ID A6Q2K2_NITSB Unreviewed; 387 AA.
AC A6Q2K2;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN Name=mrp {ECO:0000313|EMBL:BAF69711.1};
GN OrderedLocusNames=NIS_0597 {ECO:0000313|EMBL:BAF69711.1};
OS Nitratiruptor sp. (strain SB155-2).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Nautiliales;
OC Nitratiruptoraceae; Nitratiruptor.
OX NCBI_TaxID=387092 {ECO:0000313|EMBL:BAF69711.1, ECO:0000313|Proteomes:UP000001118};
RN [1] {ECO:0000313|EMBL:BAF69711.1, ECO:0000313|Proteomes:UP000001118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB155-2 {ECO:0000313|EMBL:BAF69711.1,
RC ECO:0000313|Proteomes:UP000001118};
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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}.
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DR EMBL; AP009178; BAF69711.1; -; Genomic_DNA.
DR RefSeq; WP_012081974.1; NC_009662.1.
DR AlphaFoldDB; A6Q2K2; -.
DR STRING; 387092.NIS_0597; -.
DR KEGG; nis:NIS_0597; -.
DR eggNOG; COG0489; Bacteria.
DR HOGENOM; CLU_024839_0_0_7; -.
DR InParanoid; A6Q2K2; -.
DR OrthoDB; 9809679at2; -.
DR Proteomes; UP000001118; Chromosome.
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; 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.
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:UP000001118}.
FT DOMAIN 4..72
FT /note="MIP18 family-like"
FT /evidence="ECO:0000259|Pfam:PF01883"
FT BINDING 105..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ SEQUENCE 387 AA; 41455 MW; CDF489A16C3C9641 CRC64;
MLNEAKVQEV LSTVTYPGFT KDIVTFGFVK GIEVNGDRVA VELDITSSAP EVAQQLRDEI
TKKLELEGAK EVIVNIKQPK MPRETSSRGK NLAPQVKNFV MISSGKGGVG KSTTTVNLAI
ATAMQGKKVG ILDADIYGPN VPRMMGILGV QPEVVGNKVK PIETKYGVEV MSMGVLMEEG
QSLIWRGAMI MKAIEQFLRD ILWSDLDVLF IDMPPGTGDA QLTLAQSVPV TAGVTVTTPQ
MVSLDDSRRS LDMFKKLHIP IAGIVENMSG FICPNCSTES DIFGKGTAHD VALEYGTSVL
GEIPIEPAIR EGGDEGKPVV FFHPESETAK RYHQAANKLW HFIEKVNEEG GASNEMIQPT
TPPGVSACST AGYDAGNQGG GGCGCSH
//