ID   HYPB_SYNY3              Reviewed;         285 AA.
AC   P74218;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Hydrogenase maturation factor HypB {ECO:0000250|UniProtKB:P0AAN3};
GN   Name=hypB; OrderedLocusNames=sll1432;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA18312.1; -; Genomic_DNA.
DR   PIR; S75853; S75853.
DR   AlphaFoldDB; P74218; -.
DR   SMR; P74218; -.
DR   STRING; 1148.1653398; -.
DR   PaxDb; P74218; -.
DR   EnsemblBacteria; BAA18312; BAA18312; BAA18312.
DR   KEGG; syn:sll1432; -.
DR   eggNOG; COG0378; Bacteria.
DR   InParanoid; P74218; -.
DR   OMA; ECHLDAH; -.
DR   PhylomeDB; P74218; -.
DR   Proteomes; UP000001425; 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..285
FT                   /note="Hydrogenase maturation factor HypB"
FT                   /id="PRO_0000201444"
FT   REGION          16..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          90..251
FT                   /note="G-domain"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT   COMPBIAS        16..43
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         150
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT   BINDING         150
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT   BINDING         151
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT   BINDING         151
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT   BINDING         182
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAN3"
FT   BINDING         182
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAN3"
SQ   SEQUENCE   285 AA;  31243 MW;  02A078B4A034BA86 CRC64;
     MCQNCGCSAV GTVAHSHHHH GDGNFAHSHD DHDQQEHHHH HGNYSKSPSQ QTVTIEPDRQ
     SIAIGQGILS KNDRLAERNR GYFQAKGLLV MNFLSSPGAG KTALIEKMVG DRQKDHPTAV
     IVGDLATDND AQRLRSAGAI AIQVTTGNIC HLEAEMVAKA AQKLDLDNID QLIIENVGNL
     VCPTTYDLGE DLRVVLFSVT EGEDKPLKYP ATFKSAQVIL VTKQDIAAAV DFDAELAWQN
     LRQVAPQAQI FAVSARTGKG LQSWYEYLDQ WQLQHYSPLV DPALA