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Database: UniProt
Entry: V5WIL8_9SPIO
LinkDB: V5WIL8_9SPIO
Original site: V5WIL8_9SPIO 
ID   V5WIL8_9SPIO            Unreviewed;       306 AA.
AC   V5WIL8;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN   ORFNames=L21SP2_2267 {ECO:0000313|EMBL:AHC15628.1};
OS   Salinispira pacifica.
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC   Salinispira.
OX   NCBI_TaxID=1307761 {ECO:0000313|EMBL:AHC15628.1, ECO:0000313|Proteomes:UP000018680};
RN   [1] {ECO:0000313|EMBL:AHC15628.1, ECO:0000313|Proteomes:UP000018680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L21-RPul-D2 {ECO:0000313|EMBL:AHC15628.1,
RC   ECO:0000313|Proteomes:UP000018680};
RX   PubMed=26203324; DOI=10.1186/1944-3277-10-7;
RA   Ben Hania W., Joseph M., Schumann P., Bunk B., Fiebig A., Sproer C.,
RA   Klenk H.P., Fardeau M.L., Spring S.;
RT   "Complete genome sequence and description of Salinispira pacifica gen.
RT   nov., sp. nov., a novel spirochaete isolated form a hypersaline microbial
RT   mat.";
RL   Stand. Genomic Sci. 10:7-7(2015).
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; CP006939; AHC15628.1; -; Genomic_DNA.
DR   AlphaFoldDB; V5WIL8; -.
DR   STRING; 1307761.L21SP2_2267; -.
DR   KEGG; slr:L21SP2_2267; -.
DR   PATRIC; fig|1307761.3.peg.2260; -.
DR   eggNOG; COG0489; Bacteria.
DR   HOGENOM; CLU_024839_0_1_12; -.
DR   OrthoDB; 9809679at2; -.
DR   Proteomes; UP000018680; 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_02040; Mrp_NBP35; 1.
DR   InterPro; IPR000808; Mrp-like_CS.
DR   InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR033756; YlxH/NBP35.
DR   PANTHER; PTHR23264:SF19; CYTOSOLIC FE-S CLUSTER ASSEMBLY FACTOR NUBP1; 1.
DR   PANTHER; PTHR23264; NUCLEOTIDE-BINDING PROTEIN NBP35 YEAST -RELATED; 1.
DR   Pfam; PF10609; ParA; 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:UP000018680}.
FT   REGION          273..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   306 AA;  32966 MW;  DC61AA63EE77CAF3 CRC64;
     MHGTNDKHAQ DVRIYDNLKK IKNVITVLSG KGGVGKSTVA VNLAHSLVNE GYSVGIMDVD
     IHGPNIPKML GIEDRHFSGE AEAIEPVEIL PNFHAASIAL VGYDPAEALI WRGPMKIGLI
     RQFLGDVVWG ELDYLIIDTP PGTGDEALTT AQLIPQMKGA VVVTSPQDVS ILDSRKSMTF
     ADKLNIPILG IIENMSSFVC SHCGGVTDIF GRGGGMKASE TVDVPFLGSV PIDPGIVVAG
     DQGRPFMAQF PDRPAAQAFK EIIKNVNEEI RKNSEKGLYE GKDPEDPRIA EAERKKSVAD
     GFKPLQ
//
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