HYBF_ECOLI
ID HYBF_ECOLI Reviewed; 113 AA.
AC P0A703; P37184; Q2M9K4; Q46846;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Hydrogenase maturation factor HybF {ECO:0000255|HAMAP-Rule:MF_02099, ECO:0000305};
DE AltName: Full=Hydrogenase nickel incorporation protein HybF {ECO:0000305};
DE AltName: Full=Hydrogenase-2 operon protein HybF {ECO:0000305};
GN Name=hybF {ECO:0000255|HAMAP-Rule:MF_02099, ECO:0000303|PubMed:8021226};
GN OrderedLocusNames=b2991, JW5493;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / TG1;
RX PubMed=8021226; DOI=10.1128/jb.176.14.4416-4423.1994;
RA Menon N.K., Chatelus C.Y., Dervartanian M., Wendt J.C., Shanmugam K.T.,
RA Peck H.D. Jr., Przybyla A.E.;
RT "Cloning, sequencing, and mutational analysis of the hyb operon encoding
RT Escherichia coli hydrogenase 2.";
RL J. Bacteriol. 176:4416-4423(1994).
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 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 [5]
RP SUBUNIT, NICKEL-BINDING, ZINC-BINDING, AND MUTAGENESIS OF HIS-2; GLU-3;
RP CYS-73; CYS-76; CYS-89; PRO-90 AND CYS-92.
RX PubMed=15090500; DOI=10.1128/jb.186.9.2603-2611.2004;
RA Blokesch M., Rohrmoser M., Rode S., Boeck A.;
RT "HybF, a zinc-containing protein involved in NiFe hydrogenase maturation.";
RL J. Bacteriol. 186:2603-2611(2004).
CC -!- FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Required
CC for nickel insertion into the metal center of the hydrogenase. HybF is
CC involved in maturation of hydrogenases 1 and 2. It may partially
CC substitute for the function of HypA and vice versa.
CC {ECO:0000269|PubMed:12081959}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15090500}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene severely reduces hydrogenase
CC 1 and hydrogenase 2 activity (PubMed:12081959). HypA-hybF double mutant
CC is completely blocked in maturation of hydrogenases 1, 2 and 3.
CC However, the inclusion of high nickel concentrations in the medium can
CC restore limited activity of all three hydrogenases (PubMed:12081959).
CC {ECO:0000269|PubMed:12081959}.
CC -!- SIMILARITY: Belongs to the HypA/HybF family. HybF subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02099, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA21594.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; U09177; AAA21594.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U28377; AAA69158.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76027.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77052.1; -; Genomic_DNA.
DR PIR; F55516; F55516.
DR RefSeq; NP_417465.1; NC_000913.3.
DR RefSeq; WP_000544953.1; NZ_STEB01000001.1.
DR AlphaFoldDB; P0A703; -.
DR SMR; P0A703; -.
DR BioGRID; 4261537; 5.
DR IntAct; P0A703; 1.
DR STRING; 511145.b2991; -.
DR PaxDb; P0A703; -.
DR PRIDE; P0A703; -.
DR EnsemblBacteria; AAC76027; AAC76027; b2991.
DR EnsemblBacteria; BAE77052; BAE77052; BAE77052.
DR GeneID; 58459877; -.
DR GeneID; 948004; -.
DR KEGG; ecj:JW5493; -.
DR KEGG; eco:b2991; -.
DR PATRIC; fig|1411691.4.peg.3738; -.
DR EchoBASE; EB1752; -.
DR eggNOG; COG0375; Bacteria.
DR HOGENOM; CLU_126929_0_0_6; -.
DR InParanoid; P0A703; -.
DR OMA; ILLCPCG; -.
DR PhylomeDB; P0A703; -.
DR BioCyc; EcoCyc:EG11804-MON; -.
DR PRO; PR:P0A703; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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_02099; HybF_subfam; 1.
DR HAMAP; MF_00213; HypA_HybF; 1.
DR InterPro; IPR039002; HybF.
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 Metal-binding; Nickel; Reference proteome; Zinc.
FT CHAIN 1..113
FT /note="Hydrogenase maturation factor HybF"
FT /id="PRO_0000129063"
FT BINDING 2
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02099,
FT ECO:0000305|PubMed:15090500"
FT BINDING 3
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02099,
FT ECO:0000305|PubMed:15090500"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02099,
FT ECO:0000305|PubMed:15090500"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02099,
FT ECO:0000305|PubMed:15090500"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02099,
FT ECO:0000305|PubMed:15090500"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02099,
FT ECO:0000305|PubMed:15090500"
FT MUTAGEN 2
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15090500"
FT MUTAGEN 2
FT /note="H->Q: Loss of activity. Does not affect the amount
FT of zinc, but shows a strong decrease in nickel content."
FT /evidence="ECO:0000269|PubMed:15090500"
FT MUTAGEN 3
FT /note="E->L: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15090500"
FT MUTAGEN 3
FT /note="E->Q: Does not affect activity."
FT /evidence="ECO:0000269|PubMed:15090500"
FT MUTAGEN 73
FT /note="C->A: Affects stability and solubility of the
FT protein, but mutant is still active."
FT /evidence="ECO:0000269|PubMed:15090500"
FT MUTAGEN 76
FT /note="C->A: Affects stability and solubility of the
FT protein, but mutant is still active."
FT /evidence="ECO:0000269|PubMed:15090500"
FT MUTAGEN 89
FT /note="C->A,S: Affects stability and solubility of the
FT protein, but mutant is still active."
FT /evidence="ECO:0000269|PubMed:15090500"
FT MUTAGEN 90
FT /note="P->A: Does not affect activity."
FT /evidence="ECO:0000269|PubMed:15090500"
FT MUTAGEN 92
FT /note="C->A: Affects stability and solubility of the
FT protein, but mutant is still active."
FT /evidence="ECO:0000269|PubMed:15090500"
SQ SEQUENCE 113 AA; 12697 MW; 70919C4A40CEABE6 CRC64;
MHELSLCQSA VEIIQRQAEQ HDVKRVTAVW LEIGALSCVE ESAVRFSFEI VCHGTVAQGC
DLHIVYKPAQ AWCWDCSQVV EIHQHDAQCP LCHGERLRVD TGDSLIVKSI EVE
