LEIIQLLMDH PSFNFNNPNR
     LRSLVGSFAN HNLKAFHNVS GSGYRFLTDV LIRLNESNPQ VAARLIEPLI RFSRFDAQRQ
     TLMKRALERL SVVENLSKDL FEKIEKALQ
//