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HYPA_HELPY
ID   HYPA_HELPY              Reviewed;         117 AA.
AC   P0A0U4; O25539;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Hydrogenase/urease maturation factor HypA {ECO:0000305};
GN   Name=hypA {ECO:0000303|PubMed:11123699}; OrderedLocusNames=HP_0869;
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   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 43504;
RX   PubMed=11123699; DOI=10.1046/j.1365-2958.2001.02244.x;
RA   Olson J.W., Mehta N.S., Maier R.J.;
RT   "Requirement of nickel metabolism proteins HypA and HypB for full activity
RT   of both hydrogenase and urease in Helicobacter pylori.";
RL   Mol. Microbiol. 39:176-182(2001).
RN   [3]
RP   FUNCTION, SUBUNIT, INTERACTION WITH HYPB, NICKEL-BINDING, AND MUTAGENESIS
RP   OF HIS-2; HIS-17; HIS-24; HIS-79 AND HIS-95.
RC   STRAIN=ATCC 43504;
RX   PubMed=12533448; DOI=10.1128/jb.185.3.726-734.2003;
RA   Mehta N., Olson J.W., Maier R.J.;
RT   "Characterization of Helicobacter pylori nickel metabolism accessory
RT   proteins needed for maturation of both urease and hydrogenase.";
RL   J. Bacteriol. 185:726-734(2003).
RN   [4] {ECO:0007744|PDB:2KDX}
RP   STRUCTURE BY NMR IN COMPLEX WITH ZINC, AND NICKEL-BINDING.
RX   PubMed=19621959; DOI=10.1021/ja900543y;
RA   Xia W., Li H., Sze K.H., Sun H.;
RT   "Structure of a nickel chaperone, HypA, from Helicobacter pylori reveals
RT   two distinct metal binding sites.";
RL   J. Am. Chem. Soc. 131:10031-10040(2009).
CC   -!- FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Required
CC       for nickel insertion into the metal center of the hydrogenase. Is also
CC       required for urease maturation. {ECO:0000269|PubMed:11123699,
CC       ECO:0000269|PubMed:12533448}.
CC   -!- SUBUNIT: Monomer and homodimer. Forms a complex with HypB.
CC       {ECO:0000269|PubMed:12533448}.
CC   -!- DISRUPTION PHENOTYPE: Mutant has negligible hydrogenase activity and is
CC       severely impaired in urease activity. {ECO:0000269|PubMed:11123699}.
CC   -!- SIMILARITY: Belongs to the HypA/HybF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00213, ECO:0000305}.
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DR   EMBL; AE000511; AAD07910.1; -; Genomic_DNA.
DR   PIR; E64628; E64628.
DR   RefSeq; NP_207663.1; NC_000915.1.
DR   RefSeq; WP_000545280.1; NC_018939.1.
DR   PDB; 2KDX; NMR; -; A=1-117.
DR   PDBsum; 2KDX; -.
DR   AlphaFoldDB; P0A0U4; -.
DR   BMRB; P0A0U4; -.
DR   SMR; P0A0U4; -.
DR   IntAct; P0A0U4; 19.
DR   MINT; P0A0U4; -.
DR   STRING; 85962.C694_04450; -.
DR   PaxDb; P0A0U4; -.
DR   DNASU; 899398; -.
DR   EnsemblBacteria; AAD07910; AAD07910; HP_0869.
DR   KEGG; hpy:HP_0869; -.
DR   PATRIC; fig|85962.47.peg.923; -.
DR   eggNOG; COG0375; Bacteria.
DR   OMA; DCHQESE; -.
DR   PhylomeDB; P0A0U4; -.
DR   BioCyc; MetaCyc:HP_RS04240-MON; -.
DR   EvolutionaryTrace; P0A0U4; -.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0016151; F:nickel cation binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0051604; P:protein maturation; IBA:GO_Central.
DR   HAMAP; MF_00213; HypA_HybF; 1.
DR   InterPro; IPR020538; Hydgase_Ni_incorp_HypA/HybF_CS.
DR   InterPro; IPR000688; HypA/HybF.
DR   PANTHER; PTHR34535; PTHR34535; 1.
DR   Pfam; PF01155; HypA; 1.
DR   PIRSF; PIRSF004761; Hydrgn_mat_HypA; 1.
DR   TIGRFAMs; TIGR00100; hypA; 1.
DR   PROSITE; PS01249; HYPA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Metal-binding; Nickel; Reference proteome; Zinc.
FT   CHAIN           1..117
FT                   /note="Hydrogenase/urease maturation factor HypA"
FT                   /id="PRO_0000129042"
FT   BINDING         2
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00213,
FT                   ECO:0000305|PubMed:12533448, ECO:0000305|PubMed:19621959"
FT   BINDING         3
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000305|PubMed:19621959"
FT   BINDING         40
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000305|PubMed:19621959"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00213,
FT                   ECO:0000269|PubMed:19621959, ECO:0007744|PDB:2KDX"
FT   BINDING         77
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00213,
FT                   ECO:0000269|PubMed:19621959, ECO:0007744|PDB:2KDX"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00213,
FT                   ECO:0000269|PubMed:19621959, ECO:0007744|PDB:2KDX"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00213,
FT                   ECO:0000269|PubMed:19621959, ECO:0007744|PDB:2KDX"
FT   MUTAGEN         2
FT                   /note="H->A: Cannot bind nickel. Lacks hydrogenase activity
FT                   and has only 2% of the urease activity."
FT                   /evidence="ECO:0000269|PubMed:12533448"
FT   MUTAGEN         17
FT                   /note="H->A: Does not affect nickel-binding ability."
FT                   /evidence="ECO:0000269|PubMed:12533448"
FT   MUTAGEN         24
FT                   /note="H->A: Does not affect nickel-binding ability."
FT                   /evidence="ECO:0000269|PubMed:12533448"
FT   MUTAGEN         79
FT                   /note="H->A: Does not affect nickel-binding ability."
FT                   /evidence="ECO:0000269|PubMed:12533448"
FT   MUTAGEN         95
FT                   /note="H->A: Does not affect nickel-binding ability."
FT                   /evidence="ECO:0000269|PubMed:12533448"
FT   HELIX           2..20
FT                   /evidence="ECO:0007829|PDB:2KDX"
FT   STRAND          28..34
FT                   /evidence="ECO:0007829|PDB:2KDX"
FT   HELIX           41..51
FT                   /evidence="ECO:0007829|PDB:2KDX"
FT   HELIX           52..54
FT                   /evidence="ECO:0007829|PDB:2KDX"
FT   TURN            56..58
FT                   /evidence="ECO:0007829|PDB:2KDX"
FT   STRAND          63..68
FT                   /evidence="ECO:0007829|PDB:2KDX"
FT   STRAND          71..73
FT                   /evidence="ECO:0007829|PDB:2KDX"
FT   STRAND          75..78
FT                   /evidence="ECO:0007829|PDB:2KDX"
FT   STRAND          92..96
FT                   /evidence="ECO:0007829|PDB:2KDX"
FT   STRAND          100..105
FT                   /evidence="ECO:0007829|PDB:2KDX"
FT   STRAND          108..113
FT                   /evidence="ECO:0007829|PDB:2KDX"
SQ   SEQUENCE   117 AA;  13202 MW;  BA67A69E2EC35506 CRC64;
     MHEYSVVSSL IALCEEHAKK NQAHKIERVV VGIGERSAMD KSLFVSAFET FREESLVCKD
     AILDIVDEKV ELECKDCSHV FKPNALDYGV CEKCHSKNVI ITQGNEMRLL SLEMLAE
 
 
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