ID A0A2A5QUN0_9EURY Unreviewed; 358 AA.
AC A0A2A5QUN0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN ORFNames=CP557_08350 {ECO:0000313|EMBL:PCR90525.1};
OS Natrinema ejinorense.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=373386 {ECO:0000313|EMBL:PCR90525.1, ECO:0000313|Proteomes:UP000219689};
RN [1] {ECO:0000313|EMBL:PCR90525.1, ECO:0000313|Proteomes:UP000219689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13890 {ECO:0000313|EMBL:PCR90525.1,
RC ECO:0000313|Proteomes:UP000219689};
RA Roh S.W., Kim Y.B., Kim J.Y.;
RT "Genome sequences of Natrinema ejinorence JCM 13890T.";
RL Submitted (SEP-2017) 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:PCR90525.1}.
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DR EMBL; NXNI01000001; PCR90525.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A5QUN0; -.
DR OrthoDB; 8297at2157; -.
DR Proteomes; UP000219689; 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|HAMAP-Rule:MF_02040};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02040}.
FT DOMAIN 3..65
FT /note="MIP18 family-like"
FT /evidence="ECO:0000259|Pfam:PF01883"
FT REGION 304..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 101..108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ SEQUENCE 358 AA; 37863 MW; A865750E546D78BF CRC64;
MDEAAVRDRL RTVEDPELGD DIVSLGLVND ISVDGDEVDI DLALGAPYSP SESDIAAEVR
EVLTAEGLEP DLTASVPDRD DLTSEEQVLP NVKNVIAVAS GKGGVGKSTV AVNLAAGLSQ
LGARVGLFDA DVYGPNVPRM VDADEPPMAT EDETLVPPEK YGVKLMSMAF LTGEDDPVIW
RGPMVHKVIT QLTEDVEWGH LDYLVVDLPP GTGDTQLTML QTMPVTGAVI VTTPQDVALD
DARKGLEMFA KHDTVVLGIA ENMSTFACPD CGGEHDIFGS GGGEDFAEEH ELPFLGSIPL
DPAVREGGDG GKPTVLKDGD GTSDALRTIT ENVANNTGIV HRQAISQSRR NEAASPDR
//