AMPN_HAEIN
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 03-AUG-2022, entry version 147.
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; Proteobacteria; 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 RefSeq; WP_005693625.1; 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 OMA; FKRWYSQ; -.
DR PhylomeDB; P45274; -.
DR BioCyc; HINF71421:G1GJ1-1627-MON; -.
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 Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 1.25.50.10; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR Gene3D; 2.60.40.1840; -; 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 PANTHER; PTHR46322; PTHR46322; 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; SSF63737; 1.
DR TIGRFAMs; TIGR02414; pepN_proteo; 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
