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Database: UniProt
Entry: F6IIJ6_9SPHN
LinkDB: F6IIJ6_9SPHN
Original site: F6IIJ6_9SPHN 
ID   F6IIJ6_9SPHN            Unreviewed;       328 AA.
AC   F6IIJ6;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN   ORFNames=PP1Y_AT33463 {ECO:0000313|EMBL:CCA94064.1};
OS   Novosphingobium sp. PP1Y.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=702113 {ECO:0000313|EMBL:CCA94064.1, ECO:0000313|Proteomes:UP000009242};
RN   [1] {ECO:0000313|EMBL:CCA94064.1, ECO:0000313|Proteomes:UP000009242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=sp. PP1Y {ECO:0000313|Proteomes:UP000009242};
RX   PubMed=21685292; DOI=10.1128/JB.05349-11;
RA   D'Argenio V., Petrillo M., Cantiello P., Naso B., Cozzuto L., Notomista E.,
RA   Paolella G., Di Donato A., Salvatore F.;
RT   "De novo sequencing and assembly of the whole genome of Novosphingobium sp.
RT   strain PP1Y.";
RL   J. Bacteriol. 193:4296-4296(2011).
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}.
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DR   EMBL; FR856862; CCA94064.1; -; Genomic_DNA.
DR   RefSeq; WP_007012204.1; NC_015580.1.
DR   AlphaFoldDB; F6IIJ6; -.
DR   KEGG; npp:PP1Y_AT33463; -.
DR   eggNOG; COG0489; Bacteria.
DR   HOGENOM; CLU_024839_0_0_5; -.
DR   OrthoDB; 9809679at2; -.
DR   Proteomes; UP000009242; Chromosome.
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; 3.40.50.300; 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   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|HAMAP-Rule:MF_02040};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02040}; Reference proteome {ECO:0000313|Proteomes:UP000009242}.
FT   BINDING         84..91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   328 AA;  33717 MW;  489CCCAFF82F1CED CRC64;
     MSNDQAEGLK ALLPQEAATR LQSLRVADGR ATLVLDATGL DSSARSALEA AAKQALSGAE
     GVAEVRVAMM ADKVERRIIA VGSGKGGVGK STLATNLAVA LARQGRKVGL VDADIYGPSQ
     ARLLGTEGQR PVAHDSKLVP IASRWGVPVL SMAHLSDPGQ AIAWRGPMAA GALTQLLEGH
     WDGAEILIVD LPPGTGDVQL TMLQKFKPAG AVIVSTPQDL ALMDATRAME LFEKGGVPIV
     GVVENMAGYA CPHCGEVSDP FGAGGAEAAA KTMNQTFLGR IPLDMSIRLD SDAGQPPAAG
     EGPQAQAFAD LARKVGEWLD GGASKAHP
//
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