ID R9BYC7_9BACI Unreviewed; 351 AA.
AC R9BYC7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN ORFNames=A499_20338 {ECO:0000313|EMBL:EOR22052.1};
OS Niallia nealsonii AAU1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Niallia.
OX NCBI_TaxID=1202533 {ECO:0000313|EMBL:EOR22052.1, ECO:0000313|Proteomes:UP000014030};
RN [1] {ECO:0000313|EMBL:EOR22052.1, ECO:0000313|Proteomes:UP000014030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAU1 {ECO:0000313|EMBL:EOR22052.1,
RC ECO:0000313|Proteomes:UP000014030};
RA Joshi C.G., Duggirala S.M., Nathani N.M., Bhatt V.D., KaPatel J.A.,
RA Parnerkar S.P.;
RT "Whole genome shotgun sequencing of Bacillus nealsonii AAU1.";
RL Submitted (MAR-2013) 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}.
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:EOR22052.1}.
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DR EMBL; ASRU01000249; EOR22052.1; -; Genomic_DNA.
DR RefSeq; WP_016204591.1; NZ_ASRU01000249.1.
DR AlphaFoldDB; R9BYC7; -.
DR PATRIC; fig|1202533.3.peg.4211; -.
DR OrthoDB; 9809679at2; -.
DR Proteomes; UP000014030; 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; IPR000808; Mrp-like_CS.
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; SSF117916; Fe-S cluster assembly (FSCA) domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS01215; MRP; 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}.
FT BINDING 108..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ SEQUENCE 351 AA; 38612 MW; 37F2943B0BD25392 CRC64;
MITKEEIEKI VENMIDPFLH KSLLELGAVK DVKWNAEKGL ASLKIAVAKL GSAYQIELQN
QIVSALKDKG VKSVGLRFTE LSSTLVEEIV NETESREKIP IYIAIASGKG GVGKSTVSVN
LAVSLARLGK KVGLLDADIY GFSVPDMMGI TKRPEVINER IIPVERFGVK VISMGFFVED
NTPIIWRGPM LGKMLTSFME EVEWGELDYL LLDLPPGTGD VALDVHSMLP TSKEIIVTTP
HPTAAFVAAR AGAMALRTEH EILGVIENMS YFESRLTGEK EYVFGKGGGK KLAKDLEVPM
LGELPLGQPD WNEEDFAPSV YQETHHIGER YRAIAEQIVE VLEKTGDKVE S
//
