ID HYPA_THEKO Reviewed; 139 AA.
AC Q5JIH3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Hydrogenase maturation factor HypA {ECO:0000305};
GN Name=hypA {ECO:0000303|PubMed:19769985}; OrderedLocusNames=TK2008;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
RN [2] {ECO:0007744|PDB:3A43, ECO:0007744|PDB:3A44}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH ZINC, AND SUBUNIT.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=19769985; DOI=10.1016/j.jmb.2009.09.030;
RA Watanabe S., Arai T., Matsumi R., Atomi H., Imanaka T., Miki K.;
RT "Crystal structure of HypA, a nickel-binding metallochaperone for [NiFe]
RT hydrogenase maturation.";
RL J. Mol. Biol. 394:448-459(2009).
RN [3] {ECO:0007744|PDB:5AUN, ECO:0007744|PDB:5AUO, ECO:0007744|PDB:5AUP}
RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) IN COMPLEXES WITH ZINC AND NICKEL,
RP AND INTERACTION WITH HYPB.
RX PubMed=26056269; DOI=10.1073/pnas.1503102112;
RA Watanabe S., Kawashima T., Nishitani Y., Kanai T., Wada T., Inaba K.,
RA Atomi H., Imanaka T., Miki K.;
RT "Structural basis of a Ni acquisition cycle for [NiFe] hydrogenase by Ni-
RT metallochaperone HypA and its enhancer.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:7701-7706(2015).
CC -!- FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Required
CC for nickel insertion into the metal center of the hydrogenase.
CC {ECO:0000255|HAMAP-Rule:MF_00213}.
CC -!- SUBUNIT: Monomer and homodimer. Could also form hexamers
CC (PubMed:19769985). Forms a complex with HypB (PubMed:26056269).
CC {ECO:0000269|PubMed:19769985, ECO:0000269|PubMed:26056269}.
CC -!- SIMILARITY: Belongs to the HypA/HybF family. {ECO:0000255|HAMAP-
CC Rule:MF_00213}.
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DR EMBL; AP006878; BAD86197.1; -; Genomic_DNA.
DR RefSeq; WP_011250958.1; NC_006624.1.
DR PDB; 3A43; X-ray; 2.30 A; A/B=1-139.
DR PDB; 3A44; X-ray; 3.31 A; A/B/C/D=1-139.
DR PDB; 5AUN; X-ray; 1.63 A; A=1-139.
DR PDB; 5AUO; X-ray; 1.80 A; A=1-139.
DR PDB; 5AUP; X-ray; 3.10 A; A/H=1-139.
DR PDB; 5YXY; X-ray; 3.30 A; D/E/F=1-139.
DR PDB; 5YY0; X-ray; 3.24 A; B=1-139.
DR PDBsum; 3A43; -.
DR PDBsum; 3A44; -.
DR PDBsum; 5AUN; -.
DR PDBsum; 5AUO; -.
DR PDBsum; 5AUP; -.
DR PDBsum; 5YXY; -.
DR PDBsum; 5YY0; -.
DR AlphaFoldDB; Q5JIH3; -.
DR SMR; Q5JIH3; -.
DR STRING; 69014.TK2008; -.
DR EnsemblBacteria; BAD86197; BAD86197; TK2008.
DR GeneID; 78448543; -.
DR KEGG; tko:TK2008; -.
DR PATRIC; fig|69014.16.peg.1961; -.
DR eggNOG; arCOG04426; Archaea.
DR HOGENOM; CLU_126929_2_0_2; -.
DR InParanoid; Q5JIH3; -.
DR OrthoDB; 36835at2157; -.
DR PhylomeDB; Q5JIH3; -.
DR EvolutionaryTrace; Q5JIH3; -.
DR Proteomes; UP000000536; Chromosome.
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 GO; GO:0036211; P:protein modification process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.2320.80; -; 1.
DR HAMAP; MF_00213; HypA_HybF; 1.
DR InterPro; IPR020538; Hydgase_Ni_incorp_HypA/HybF_CS.
DR InterPro; IPR000688; HypA/HybF.
DR PANTHER; PTHR34535; HYDROGENASE MATURATION FACTOR HYPA; 1.
DR PANTHER; PTHR34535:SF3; HYDROGENASE MATURATION FACTOR HYPA; 1.
DR Pfam; PF01155; HypA; 1.
DR PIRSF; PIRSF004761; Hydrgn_mat_HypA; 1.
DR PROSITE; PS01249; HYPA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Nickel; Reference proteome; Zinc.
FT CHAIN 1..139
FT /note="Hydrogenase maturation factor HypA"
FT /id="PRO_0000129085"
FT BINDING 1
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000269|PubMed:26056269,
FT ECO:0007744|PDB:5AUN, ECO:0007744|PDB:5AUO"
FT BINDING 2
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000269|PubMed:26056269,
FT ECO:0007744|PDB:5AUN, ECO:0007744|PDB:5AUO"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00213,
FT ECO:0000269|PubMed:19769985, ECO:0000269|PubMed:26056269,
FT ECO:0007744|PDB:3A43, ECO:0007744|PDB:3A44,
FT ECO:0007744|PDB:5AUN, ECO:0007744|PDB:5AUO,
FT ECO:0007744|PDB:5AUP"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00213,
FT ECO:0000269|PubMed:19769985, ECO:0000269|PubMed:26056269,
FT ECO:0007744|PDB:3A43, ECO:0007744|PDB:3A44,
FT ECO:0007744|PDB:5AUN, ECO:0007744|PDB:5AUO,
FT ECO:0007744|PDB:5AUP"
FT BINDING 98
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000269|PubMed:26056269,
FT ECO:0007744|PDB:5AUN, ECO:0007744|PDB:5AUO"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00213,
FT ECO:0000269|PubMed:19769985, ECO:0000269|PubMed:26056269,
FT ECO:0007744|PDB:3A43, ECO:0007744|PDB:3A44,
FT ECO:0007744|PDB:5AUN, ECO:0007744|PDB:5AUO,
FT ECO:0007744|PDB:5AUP"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00213,
FT ECO:0000269|PubMed:19769985, ECO:0000269|PubMed:26056269,
FT ECO:0007744|PDB:3A43, ECO:0007744|PDB:3A44,
FT ECO:0007744|PDB:5AUN, ECO:0007744|PDB:5AUO,
FT ECO:0007744|PDB:5AUP"
FT HELIX 3..20
FT /evidence="ECO:0007829|PDB:5AUN"
FT STRAND 24..34
FT /evidence="ECO:0007829|PDB:5AUN"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:5AUN"
FT HELIX 41..52
FT /evidence="ECO:0007829|PDB:5AUN"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:5AUN"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:5AUN"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:5AUN"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:5AUN"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:5AUN"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:5AUN"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:5AUN"
FT HELIX 91..99
FT /evidence="ECO:0007829|PDB:5AUN"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:5AUN"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:5AUN"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:5AUN"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:5AUN"
FT STRAND 125..134
FT /evidence="ECO:0007829|PDB:5AUN"
SQ SEQUENCE 139 AA; 15689 MW; 2D8CC76DE5D9C55B CRC64;
MHEWALADAI VRTVLDYAQR EGASRVKAVR VVLGELQDVA EDIVKFAMEQ LFAGTIAEGA
EIEFVEEEAV FKCRNCNYEW KLKEVKDKFD ERIKEDIHFI PEVVHAFLAC PKCGSHDFEV
VKGRGVYVAG IKIEKEGGS
//
