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HYPB_METJA
ID   HYPB_METJA              Reviewed;         221 AA.
AC   Q57884;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Probable hydrogenase maturation factor HypB {ECO:0000305};
GN   Name=hypB {ECO:0000303|PubMed:16807243}; OrderedLocusNames=MJ0442;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2] {ECO:0007744|PDB:2HF8, ECO:0007744|PDB:2HF9}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ZINC, AND SUBUNIT.
RX   PubMed=16807243; DOI=10.1074/jbc.m600809200;
RA   Gasper R., Scrima A., Wittinghofer A.;
RT   "Structural insights into HypB, a GTP-binding protein that regulates metal
RT   binding.";
RL   J. Biol. Chem. 281:27492-27502(2006).
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   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16807243}.
CC   -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. HypB/HupM
CC       subfamily. {ECO:0000305}.
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DR   EMBL; L77117; AAB98429.1; -; Genomic_DNA.
DR   PIR; B64355; B64355.
DR   RefSeq; WP_010869941.1; NC_000909.1.
DR   PDB; 2HF8; X-ray; 2.10 A; A/B=1-221.
DR   PDB; 2HF9; X-ray; 1.90 A; A/B=1-221.
DR   PDBsum; 2HF8; -.
DR   PDBsum; 2HF9; -.
DR   AlphaFoldDB; Q57884; -.
DR   SMR; Q57884; -.
DR   STRING; 243232.MJ_0442; -.
DR   EnsemblBacteria; AAB98429; AAB98429; MJ_0442.
DR   GeneID; 1451302; -.
DR   KEGG; mja:MJ_0442; -.
DR   eggNOG; arCOG01231; Archaea.
DR   HOGENOM; CLU_056148_0_1_2; -.
DR   InParanoid; Q57884; -.
DR   OMA; ECHLDAH; -.
DR   OrthoDB; 76245at2157; -.
DR   PhylomeDB; Q57884; -.
DR   EvolutionaryTrace; Q57884; -.
DR   Proteomes; UP000000805; 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   1: Evidence at protein level;
KW   3D-structure; GTP-binding; Hydrolase; Metal-binding; Nickel;
KW   Nucleotide-binding; Reference proteome; Zinc.
FT   CHAIN           1..221
FT                   /note="Probable hydrogenase maturation factor HypB"
FT                   /id="PRO_0000201445"
FT   REGION          35..196
FT                   /note="G-domain"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT   BINDING         95
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250|UniProtKB:O25560"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:16807243,
FT                   ECO:0007744|PDB:2HF8"
FT   BINDING         96
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250|UniProtKB:O25560"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:16807243,
FT                   ECO:0007744|PDB:2HF8"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:16807243,
FT                   ECO:0007744|PDB:2HF8, ECO:0007744|PDB:2HF9"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:16807243,
FT                   ECO:0007744|PDB:2HF8, ECO:0007744|PDB:2HF9"
FT   BINDING         127
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000250|UniProtKB:O25560"
FT   BINDING         127
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:16807243,
FT                   ECO:0007744|PDB:2HF8"
FT   HELIX           13..30
FT                   /evidence="ECO:0007829|PDB:2HF9"
FT   STRAND          34..41
FT                   /evidence="ECO:0007829|PDB:2HF9"
FT   HELIX           46..57
FT                   /evidence="ECO:0007829|PDB:2HF9"
FT   TURN            58..60
FT                   /evidence="ECO:0007829|PDB:2HF9"
FT   STRAND          63..69
FT                   /evidence="ECO:0007829|PDB:2HF9"
FT   TURN            70..72
FT                   /evidence="ECO:0007829|PDB:2HF9"
FT   HELIX           73..80
FT                   /evidence="ECO:0007829|PDB:2HF9"
FT   TURN            81..83
FT                   /evidence="ECO:0007829|PDB:2HF9"
FT   STRAND          85..90
FT                   /evidence="ECO:0007829|PDB:2HF9"
FT   HELIX           99..106
FT                   /evidence="ECO:0007829|PDB:2HF9"
FT   HELIX           111..113
FT                   /evidence="ECO:0007829|PDB:2HF9"
FT   STRAND          115..120
FT                   /evidence="ECO:0007829|PDB:2HF9"
FT   HELIX           127..130
FT                   /evidence="ECO:0007829|PDB:2HF9"
FT   STRAND          136..143
FT                   /evidence="ECO:0007829|PDB:2HF9"
FT   HELIX           144..146
FT                   /evidence="ECO:0007829|PDB:2HF9"
FT   TURN            148..153
FT                   /evidence="ECO:0007829|PDB:2HF9"
FT   HELIX           155..158
FT                   /evidence="ECO:0007829|PDB:2HF9"
FT   STRAND          162..167
FT                   /evidence="ECO:0007829|PDB:2HF9"
FT   HELIX           169..171
FT                   /evidence="ECO:0007829|PDB:2HF9"
FT   HELIX           172..175
FT                   /evidence="ECO:0007829|PDB:2HF9"
FT   HELIX           179..189
FT                   /evidence="ECO:0007829|PDB:2HF9"
FT   STRAND          193..197
FT                   /evidence="ECO:0007829|PDB:2HF9"
FT   TURN            200..202
FT                   /evidence="ECO:0007829|PDB:2HF9"
FT   HELIX           206..219
FT                   /evidence="ECO:0007829|PDB:2HF9"
SQ   SEQUENCE   221 AA;  24340 MW;  0BB5415386A81138 CRC64;
     MHLVGVLDIA KDILKANKRL ADKNRKLLNK HGVVAFDFMG AIGSGKTLLI EKLIDNLKDK
     YKIACIAGDV IAKFDAERME KHGAKVVPLN TGKECHLDAH LVGHALEDLN LDEIDLLFIE
     NVGNLICPAD FDLGTHKRIV VISTTEGDDT IEKHPGIMKT ADLIVINKID LADAVGADIK
     KMENDAKRIN PDAEVVLLSL KTMEGFDKVL EFIEKSVKEV K
 
 
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