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Database: UniProt
Entry: G0VM23_MEGEL
LinkDB: G0VM23_MEGEL
Original site: G0VM23_MEGEL 
ID   G0VM23_MEGEL            Unreviewed;       278 AA.
AC   G0VM23;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN   ORFNames=MELS_0362 {ECO:0000313|EMBL:CCC72585.1};
OS   Megasphaera elsdenii DSM 20460.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=1064535 {ECO:0000313|EMBL:CCC72585.1, ECO:0000313|Proteomes:UP000010111};
RN   [1] {ECO:0000313|EMBL:CCC72585.1, ECO:0000313|Proteomes:UP000010111}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20460 {ECO:0000313|EMBL:CCC72585.1,
RC   ECO:0000313|Proteomes:UP000010111};
RX   PubMed=21914887; DOI=10.1128/JB.05861-11;
RA   Marx H., Graf A.B., Tatto N., Thallinger G.G., Mattanovich D., Sauer M.;
RT   "Genome Sequence of the Ruminal Bacterium Megasphaera elsdenii.";
RL   J. Bacteriol. 193:5578-5579(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; HE576794; CCC72585.1; -; Genomic_DNA.
DR   RefSeq; WP_014015330.1; NZ_CP027570.1.
DR   AlphaFoldDB; G0VM23; -.
DR   STRING; 1064535.MELS_0362; -.
DR   GeneID; 69664258; -.
DR   KEGG; med:MELS_0362; -.
DR   eggNOG; COG0489; Bacteria.
DR   HOGENOM; CLU_024839_0_2_9; -.
DR   Proteomes; UP000010111; 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:UP000010111}.
FT   BINDING         44..51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   278 AA;  29926 MW;  6142006E38952C23 CRC64;
     MSENCTHDCS SCGSSCAERT QPQSLQAAPH AGSHIKHVIA VVSGKGGVGK SLVTSLMAVE
     MQRRGFKTAI LDADITGPSI PKVFGLTDHA TGDENGIYPV TTKTGIKVMS MNLLLEDAAA
     PVVWRGPVIS GAVKQFWTDV IWGDIDYMFV DMPPGTGDVP LTVFQSLPMD GILVVTSPQE
     LVSMIVEKAL NMSEMMHVPV LGLIENMSYF ECPHCHEKLA IFGQSHVEES AQKYDIPHTA
     KLPIDPEFAS HCDKGDIEGY EASYMADTAS FLQGVLGK
//
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