HYPB_CUPNH
ID HYPB_CUPNH Reviewed; 361 AA.
AC P31902;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Hydrogenase maturation factor HypB {ECO:0000250|UniProtKB:P0AAN3};
GN Name=hypB; OrderedLocusNames=PHG013;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OG Plasmid megaplasmid pHG1.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8352644; DOI=10.1007/bf00249034;
RA Dernedde J., Eitinger M., Friedrich B.;
RT "Analysis of a pleiotropic gene region involved in formation of
RT catalytically active hydrogenases in Alcaligenes eutrophus H16.";
RL Arch. Microbiol. 159:545-553(1993).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=8631353; DOI=10.1111/j.1432-1033.1996.00351.x;
RA Dernedde J., Eitinger T., Patenge N., Friedrich B.;
RT "hyp gene products in Alcaligenes eutrophus are part of a hydrogenase-
RT maturation system.";
RL Eur. J. Biochem. 235:351-358(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=12948488; DOI=10.1016/s0022-2836(03)00894-5;
RA Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.;
RT "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid
RT encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis.";
RL J. Mol. Biol. 332:369-383(2003).
CC -!- FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Required
CC for nickel insertion into the metal center of the hydrogenase. Exhibits
CC a low intrinsic GTPase activity, which is essential for nickel
CC insertion. {ECO:0000250|UniProtKB:P0AAN3}.
CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. HypB/HupM
CC subfamily. {ECO:0000305}.
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DR EMBL; X70183; CAA49732.1; -; Genomic_DNA.
DR EMBL; AY305378; AAP85769.1; -; Genomic_DNA.
DR PIR; I39529; I39529.
DR RefSeq; WP_011153938.1; NZ_CP039289.1.
DR AlphaFoldDB; P31902; -.
DR SMR; P31902; -.
DR STRING; 381666.PHG013; -.
DR EnsemblBacteria; AAP85769; AAP85769; PHG013.
DR GeneID; 39976468; -.
DR KEGG; reh:PHG013; -.
DR PATRIC; fig|381666.6.peg.9; -.
DR eggNOG; COG0378; Bacteria.
DR HOGENOM; CLU_056148_1_0_4; -.
DR OMA; ECHLDAH; -.
DR OrthoDB; 1134430at2; -.
DR Proteomes; UP000008210; Plasmid megaplasmid pHG1.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR GO; GO:0051604; P:protein maturation; IEA:InterPro.
DR CDD; cd05390; HypB; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003495; CobW/HypB/UreG_dom.
DR InterPro; IPR004392; Hyd_mat_HypB.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR30134; PTHR30134; 2.
DR Pfam; PF02492; cobW; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00073; hypB; 2.
PE 3: Inferred from homology;
KW GTP-binding; Hydrolase; Metal-binding; Nickel; Nucleotide-binding; Plasmid;
KW Reference proteome; Zinc.
FT CHAIN 1..361
FT /note="Hydrogenase maturation factor HypB"
FT /id="PRO_0000201434"
FT REGION 14..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..300
FT /note="G-domain"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT REGION 183..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 5
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 7
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 162
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 163
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 231
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
SQ SEQUENCE 361 AA; 38483 MW; BC42976B7C5F75C4 CRC64;
MCVICGCNTN HETARQDENK GEHAPGRGLV DTGTEPPGAA HVRIDASTGD LHYGAGPAHV
SVPGLSQARA IKLEQDVLGH NNRLAAHNRQ HFVAHGVLAL NLVSSPGSGK TTLLCTTIEA
LRRCRADLQL AVIEGDQQTS HDAERIRATG VPAIQINTGK GCHLDALMVA NAYERLPLHA
AAHAHTHEHR QEDGQHSHHH DHEHARHDHH DHRSSGIGSV LFIENVGNLV CPAMWDLGES
AKVAILSVTE GEDKPLKYPD MFAAASLMIL NKIDLLPHLR FDVARCIEYA RQVNPHLQVL
QLSAATGEGV DEWLDWMLAG GAAAGAAAAT DGARMRIAAP EAGIAALGTQ LAPGPAVSKE
M
