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Protein

Hydrogenase maturation factor HypB

Gene

hypB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase (PubMed:7601092, PubMed:8756471). Exhibits a low intrinsic GTPase activity, which is essential for nickel insertion (PubMed:7601092, PubMed:21544686, PubMed:27951644). In the presence of GDP, nickel, but not zinc, is transferred from the HypB GTPase domain (G-domain) to HypA (PubMed:23899293, PubMed:27951644).5 Publications

Enzyme regulationi

Binding of zinc or nickel in the G-domain decreases GTPase activity (PubMed:21544686). Once GTP hydrolysis is triggered, probably via a GTPase activating protein, the GDP-loaded state may enhance HypA-HypB complex formation and reduces the affinity of HypB for nickel, which is then transferred to HypA (PubMed:27951644). In contrast to nickel, zinc reduces the formation of complexes with HypA (PubMed:27951644).2 Publications

Kineticsi

kcat is 0.18 min(-1) for GTPase activity. kcat is 0.04 min1 for GTPase activity in the presence of 1 µM Zn(II). kcat is 0.10 min(-1) for GTPase activity in the presence of 10 µM Ni(II).1 Publication

      Sites

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      Metal bindingi2Nickel 12 Publications1
      Metal bindingi5Nickel 12 Publications1
      Metal bindingi7Nickel 12 Publications1
      Metal bindingi166Nickel 2 or zinc2 Publications1
      Metal bindingi167Nickel 2 or zinc2 Publications1
      Metal bindingi198Nickel 2 or zinc1 Publication1

      GO - Molecular functioni

      • GTPase activity Source: EcoCyc
      • GTP binding Source: UniProtKB-KW
      • nickel cation binding Source: EcoCyc
      • zinc ion binding Source: EcoCyc

      GO - Biological processi

      • cofactor biosynthetic process Source: EcoCyc
      • protein maturation Source: EcoCyc

      Keywordsi

      Molecular functionHydrolase
      LigandGTP-binding, Metal-binding, Nickel, Nucleotide-binding, Zinc

      Enzyme and pathway databases

      BioCyciEcoCyc:EG10484-MONOMER
      MetaCyc:EG10484-MONOMER

      Names & Taxonomyi

      Protein namesi
      Recommended name:
      Hydrogenase maturation factor HypBCurated
      Alternative name(s):
      Hydrogenase isoenzymes nickel incorporation protein HypBCurated
      Gene namesi
      Name:hypB
      Ordered Locus Names:b2727, JW2697
      OrganismiEscherichia coli (strain K12)
      Taxonomic identifieri83333 [NCBI]
      Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
      Proteomesi
      • UP000000318 Componenti: Chromosome
      • UP000000625 Componenti: Chromosome

      Organism-specific databases

      EcoGeneiEG10484 hypB

      Pathology & Biotechi

      Mutagenesis

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      Mutagenesisi2C → A: Decreases nickel content. Disruption of the N-terminal metal-binding site; when associated with A-5 and A-7. 1 Publication1
      Mutagenesisi5C → A: Decreases nickel content. Disruption of the N-terminal metal-binding site; when associated with A-3 and A-7. 1 Publication1
      Mutagenesisi7C → A: Decreases nickel content. Decreases hydrogenase activity of the cell. Disruption of the N-terminal metal-binding site; when associated with A-3 and A-5. 2 Publications1
      Mutagenesisi78 – 80LEV → AEA: Disrupts interaction with HypA. Can only partially restore hydrogenase production in a hypB deletion mutant. 1 Publication3
      Mutagenesisi117K → N: Important decrease in GTPase activity. 1 Publication1
      Mutagenesisi166C → A: Does not affect nickel content. Mutant lacks hydrogenase activity. 2 Publications1
      Mutagenesisi167H → A: Does not affect nickel content. Mutant lacks hydrogenase activity. 2 Publications1
      Mutagenesisi198C → A: Does not affect nickel content. 1 Publication1
      Mutagenesisi241D → N: 85-fold decrease in kcat/KM value of GTPase activity and loss of the specificity for GTP. 1 Publication1
      Mutagenesisi242L → A: Cannot form dimers. Can still bind metal in both sites and activate GTP hydrolysis, but hydrogenase activity of the cell is decreased; when associated with A-246. 1 Publication1
      Mutagenesisi246L → A: Cannot form dimers. Can still bind metal in both sites and activate GTP hydrolysis, but hydrogenase activity of the cell is decreased; when associated with A-242. 1 Publication1

      PTM / Processingi

      Molecule processing

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      ChainiPRO_00002014401 – 290Hydrogenase maturation factor HypBAdd BLAST290

      Proteomic databases

      PaxDbiP0AAN3
      PRIDEiP0AAN3

      2D gel databases

      SWISS-2DPAGEiP0AAN3

      Interactioni

      Subunit structurei

      Monomer (PubMed:21544686). Can form homodimers, but dimerization does not have a critical role in the hydrogenase maturation pathway (PubMed:21544686). Forms complexes with HypA and SlyD (PubMed:15995183, PubMed:15569666, PubMed:23899293).4 Publications

      Binary interactionsi

      WithEntry#Exp.IntActNotes
      slyDP0A9K96EBI-558261,EBI-369251

      Protein-protein interaction databases

      BioGridi4261427, 13 interactors
      DIPiDIP-36428N
      IntActiP0AAN3, 9 interactors
      MINTiP0AAN3
      STRINGi316385.ECDH10B_2895

      Structurei

      3D structure databases

      ProteinModelPortaliP0AAN3
      SMRiP0AAN3
      ModBaseiSearch...
      MobiDBiSearch...

      Family & Domainsi

      Region

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      Regioni106 – 267G-domainCuratedAdd BLAST162

      Domaini

      The N-terminal region contains a high-affinity nickel-binding site and the C-terminal G-domain contains a low-affinity metal-binding site, which is not selective for nickel and could possibly accommodate other divalent metals (PubMed:16142921, PubMed:18942856). Both metal sites are critical for the maturation of the hydrogenases (PubMed:18942856).2 Publications

      Sequence similaritiesi

      Phylogenomic databases

      eggNOGiENOG4107RSS Bacteria
      COG0378 LUCA
      HOGENOMiHOG000236980
      InParanoidiP0AAN3
      KOiK04652
      OMAiECHLDAH
      PhylomeDBiP0AAN3

      Family and domain databases

      InterProiView protein in InterPro
      IPR003495 CobW/HypB/UreG_dom
      IPR004392 Hyd_mat_HypB
      IPR012202 NiFe-hyd/urease_mat_GTPase
      IPR027417 P-loop_NTPase
      PANTHERiPTHR30134:SF2 PTHR30134:SF2, 1 hit
      PfamiView protein in Pfam
      PF02492 cobW, 1 hit
      PIRSFiPIRSF005624 Ni-bind_GTPase, 1 hit
      SUPFAMiSSF52540 SSF52540, 1 hit
      TIGRFAMsiTIGR00073 hypB, 1 hit

      Sequencei

      Sequence statusi: Complete.

      P0AAN3-1 [UniParc]FASTAAdd to basket

      « Hide

              10         20         30         40         50
      MCTTCGCGEG NLYIEGDEHN PHSAFRSAPF APAARPKMKI TGIKAPEFTP
      60 70 80 90 100
      SQTEEGDLHY GHGEAGTHAP GMSQRRMLEV EIDVLDKNNR LAERNRARFA
      110 120 130 140 150
      ARKQLVLNLV SSPGSGKTTL LTETLMRLKD SVPCAVIEGD QQTVNDAARI
      160 170 180 190 200
      RATGTPAIQV NTGKGCHLDA QMIADAAPRL PLDDNGILFI ENVGNLVCPA
      210 220 230 240 250
      SFDLGEKHKV AVLSVTEGED KPLKYPHMFA AASLMLLNKV DLLPYLNFDV
      260 270 280 290
      EKCIACAREV NPEIEIILIS ATSGEGMDQW LNWLETQRCA
      Length:290
      Mass (Da):31,565
      Last modified:October 11, 2005 - v1
      Checksum:i5B3AEB59AA6915C3
      GO

      Experimental Info

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      Sequence conflicti36P → R in CAA38413 (PubMed:1849603).Curated1

      Sequence databases

      Select the link destinations:
      EMBLi
      GenBanki
      DDBJi
      Links Updated
      X54543 Genomic DNA Translation: CAA38413.1
      U29579 Genomic DNA Translation: AAA69237.1
      U00096 Genomic DNA Translation: AAC75769.1
      AP009048 Genomic DNA Translation: BAE76804.1
      PIRiC65053
      RefSeqiNP_417207.1, NC_000913.3
      WP_000337665.1, NZ_LN832404.1

      Genome annotation databases

      EnsemblBacteriaiAAC75769; AAC75769; b2727
      BAE76804; BAE76804; BAE76804
      GeneIDi947194
      KEGGiecj:JW2697
      eco:b2727
      PATRICifig|1411691.4.peg.4014

      Similar proteinsi

      Entry informationi

      Entry nameiHYPB_ECOLI
      AccessioniPrimary (citable) accession number: P0AAN3
      Secondary accession number(s): P24190, Q2MAA2, Q46884
      Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2005
      Last sequence update: October 11, 2005
      Last modified: April 25, 2018
      This is version 88 of the entry and version 1 of the sequence. See complete history.
      Entry statusiReviewed (UniProtKB/Swiss-Prot)
      Annotation programProkaryotic Protein Annotation Program

      Miscellaneousi

      Keywords - Technical termi

      Complete proteome, Direct protein sequencing, Reference proteome
      UniProt is an ELIXIR core data resource
      Main funding by: National Institutes of Health