HYPB_RHILV
ID HYPB_RHILV Reviewed; 299 AA.
AC P28155;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Hydrogenase maturation factor HypB {ECO:0000250|UniProtKB:P0AAN3};
GN Name=hypB {ECO:0000303|PubMed:8326860}; Synonyms=hupM;
OS Rhizobium leguminosarum bv. viciae.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=387;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=128c53;
RX PubMed=8326860; DOI=10.1111/j.1365-2958.1993.tb01591.x;
RA Rey L., Murillo J., Hernando Y., Hidalgo E., Cabrera E., Imperial J.,
RA Ruiz-Argueso T.;
RT "Molecular analysis of a microaerobically induced operon required for
RT hydrogenase synthesis in Rhizobium leguminosarum biovar viciae.";
RL Mol. Microbiol. 8:471-481(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B10;
RA Brito B., Palacios J.M., Imperial J., Ruiz-Argueso T., Yang W.C.,
RA Bisseling T., Schmitt H., Kerl V., Bauer T., Kokotek W., Lotz W.;
RT "Organization of the hup-region and its differential transcription in non-
RT symbiotic and symbiotic cells of Rhizobium leguminosarum bv. viciae B10.";
RL Mol. Plant Microbe Interact. 8:235-240(1997).
RN [3]
RP PROTEIN SEQUENCE OF 2-13, FUNCTION, NICKEL-BINDING, DEVELOPMENTAL STAGE,
RP AND DOMAIN.
RX PubMed=7928968; DOI=10.1128/jb.176.19.6066-6073.1994;
RA Rey L., Imperial J., Palacios J.M., Ruiz-Argueeso T.;
RT "Purification of Rhizobium leguminosarum HypB, a nickel-binding protein
RT required for hydrogenase synthesis.";
RL J. Bacteriol. 176:6066-6073(1994).
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 (By similarity). Is able to bind 4 nickel ions per subunit.
CC Can also bind zinc (PubMed:7928968). {ECO:0000250|UniProtKB:P0AAN3,
CC ECO:0000269|PubMed:7928968}.
CC -!- DEVELOPMENTAL STAGE: Is synthesized in microaerobic vegetative cells
CC and pea bacteroids but not in aerobic vegetative cells.
CC {ECO:0000269|PubMed:7928968}.
CC -!- DOMAIN: A histidine-rich region at the N-terminus is proposed to play a
CC role in nickel binding, both in solution and in chelated form.
CC {ECO:0000269|PubMed:7928968}.
CC -!- DISRUPTION PHENOTYPE: Insertion mutant lacks any hydrogenase activity
CC in symbiosis with peas, but is still able to synthesize the polypeptide
CC for the hydrogenase large subunit. {ECO:0000269|PubMed:8326860}.
CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. HypB/HupM
CC subfamily. {ECO:0000305}.
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DR EMBL; X52974; CAA37160.1; -; Genomic_DNA.
DR EMBL; Z36981; CAA85442.1; -; Genomic_DNA.
DR PIR; S32874; S32874.
DR RefSeq; WP_026242367.1; NZ_SJNH01000008.1.
DR AlphaFoldDB; P28155; -.
DR SMR; P28155; -.
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 1: Evidence at protein level;
KW Direct protein sequencing; GTP-binding; Hydrolase; Metal-binding; Nickel;
KW Nucleotide-binding; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..299
FT /note="Hydrogenase maturation factor HypB"
FT /id="PRO_0000201438"
FT REGION 18..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..268
FT /note="G-domain"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
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 167
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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 199
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT CONFLICT 13
FT /note="E -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 299 AA; 32590 MW; 5B7A53059D92E87D CRC64;
MCTVCGCGTS AIEGHTHEVG DDGHGHHHHD GHHDHDHDHD HHRGDHEHDD HHHAEDGSVH
YSKGIAGVHV PGMSQERIIQ VEKDILSKND AYAAENRRHF ERQGVFALNF VSSPGSGKTS
LLVRTIKDLK DRLSISVIEG DQQTSNDAAR IRETGARAIQ INTGKGCHLD AHMVGHAVED
LAPEPGSALF IENVGNLVCP AAFDLGEAHK VVVLSVTEGE DKPLKYPDMF AAADLMILNK
ADLLPHLDFN TGFCIANALR VNPRLQTLTV SARTGEGMEA FYAWLEVSAA RRAIRSKVA
