ID Q5JIH4_THEKO Unreviewed; 248 AA. AC Q5JIH4; DT 15-FEB-2005, integrated into UniProtKB/TrEMBL. DT 15-FEB-2005, sequence version 1. DT 27-MAR-2024, entry version 109. DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040}; GN OrderedLocusNames=TK2007 {ECO:0000313|EMBL:BAD86196.1}; 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 {ECO:0000313|EMBL:BAD86196.1, ECO:0000313|Proteomes:UP000000536}; RN [1] {ECO:0000313|EMBL:BAD86196.1, ECO:0000313|Proteomes:UP000000536} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1 RC {ECO:0000313|Proteomes:UP000000536}; 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:0007829|PDB:3VX3} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH ADP. RX PubMed=23399544; DOI=10.1016/j.jmb.2013.02.004; RA Sasaki D., Watanabe S., Matsumi R., Shoji T., Yasukochi A., Tagashira K., RA Fukuda W., Kanai T., Atomi H., Imanaka T., Miki K.; RT "Identification and structure of a novel archaeal HypB for [NiFe] RT hydrogenase maturation."; RL J. Mol. Biol. 425:1627-1640(2013). RN [3] {ECO:0007829|PDB:5AUN, ECO:0007829|PDB:5AUO} RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) IN COMPLEX WITH ADP AND ATP ANALOG. 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: Binds and transfers iron-sulfur (Fe-S) clusters to target CC apoproteins. Can hydrolyze ATP. {ECO:0000256|HAMAP-Rule:MF_02040}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02040}. CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family. CC {ECO:0000256|HAMAP-Rule:MF_02040}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP006878; BAD86196.1; -; Genomic_DNA. DR RefSeq; WP_011250957.1; NC_006624.1. DR PDB; 3VX3; X-ray; 2.10 A; A/B=1-248. DR PDB; 5AUN; X-ray; 1.63 A; B=1-248. DR PDB; 5AUO; X-ray; 1.80 A; B=1-248. DR PDB; 5AUP; X-ray; 3.10 A; B/I=1-248. DR PDB; 5AUQ; X-ray; 2.52 A; A/B/C/D/E/F/G/H=1-248. DR PDBsum; 3VX3; -. DR PDBsum; 5AUN; -. DR PDBsum; 5AUO; -. DR PDBsum; 5AUP; -. DR PDBsum; 5AUQ; -. DR AlphaFoldDB; Q5JIH4; -. DR SMR; Q5JIH4; -. DR STRING; 69014.TK2007; -. DR EnsemblBacteria; BAD86196; BAD86196; TK2007. DR GeneID; 78448542; -. DR KEGG; tko:TK2007; -. DR PATRIC; fig|69014.16.peg.1960; -. DR eggNOG; arCOG00585; Archaea. DR HOGENOM; CLU_024839_0_2_2; -. DR InParanoid; Q5JIH4; -. DR OrthoDB; 85513at2157; -. DR PhylomeDB; Q5JIH4; -. DR Proteomes; UP000000536; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule. DR GO; GO:0140663; F:ATP-dependent FeS chaperone activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central. DR CDD; cd02037; Mrp_NBP35; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_02040; Mrp_NBP35; 1. DR InterPro; IPR019591; Mrp/NBP35_ATP-bd. DR InterPro; IPR044304; NUBPL-like. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR033756; YlxH/NBP35. DR PANTHER; PTHR42961; IRON-SULFUR PROTEIN NUBPL; 1. DR PANTHER; PTHR42961:SF2; IRON-SULFUR PROTEIN NUBPL; 1. DR Pfam; PF10609; ParA; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:3VX3, ECO:0007829|PDB:5AUN}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_02040}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_02040}; KW Iron {ECO:0000256|HAMAP-Rule:MF_02040}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_02040}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_02040}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_02040}; Reference proteome {ECO:0000313|Proteomes:UP000000536}. FT BINDING 27..34 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02040" FT BINDING 28 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:3VX3, ECO:0007829|PDB:5AUN" FT BINDING 30 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:3VX3, ECO:0007829|PDB:5AUN" FT BINDING 31 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:3VX3, ECO:0007829|PDB:5AUN" FT BINDING 32 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:3VX3, ECO:0007829|PDB:5AUN" FT BINDING 33 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:3VX3, ECO:0007829|PDB:5AUN" FT BINDING 34 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:3VX3, ECO:0007829|PDB:5AUN" FT BINDING 34 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:5AUN, ECO:0007829|PDB:5AUO" FT BINDING 34 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:5AUP" FT BINDING 35 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:3VX3, ECO:0007829|PDB:5AUN" FT BINDING 57 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:5AUN, ECO:0007829|PDB:5AUO" FT BINDING 57 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:5AUP" FT BINDING 132 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:5AUP" FT BINDING 149 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:5AUN, ECO:0007829|PDB:5AUO" FT BINDING 160 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:3VX3, ECO:0007829|PDB:5AUN" FT BINDING 187 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:3VX3, ECO:0007829|PDB:5AUN" FT BINDING 217 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:3VX3, ECO:0007829|PDB:5AUN" FT BINDING 219 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:3VX3, ECO:0007829|PDB:5AUN" FT BINDING 223 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:3VX3" SQ SEQUENCE 248 AA; 27586 MW; D0E5F945B639C2B4 CRC64; MNAIDPREIA INARLEGVKR IIPVVSGKGG VGKSLVSTTL ALVLAEKGYR VGLLDLDFHG ASDHVILGFE PKEFPEEDRG VVPPTVHGIK FMTIAYYTED RPTPLRGKEI SDALIELLTI TRWDELDYLV IDMPPGLGDQ LLDVLRFLKR GEFLVVATPS KLSLNVVRKL IELLKEEGHK VIGVVENMKL RSEQLDDEKD VEKLAEEFGV PYLVGIPFYP DLDAKVGNVE ELMKTEFAGK VRELAGRL //