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Database: UniProt
Entry: W7UF53_RUMFL
LinkDB: W7UF53_RUMFL
Original site: W7UF53_RUMFL 
ID   W7UF53_RUMFL            Unreviewed;       274 AA.
AC   W7UF53;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-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=RF007C_08930 {ECO:0000313|EMBL:EWM53826.1};
OS   Ruminococcus flavefaciens 007c.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1341157 {ECO:0000313|EMBL:EWM53826.1, ECO:0000313|Proteomes:UP000019365};
RN   [1] {ECO:0000313|EMBL:EWM53826.1, ECO:0000313|Proteomes:UP000019365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=007c {ECO:0000313|EMBL:EWM53826.1,
RC   ECO:0000313|Proteomes:UP000019365};
RX   PubMed=24992679;
RA   Dassa B., Borovok I., Ruimy-Israeli V., Lamed R., Flint H.J., Duncan S.H.,
RA   Henrissat B., Coutinho P., Morrison M., Mosoni P., Yeoman C.J., White B.A.,
RA   Bayer E.A.;
RT   "Rumen cellulosomics: divergent fiber-degrading strategies revealed by
RT   comparative genome-wide analysis of six ruminococcal strains.";
RL   PLoS ONE 9:E99221-E99221(2014).
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:EWM53826.1}.
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DR   EMBL; ATAX01000023; EWM53826.1; -; Genomic_DNA.
DR   RefSeq; WP_037298722.1; NZ_ATAX01000023.1.
DR   AlphaFoldDB; W7UF53; -.
DR   PATRIC; fig|1341157.4.peg.1467; -.
DR   eggNOG; COG0489; Bacteria.
DR   OrthoDB; 9809679at2; -.
DR   Proteomes; UP000019365; 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; 3.40.50.300; 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:UP000019365}.
FT   BINDING         43..50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   274 AA;  29445 MW;  83322B635DCF6B83 CRC64;
     MSECTHDCSS CGSDCGSRTE PQSLLEKPNA MSSIGKVIGV VSGKGGVGKT LVSSMLAVSM
     QRLGKKVGIM DADITGPSIP KAFGIHQKAD ACEFGIIPAR TKMGLDIMSI NLLLENESDP
     VVWRGPVIAG VVKQFWTDVI WKDIDCLVVD MPPGTGDVPL TVFQSLPVDG IVIVTSPQEL
     VSMIVEKAVK MAKLMNIPIL GIIENMSYFE CPDCGKRHSI YGESHIEEIA AQYDIPVLAK
     LPIDPQLAKL CDQGTIELFE GEWLTEAAEK VASL
//
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