ID A0A0Q3SZ99_BRECH Unreviewed; 370 AA.
AC A0A0Q3SZ99;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN ORFNames=AN963_20170 {ECO:0000313|EMBL:KQL47150.1};
OS Brevibacillus choshinensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=54911 {ECO:0000313|EMBL:KQL47150.1, ECO:0000313|Proteomes:UP000051063};
RN [1] {ECO:0000313|EMBL:KQL47150.1, ECO:0000313|Proteomes:UP000051063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8552 {ECO:0000313|EMBL:KQL47150.1,
RC ECO:0000313|Proteomes:UP000051063};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (SEP-2015) 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:KQL47150.1}.
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DR EMBL; LJJB01000010; KQL47150.1; -; Genomic_DNA.
DR RefSeq; WP_055746234.1; NZ_LJJB01000010.1.
DR AlphaFoldDB; A0A0Q3SZ99; -.
DR STRING; 54911.AN963_20170; -.
DR PATRIC; fig|54911.3.peg.2049; -.
DR OrthoDB; 9809679at2; -.
DR Proteomes; UP000051063; 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; IPR002744; MIP18-like.
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; PF01883; FeS_assembly_P; 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.
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 DOMAIN 4..69
FT /note="MIP18 family-like"
FT /evidence="ECO:0000259|Pfam:PF01883"
FT BINDING 128..135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ SEQUENCE 370 AA; 40093 MW; A2D9DBC69AC1F8FD CRC64;
MLTKEQVLEA LRDVKDPEIN RSLVELNMIR DIRIEGSTVS LTVVLTITGC PLKAKIEDDV
IAALRALGAE DVHLQFGAMT DDERAALSAQ LRGGGAGQTH NMTPGQAPVL NPILDKNSKT
TFIAVTSGKG GVGKSTVTVN LAVALARMGK KVGIIDADIY GFSVPDMMNI EQRPTVIGET
ILPVERMNVK VMSMGFFVED NSPIIWRGPM LGKMLRNFFS EVHWGEELDY LLLDLPPGTG
DMALDVHTMI PQSMEIVVTT PHATAAFVAA RAGAMAKRTG HEILGIVENM AWYEAKDGSK
EYVFGRGGGA KLAETLTSEL LAQIPLGQPD NHPSEPDYSP SIYREQSAIG QIYMDMAKRV
AEKCESAVKQ
//