HYPA_ECOLI
ID HYPA_ECOLI Reviewed; 116 AA.
AC P0A700; P24189; Q2MAA3;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Hydrogenase maturation factor HypA {ECO:0000305};
GN Name=hypA {ECO:0000303|PubMed:1849603}; OrderedLocusNames=b2726, JW2696;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1849603; DOI=10.1111/j.1365-2958.1991.tb01833.x;
RA Lutz S., Jacobi A., Schlensog V., Boehm R., Sawers G., Boeck A.;
RT "Molecular characterization of an operon (hyp) necessary for the activity
RT of the three hydrogenase isoenzymes in Escherichia coli.";
RL Mol. Microbiol. 5:123-135(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=1482271; DOI=10.1007/bf00276307;
RA Jacobi A., Rossmann R., Boeck A.;
RT "The hyp operon gene products are required for the maturation of
RT catalytically active hydrogenase isoenzymes in Escherichia coli.";
RL Arch. Microbiol. 158:444-451(1992).
RN [5]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12081959; DOI=10.1128/jb.184.14.3879-3885.2002;
RA Hube M., Blokesch M., Boeck A.;
RT "Network of hydrogenase maturation in Escherichia coli: role of accessory
RT proteins HypA and HybF.";
RL J. Bacteriol. 184:3879-3885(2002).
RN [7]
RP FUNCTION, SUBUNIT, INTERACTION WITH HYPB, NICKEL-BINDING, AND ZINC-BINDING.
RX PubMed=15995183; DOI=10.1128/jb.187.14.4689-4697.2005;
RA Atanassova A., Zamble D.B.;
RT "Escherichia coli HypA is a zinc metalloprotein with a weak affinity for
RT nickel.";
RL J. Bacteriol. 187:4689-4697(2005).
RN [8]
RP FUNCTION, INTERACTION WITH HYPB; SLYD AND HYCE, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF HIS-2.
RX PubMed=22016389; DOI=10.1074/jbc.m111.290726;
RA Chan Chung K.C., Zamble D.B.;
RT "Protein interactions and localization of the Escherichia coli accessory
RT protein HypA during nickel insertion to [NiFe] hydrogenase.";
RL J. Biol. Chem. 286:43081-43090(2011).
RN [9]
RP FUNCTION, AND INTERACTION WITH HYPB.
RX PubMed=23899293; DOI=10.1021/bi400812r;
RA Douglas C.D., Ngu T.T., Kaluarachchi H., Zamble D.B.;
RT "Metal transfer within the Escherichia coli HypB-HypA complex of
RT hydrogenase accessory proteins.";
RL Biochemistry 52:6030-6039(2013).
RN [10]
RP FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF HIS-2.
RX PubMed=27951644; DOI=10.1021/acs.biochem.6b00706;
RA Lacasse M.J., Douglas C.D., Zamble D.B.;
RT "Mechanism of selective nickel transfer from HypB to HypA, Escherichia coli
RT [NiFe]-hydrogenase accessory proteins.";
RL Biochemistry 55:6821-6831(2016).
CC -!- FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Required
CC for nickel insertion into the metal center of the hydrogenase
CC (PubMed:12081959, PubMed:15995183). Mediates transfer of nickel, but
CC not zinc, from the low-affinity metal-binding site in the GTPase domain
CC of HypB to HypA (PubMed:23899293, PubMed:27951644). HypA is involved in
CC maturation of hydrogenase 3. It may partially substitute for the
CC function of HybF and vice versa (PubMed:12081959). May act as a
CC scaffold for assembly of the nickel insertion proteins with the
CC hydrogenase precursor protein after delivery of the iron center
CC (PubMed:22016389). {ECO:0000269|PubMed:12081959,
CC ECO:0000269|PubMed:15995183, ECO:0000269|PubMed:22016389,
CC ECO:0000269|PubMed:23899293, ECO:0000269|PubMed:27951644}.
CC -!- ACTIVITY REGULATION: GDP-loaded state of HypB enhances HypA-HypB
CC complex formation and nickel transfer. {ECO:0000269|PubMed:27951644}.
CC -!- SUBUNIT: Homodimer (PubMed:15995183). Forms complexes with HypB and
CC SlyD, and interacts with HycE, the large subunit of hydrogenase 3
CC (PubMed:15995183, PubMed:22016389, PubMed:23899293).
CC {ECO:0000269|PubMed:15995183, ECO:0000269|PubMed:22016389,
CC ECO:0000269|PubMed:23899293}.
CC -!- INTERACTION:
CC P0A700; P16431: hycE; NbExp=14; IntAct=EBI-6290024, EBI-552702;
CC P0A700; P0A700: hypA; NbExp=4; IntAct=EBI-6290024, EBI-6290024;
CC P0A700; P0AAN3: hypB; NbExp=9; IntAct=EBI-6290024, EBI-558261;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:22016389}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene prevents development of
CC hydrogenase 3 activity, does not influence the level of hydrogenase 1
CC and leads to a considerable increase in hydrogenase 2 activity
CC (PubMed:1482271). HypA-hybF double mutant is completely blocked in
CC maturation of hydrogenases 1, 2 and 3. However, the inclusion of high
CC nickel concentrations in the medium can restore limited activity of all
CC three hydrogenases (PubMed:12081959). {ECO:0000269|PubMed:12081959,
CC ECO:0000269|PubMed:1482271}.
CC -!- SIMILARITY: Belongs to the HypA/HybF family. {ECO:0000255|HAMAP-
CC Rule:MF_00213, ECO:0000305}.
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DR EMBL; X54543; CAA38412.1; -; Genomic_DNA.
DR EMBL; U29579; AAA69236.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75768.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76803.1; -; Genomic_DNA.
DR PIR; S15197; S15197.
DR RefSeq; NP_417206.1; NC_000913.3.
DR RefSeq; WP_001299100.1; NZ_STEB01000027.1.
DR AlphaFoldDB; P0A700; -.
DR SMR; P0A700; -.
DR BioGRID; 4261428; 8.
DR BioGRID; 851527; 1.
DR ComplexPortal; CPX-5056; HypAB Ni-hydrogenase maturation complex.
DR DIP; DIP-48022N; -.
DR IntAct; P0A700; 9.
DR STRING; 511145.b2726; -.
DR PaxDb; P0A700; -.
DR PRIDE; P0A700; -.
DR EnsemblBacteria; AAC75768; AAC75768; b2726.
DR EnsemblBacteria; BAE76803; BAE76803; BAE76803.
DR GeneID; 66673405; -.
DR GeneID; 947195; -.
DR KEGG; ecj:JW2696; -.
DR KEGG; eco:b2726; -.
DR PATRIC; fig|1411691.4.peg.4015; -.
DR EchoBASE; EB0478; -.
DR eggNOG; COG0375; Bacteria.
DR HOGENOM; CLU_126929_0_0_6; -.
DR InParanoid; P0A700; -.
DR OMA; EEQQAEC; -.
DR PhylomeDB; P0A700; -.
DR BioCyc; EcoCyc:EG10483-MON; -.
DR BioCyc; MetaCyc:EG10483-MON; -.
DR PRO; PR:P0A700; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:EcoCyc.
DR GO; GO:1905360; C:GTPase complex; IPI:ComplexPortal.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016151; F:nickel cation binding; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0051604; P:protein maturation; IMP:EcoCyc.
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 Cell inner membrane; Cell membrane; Membrane; Metal-binding; Nickel;
KW Reference proteome; Zinc.
FT CHAIN 1..116
FT /note="Hydrogenase maturation factor HypA"
FT /id="PRO_0000129057"
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:27951644"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00213"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00213"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00213"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00213"
FT MUTAGEN 2
FT /note="H->A: Does not affect interaction with HycE."
FT /evidence="ECO:0000269|PubMed:22016389"
FT MUTAGEN 2
FT /note="H->Q: Can bind nickel, but with reduced affinity.
FT Decreases nickel transfer from HypB and cannot support
FT hydrogenase maturation."
FT /evidence="ECO:0000269|PubMed:27951644"
SQ SEQUENCE 116 AA; 13168 MW; 57458941783073D4 CRC64;
MHEITLCQRA LELIEQQAAK HGAKRVTGVW LKIGAFSCVE TSSLAFCFDL VCRGSVAEGC
KLHLEEQEAE CWCETCQQYV TLLTQRVRRC PQCHGDMLQI VADDGLQIRR IEIDQE
