ID B2I6C3_XYLF2 Unreviewed; 303 AA.
AC B2I6C3;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN OrderedLocusNames=XfasM23_1420 {ECO:0000313|EMBL:ACB92833.1};
OS Xylella fastidiosa (strain M23).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=405441 {ECO:0000313|EMBL:ACB92833.1, ECO:0000313|Proteomes:UP000001698};
RN [1] {ECO:0000313|EMBL:ACB92833.1, ECO:0000313|Proteomes:UP000001698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M23 {ECO:0000313|EMBL:ACB92833.1,
RC ECO:0000313|Proteomes:UP000001698};
RX PubMed=20601474; DOI=10.1128/JB.00651-10;
RA Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT causing almond leaf scorch disease in California.";
RL J. Bacteriol. 192:4534-4534(2010).
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; CP001011; ACB92833.1; -; Genomic_DNA.
DR AlphaFoldDB; B2I6C3; -.
DR SMR; B2I6C3; -.
DR KEGG; xfn:XfasM23_1420; -.
DR HOGENOM; CLU_024839_0_0_6; -.
DR Proteomes; UP000001698; 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; 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; 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 51..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ SEQUENCE 303 AA; 31879 MW; 4E00CA288F22A07F CRC64;
MSEDGGVTTD ERACAAPLQL SNTFPRVSRH AVQTGLSPHP RVRNVIAVGS GKGGVGKSTI
AVNLAVALQR TGVRVGLLDA DIYGPSVPAM LGLSGRPESP DNKLIEPLRA FGIEAMSIGL
LIDVDTPMIW RGPMATSALT QLFNDTLWGD LDYLLIDLPP GTGDIQLTLS QKIPVAGAVI
VTTPQDIATL DARKALKMFE KVNVPVLGIV ENMAMHCCRQ CGHVEHLFGE GGAQRMAEHY
HVPLLGSLPL DIVIREHGDL GQPITVAAPK GSVGQAYAAV AACLAAELAK RPRAAIPMTT
TLG
//
