ID   HYPB_RHOCA              Reviewed;         335 AA.
AC   P26410;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Hydrogenase maturation factor HypB {ECO:0000250|UniProtKB:P0AAN3};
GN   Name=hypB; Synonyms=hupM;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33303 / B10;
RX   PubMed=8497190; DOI=10.1111/j.1365-2958.1993.tb01199.x;
RA   Colbeau A., Richaud P., Toussaint B., Caballero F.J., Elster C.,
RA   Delphin C., Smith R.L., Chabert J., Vignais P.M.;
RT   "Organization of the genes necessary for hydrogenase expression in
RT   Rhodobacter capsulatus. Sequence analysis and identification of two hyp
RT   regulatory mutants.";
RL   Mol. Microbiol. 8:15-29(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2007559; DOI=10.1128/jb.173.7.2401-2405.1991;
RA   Xu H.-W., Wall J.D.;
RT   "Clustering of genes necessary for hydrogen oxidation in Rhodobacter
RT   capsulatus.";
RL   J. Bacteriol. 173:2401-2405(1991).
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; X61007; CAA43326.1; -; Genomic_DNA.
DR   EMBL; M55089; AAA72926.1; -; Genomic_DNA.
DR   PIR; D38532; D38532.
DR   AlphaFoldDB; P26410; -.
DR   SMR; P26410; -.
DR   OMA; ECHLDAH; -.
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; 1.
DR   Pfam; PF02492; cobW; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00073; hypB; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Hydrolase; Metal-binding; Nickel; Nucleotide-binding; Zinc.
FT   CHAIN           1..335
FT                   /note="Hydrogenase maturation factor HypB"
FT                   /id="PRO_0000201439"
FT   REGION          36..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..309
FT                   /note="G-domain"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT   COMPBIAS        45..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..99
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         208
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT   BINDING         209
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT   BINDING         209
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT   BINDING         240
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT   BINDING         240
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAN3"
SQ   SEQUENCE   335 AA;  35343 MW;  B7276C3E1AA0FD02 CRC64;
     MCTVCGCGGH SVEDQFKAHL KSQGKDGAHK PAPFAVLAEP QGPHSHSHSH WHTHADGTSH
     AHPHAHSHSH AAGHGAEADS DHPHAHGHDH GHSHGACAHD IHLGHGPAGT EVPGMSQARL
     IEIETDILSK NNQYAARNRA ALAKNCTFAT NLVSSPGSGK TTLLVKTIEM LGAQPLAVIE
     GDQQTTNDAD RIRATGAPAI QVNTGKGCHL DGAMVEQALA HLPLPAGALL FIENVGNLVC
     PAAFDLGEDA KVAILSVTEG EDKPLKYPDM FAAAGLAILN KVDLAPYCDV DLDLYEANIR
     RVNPQIEVLR VSARTGDGMG AWIDWLRAGL ARKAR