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Database: UniProt
Entry: A0A069D3K0_9BACE
LinkDB: A0A069D3K0_9BACE
Original site: A0A069D3K0_9BACE 
ID   A0A069D3K0_9BACE        Unreviewed;       368 AA.
AC   A0A069D3K0;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN   ORFNames=JCM15093_2056 {ECO:0000313|EMBL:GAK36856.1};
OS   Bacteroides graminisolvens DSM 19988 = JCM 15093.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1121097 {ECO:0000313|EMBL:GAK36856.1, ECO:0000313|Proteomes:UP000027601};
RN   [1] {ECO:0000313|EMBL:GAK36856.1, ECO:0000313|Proteomes:UP000027601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 15093 {ECO:0000313|EMBL:GAK36856.1,
RC   ECO:0000313|Proteomes:UP000027601};
RX   PubMed=25736980;
RA   Inoue J., Oshima K., Suda W., Sakamoto M., Iino T., Noda S., Hongoh Y.,
RA   Hattori M., Ohkuma M.;
RT   "Distribution and evolution of nitrogen fixation genes in the phylum
RT   bacteroidetes.";
RL   Microbes Environ. 30:44-50(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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAK36856.1}.
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DR   EMBL; BAJS01000010; GAK36856.1; -; Genomic_DNA.
DR   RefSeq; WP_024996667.1; NZ_BAJS01000010.1.
DR   AlphaFoldDB; A0A069D3K0; -.
DR   STRING; 1121097.GCA_000428125_01951; -.
DR   eggNOG; COG0489; Bacteria.
DR   OrthoDB; 9809679at2; -.
DR   Proteomes; UP000027601; Unassembled WGS sequence.
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:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR   CDD; cd02037; Mrp_NBP35; 1.
DR   Gene3D; 3.30.300.130; Fe-S cluster assembly (FSCA); 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_02040; Mrp_NBP35; 1.
DR   InterPro; IPR034904; FSCA_dom_sf.
DR   InterPro; IPR002744; MIP18-like.
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; PF01883; FeS_assembly_P; 1.
DR   Pfam; PF10609; ParA; 1.
DR   SUPFAM; SSF117916; Fe-S cluster assembly (FSCA) domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
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:UP000027601}.
FT   DOMAIN          8..68
FT                   /note="MIP18 family-like"
FT                   /evidence="ECO:0000259|Pfam:PF01883"
FT   BINDING         108..115
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   368 AA;  40007 MW;  9552D414D293651B CRC64;
     MTLYPKLILD ALTNVRYPGT GKNLVEAGMV EDNIRIEGMK VSFSLVFEKP TDPFMKSVVK
     AAETAILTYV SRDVEIQGNI SVKTMQTPRP EVTQLLPQVK NIVGISSGKG GVGKSTVSAN
     LAVALAKLGY KVGLLDADVF GPSMPKMFQV EDARPYAEKV DGREMIVPVE KYGVKLLSIG
     FFVDPDQATL WRGGMASNAL KQLIGDALWG ELDYFLIDLP PGTSDIHLTV VQTLAMTGAV
     VVSTPQDVAL ADARKGINMF TNEKVNVPIL GLVENMAWFT PAELPENKYY IFGKEGAKRL
     AEEMNVPLLG QIPIVQSIRE GGDNGRPVAL DEDSITGRAF LSLAASLVRQ VDKRNVEMAP
     TQIVEMHK
//
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