ID A0A0T5XA11_9BACT Unreviewed; 295 AA.
AC A0A0T5XA11;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-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=HMPREF1705_04452 {ECO:0000313|EMBL:KRT35187.1};
OS Acetomicrobium hydrogeniformans ATCC BAA-1850.
OC Bacteria; Synergistota; Synergistia; Synergistales; Acetomicrobiaceae;
OC Acetomicrobium.
OX NCBI_TaxID=592015 {ECO:0000313|EMBL:KRT35187.1, ECO:0000313|Proteomes:UP000005273};
RN [1] {ECO:0000313|EMBL:KRT35187.1, ECO:0000313|Proteomes:UP000005273}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1850 {ECO:0000313|Proteomes:UP000005273};
RA Gruening B.A., Erxleben A., Flemming S., Lucas X., Doering K.,
RA Weitnauer G., Bechthold A., Guenther S.;
RL Submitted (SEP-2012) 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:KRT35187.1}.
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DR EMBL; ACJX03000001; KRT35187.1; -; Genomic_DNA.
DR RefSeq; WP_009202167.1; NZ_ACJX03000001.1.
DR AlphaFoldDB; A0A0T5XA11; -.
DR STRING; 592015.HMPREF1705_04452; -.
DR eggNOG; COG0489; Bacteria.
DR OrthoDB; 9809679at2; -.
DR Proteomes; UP000005273; 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; 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}.
FT BINDING 44..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ SEQUENCE 295 AA; 31977 MW; 00753A4F8C7E8EF0 CRC64;
MNVNLEREQF EAMKARIREE ALRTKGPLAM ALKDIKHKIA ILSGKGGVGK TVVTVNLASA
LKRRGYEVCI FDADLHGPAV PRALGLLGRM DVVSEHDHPG HHDLRLNPLT SLKGIKVVSV
ASMWATQEQP IMWKGAHKMR AIRQLIASVN WGTADFLLVD LPPGTGDEVQ TVMRSIPELD
GMLVVTTPQG VSAMVCSRAI SAAKELDIPL LGLVENMSSL KCPACGEKMY PFGKGEGEKL
ARLMNIPFLG DIPIELDMGQ CVDDGVPLVD KKPNSAFART LDDIASKLTA SLKKK
//
