ID A0A3M0GMJ8_9FLAO Unreviewed; 378 AA.
AC A0A3M0GMJ8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN ORFNames=EAX61_09425 {ECO:0000313|EMBL:RMB58516.1};
OS Dokdonia sinensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Dokdonia.
OX NCBI_TaxID=2479847 {ECO:0000313|EMBL:RMB58516.1, ECO:0000313|Proteomes:UP000281985};
RN [1] {ECO:0000313|EMBL:RMB58516.1, ECO:0000313|Proteomes:UP000281985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH27 {ECO:0000313|EMBL:RMB58516.1,
RC ECO:0000313|Proteomes:UP000281985};
RA Zhou L.Y., Du Z.J.;
RT "Dokdonia luteus sp. nov., isolated from sea water.";
RL Submitted (OCT-2018) 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 -!- SIMILARITY: In the C-terminal section; belongs to the Mrp/NBP35 ATP-
CC binding proteins family. {ECO:0000256|ARBA:ARBA00008205}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MIP18 family.
CC {ECO:0000256|ARBA:ARBA00007352}.
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:RMB58516.1}.
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DR EMBL; REFV01000008; RMB58516.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0GMJ8; -.
DR OrthoDB; 9809679at2; -.
DR Proteomes; UP000281985; 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; 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; 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.
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:UP000281985}.
FT DOMAIN 5..52
FT /note="MIP18 family-like"
FT /evidence="ECO:0000259|Pfam:PF01883"
FT BINDING 109..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ SEQUENCE 378 AA; 40385 MW; DC32491756CB6A04 CRC64;
MKLNKKDILE ALKTITVPGA GENMVDSGAV TNVLTFGDEV IVDVTINNPT LQARKKTEVD
ILKTIHEKVY EKAQVKVNVK VNAPAAPEKN EIKGKAIPGI KNIVAVASGK GGVGKSTVTA
NLAVTLAKMG FKVGVLDADI YGPSMPIMFD VASERPLSVT IDGKSKMKPV ESYGVKVLSI
GFFTKPDQAV IWRGPMAAKA LNQMIFDAAW GELDFLLLDL PPGTGDIHLS IMQALPITGA
VVVSTPQAIA LADAKKGVAM FQQDSINVPV LGIIENMAYF TPAELPENKY YIFGREGAKN
LAEDLDVRML GEIPLIQSIR EAGDVGRPAA LQADGPLINV MDEITRNVVE ETVRRNTDLP
PTEAIKITTM AGCAAVKN
//
