HYPB_BRADU
ID HYPB_BRADU Reviewed; 302 AA.
AC Q45257;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Hydrogenase maturation factor HypB {ECO:0000250|UniProtKB:P0AAN3};
GN Name=hypB; OrderedLocusNames=bll6931;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=8305450; DOI=10.1016/0005-2728(94)90163-5;
RA Fu C., Maier R.J.;
RT "Nucleotide sequences of two hydrogenase-related genes (hypA and hypB) from
RT Bradyrhizobium japonicum, one of which (hypB) encodes an extremely
RT histidine-rich region and guanine nucleotide-binding domains.";
RL Biochim. Biophys. Acta 1184:135-138(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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; L24513; AAA17763.1; -; Unassigned_DNA.
DR EMBL; BA000040; BAC52196.1; -; Genomic_DNA.
DR RefSeq; NP_773571.1; NC_004463.1.
DR RefSeq; WP_011089669.1; NZ_CP011360.1.
DR AlphaFoldDB; Q45257; -.
DR SMR; Q45257; -.
DR STRING; 224911.27355212; -.
DR EnsemblBacteria; BAC52196; BAC52196; BAC52196.
DR GeneID; 64026687; -.
DR KEGG; bja:bll6931; -.
DR PATRIC; fig|224911.44.peg.6965; -.
DR eggNOG; COG0378; Bacteria.
DR HOGENOM; CLU_056148_1_0_5; -.
DR InParanoid; Q45257; -.
DR OMA; ECHLDAH; -.
DR PhylomeDB; Q45257; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0016151; F:nickel cation binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0051604; P:protein maturation; IBA:GO_Central.
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;
KW Reference proteome; Zinc.
FT CHAIN 1..302
FT /note="Hydrogenase maturation factor HypB"
FT /id="PRO_0000201437"
FT REGION 18..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..269
FT /note="G-domain"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT COMPBIAS 31..47
FT /note="Basic 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 168
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 169
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 200
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT CONFLICT 72
FT /note="A -> T (in Ref. 1; AAA17763)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 302 AA; 32708 MW; D3B5F54F24AB90AA CRC64;
MCTVCGCSDG KASIEHAHDH HHDHGHDHDH GHDGHHHHHH GHDQDHHHHH DHAHGDAGLL
DCGANPAGQK IAGMSSDRII QVERDILGKN DRLAADNRAR FRADEVLAFN LVSSPGAGKT
SLLVRAVSEL KDSFAIGVIE GDQQTSNDAE RIRATGVPAI QVNTGKGCHL DAAMVGEAYD
RLPWLNGGLL FIENVGNLVC PAAFDLGEAC KIVVFSTTEG EDKPLKYPDM FAASSLMLIN
KIDLASVLDF DLARTIEYAR RVNPKIEVLT LSARTGEGFA AFYAWIRKRM AATTPAAMTA
AE
