AMPEP_HELPY
ID AMPEP_HELPY Reviewed; 357 AA.
AC O25681;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Aminopeptidase HP_1037;
DE EC=3.4.11.-;
GN OrderedLocusNames=HP_1037, C694_05365;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RA Manolov A., Prihodko E., Larin A., Karpova I., Semashko T., Alexeev D.,
RA Kostrjukova E., Govorun V.;
RT "Draft genome of Helicobacter pylori.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=23825549; DOI=10.1371/journal.pone.0066605;
RA Choi H.P., Juarez S., Ciordia S., Fernandez M., Bargiela R., Albar J.P.,
RA Mazumdar V., Anton B.P., Kasif S., Ferrer M., Steffen M.;
RT "Biochemical characterization of hypothetical proteins from Helicobacter
RT pylori.";
RL PLoS ONE 8:E66605-E66605(2013).
CC -!- FUNCTION: Hydrolyzes the N-terminal amino acid residue from a
CC polypeptide chain, with a preference for substrates containing multiple
CC alanine residues. {ECO:0000269|PubMed:23825549}.
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Note=Binds 2 cobalt ions per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.38 mM for N-succinyl-Ala-Ala-Ala-Pro-Phe-p-nitroanilide
CC {ECO:0000269|PubMed:23825549};
CC KM=7.56 mM for pyroglutamyl-Pro-Arg-p-nitroanilide
CC {ECO:0000269|PubMed:23825549};
CC KM=1.12 mM for N-succinyl-Ala-Ala-Ala-p-nitroanilide
CC {ECO:0000269|PubMed:23825549};
CC KM=7.43 mM for Phe-Arg-methylcoumarine amide
CC {ECO:0000269|PubMed:23825549};
CC KM=4.06 mM for N-succinyl-Leu-Leu-Val-Tyr-methylcoumarine amide
CC {ECO:0000269|PubMed:23825549};
CC Note=kcat is 1145 min(-1) and 122 min(-1) with N-succinyl-Ala-Ala-
CC Ala-Pro-Phe-p-nitroanilide and N-succinyl-Ala-Ala-Ala-p-nitroanilide
CC as substrate, respectively.;
CC pH dependence:
CC Optimum pH is 4.0-5.0. {ECO:0000269|PubMed:23825549};
CC Temperature dependence:
CC Optimum temperature is about 40 degrees Celsius.
CC {ECO:0000269|PubMed:23825549};
CC -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR EMBL; AE000511; AAD08080.1; -; Genomic_DNA.
DR EMBL; CP003904; AFV42250.1; -; Genomic_DNA.
DR PIR; E64649; E64649.
DR RefSeq; NP_207827.1; NC_000915.1.
DR RefSeq; WP_000677174.1; NC_018939.1.
DR AlphaFoldDB; O25681; -.
DR SMR; O25681; -.
DR DIP; DIP-3255N; -.
DR IntAct; O25681; 5.
DR MINT; O25681; -.
DR STRING; 85962.C694_05365; -.
DR PaxDb; O25681; -.
DR EnsemblBacteria; AAD08080; AAD08080; HP_1037.
DR KEGG; heo:C694_05365; -.
DR KEGG; hpy:HP_1037; -.
DR PATRIC; fig|85962.47.peg.1116; -.
DR eggNOG; COG0006; Bacteria.
DR HOGENOM; CLU_017266_4_0_7; -.
DR OMA; YCSDRTR; -.
DR PhylomeDB; O25681; -.
DR SABIO-RK; O25681; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004177; F:aminopeptidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.350.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SUPFAM; SSF53092; SSF53092; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Cobalt; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome.
FT CHAIN 1..357
FT /note="Aminopeptidase HP_1037"
FT /id="PRO_0000424562"
FT BINDING 215
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 357 AA; 40796 MW; 91BBA1FB30983E3B CRC64;
MKGLERESHF TLNENAMFFE CAYSCDNALF LQLDDRSFFI TDSRYTQEAK ESVQPKNGVL
AEVVESSDLV QSAIDLIVKS SVKKLFFDPN QVNLQTYKRL NSALGDKVAL EGVPSYHRQK
RIIKNEHEIQ LLKKSQALNV EAFENFAEYV KKIFDEKESL SERYLQHKVK DFLTREGVYD
LSFEPILALN ANASKPHALP SAKDFLKAEH SILLDMGIKY ERYCSDRTRT AFFDPKDFVF
KREQSFKDKE RQKIYDIVKE AQEKAISGIR AGMTGKEADS LARGVISDYG YGQYFTHSTG
HGIGLDIHEL PYISSRSETI LEEGMVFSVE PGIYIPGFFG VRIEDLVVIK NSRSELL
