ID A0A0J8YA63_9ENTR Unreviewed; 369 AA.
AC A0A0J8YA63;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN ORFNames=ACH50_13090 {ECO:0000313|EMBL:KMV34334.1};
OS Franconibacter pulveris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Franconibacter.
OX NCBI_TaxID=435910 {ECO:0000313|EMBL:KMV34334.1, ECO:0000313|Proteomes:UP000037315};
RN [1] {ECO:0000313|EMBL:KMV34334.1, ECO:0000313|Proteomes:UP000037315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ34 {ECO:0000313|EMBL:KMV34334.1,
RC ECO:0000313|Proteomes:UP000037315};
RA Pal S., Banerjee T.D., Roy A., Sar P., Kazy S.K.;
RT "Genome sequencing of Cronobacter sp. strain DJ34 isolated from petroleum
RT contaminated sludge of Duliajan Oil Fields, Assam, India.";
RL Submitted (JUN-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:KMV34334.1}.
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DR EMBL; LFEJ01000015; KMV34334.1; -; Genomic_DNA.
DR RefSeq; WP_024556348.1; NZ_LFEJ01000015.1.
DR AlphaFoldDB; A0A0J8YA63; -.
DR STRING; 1121863.GCA_000621185_03857; -.
DR PATRIC; fig|1656095.3.peg.2705; -.
DR OrthoDB; 9809679at2; -.
DR Proteomes; UP000037315; 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; 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|HAMAP-Rule:MF_02040};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02040}.
FT BINDING 115..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ SEQUENCE 369 AA; 39572 MW; C299A82867A77B81 CRC64;
MSSQSQTTSP EALRAMVAGT LANFQHPTLK HNLTALKALH HVAWLDDTIH IELQMPFAWN
SAFEDLKEQC SAELLRMTGA KAIDWKLSHS IATLKRVKNQ PGVNGVKNII AVSSGKGGVG
KSSTAVNLAL ALIAEGAKVG ILDADIYGPS VPTMLGAEGQ RPTSPDGTHM APIVAHGLAT
NSIGYLVTDD NAMVWRGPMA SKALMQLLQE TMWPDLDYLV LDMPPGTGDI QLTLAQNIPV
TGAVVVTTPQ DIALIDAKKG IVMFEKVEVP VLGVVENMSM HICSNCGHHE PIFGTGGAQK
LAETYHTQLL GQLPLHISLR EDLDNGTPTV IARPDSEFTT LYRQLAGRVA AQLYWQGEVI
PGDIAFRAV
//