ID G6XMR4_9PROT Unreviewed; 412 AA.
AC G6XMR4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, 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=GMO_27820 {ECO:0000313|EMBL:EHH66963.1};
OS Gluconobacter morbifer G707.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=1088869 {ECO:0000313|EMBL:EHH66963.1, ECO:0000313|Proteomes:UP000004949};
RN [1] {ECO:0000313|EMBL:EHH66963.1, ECO:0000313|Proteomes:UP000004949}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G707 {ECO:0000313|EMBL:EHH66963.1,
RC ECO:0000313|Proteomes:UP000004949};
RA Lee W.-J., Kim E.-K.;
RT "Genome sequence of Gluconobacter morbifer G707, isolated from Drosophila
RT gut.";
RL Submitted (OCT-2011) 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:EHH66963.1}.
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DR EMBL; AGQV01000015; EHH66963.1; -; Genomic_DNA.
DR AlphaFoldDB; G6XMR4; -.
DR STRING; 1088869.GMO_27820; -.
DR PATRIC; fig|1088869.3.peg.2775; -.
DR eggNOG; COG0489; Bacteria.
DR Proteomes; UP000004949; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000004949}.
FT REGION 15..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 163..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ SEQUENCE 412 AA; 43229 MW; A3BC6765798ECAA2 CRC64;
MLKYTFFLTG RFPIESPGMT DNSKPPVDDT TPSVSPEKRI ADLLNSEQDD AGANVLSFAA
LESISVRDGH AHVSLSTSRD NAERVTPFRS RVEAAIVQLP GISAATLSLT AHRTPTAANA
PTAGQGDGGH RPLNLGGRRN AASRHDAASL LTGVRAVIAV ASGKGGVGKS TTAVNLAVGL
AKQGLKAGLL DADIYGPSLP RMLGRNARPE VRDGTILPIE AWGLKSMSIG YLVDENQAMI
WRGPMVMGAL TQFLGEVDWG ELDVLIIDMP PGTGDAQLTL AQKLGPKLAV GGAVIVSTPQ
DIALLDARRG VAMFERMETP ILGVVENMSY FCCPNCNHRT ELFGHGGART EAEKLGVPFL
GEVPLLADIR ASGDEGTPII LSAPDSEAAR AYTALATTIA QKLESSPVKE PS
//
