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Database: UniProt
Entry: A0A1S6FL74_9SPHN
LinkDB: A0A1S6FL74_9SPHN
Original site: A0A1S6FL74_9SPHN 
ID   A0A1S6FL74_9SPHN        Unreviewed;       321 AA.
AC   A0A1S6FL74;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN   ORFNames=BXU08_12070 {ECO:0000313|EMBL:AQR74288.1};
OS   Sphingomonas sp. LM7.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1938607 {ECO:0000313|EMBL:AQR74288.1, ECO:0000313|Proteomes:UP000189383};
RN   [1] {ECO:0000313|EMBL:AQR74288.1, ECO:0000313|Proteomes:UP000189383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LM7 {ECO:0000313|EMBL:AQR74288.1,
RC   ECO:0000313|Proteomes:UP000189383};
RA   Hentchel K., Vargas G., Fiebig A., Chen S.L., Coleman M., Crosson S.;
RT   "Genome sequences of bacteria isolated from the littoral zone of southern
RT   Lake Michigan.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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; CP019511; AQR74288.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S6FL74; -.
DR   STRING; 1938607.BXU08_12070; -.
DR   KEGG; splm:BXU08_12070; -.
DR   OrthoDB; 9809679at2; -.
DR   Proteomes; UP000189383; 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|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:UP000189383}.
FT   BINDING         81..88
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   321 AA;  32951 MW;  BDBA817E86CA6CDC CRC64;
     MNDVQSLKAA LAPIAAGRAS ARIEDGKASI VLDVTGLGEA ARAELEADVR RVAQAVPGVT
     EVRVLLTSER RTRRLIAVAS GKGGVGKSTV AANIAIALAR RGRRVGLVDA DIYGPSQTRL
     LGVDGIRPEA REKTLIPVQT KFGVPLLSMG GLVPEGQAIA WRGSMAGGAL GQMVDADWGD
     AEVLILDLPP GTGDLQLTMV QKHKPAGAII VSTPQDLALI DATRAIDLFN KVNVPIVGVI
     ENMSGYACPH CGEVSDPFGS GGAEAAAGKM GLPFLGRIPL ELAIRTASDA GDPPAAGNGP
     QAETFALLAA RLDDWLAANG G
//
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