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Database: UniProt
Entry: A0A1M4VYC8_9FIRM
LinkDB: A0A1M4VYC8_9FIRM
Original site: A0A1M4VYC8_9FIRM 
ID   A0A1M4VYC8_9FIRM        Unreviewed;       282 AA.
AC   A0A1M4VYC8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN   ORFNames=SAMN02745133_01041 {ECO:0000313|EMBL:SHE74054.1};
OS   Desulforamulus putei DSM 12395.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=1121429 {ECO:0000313|EMBL:SHE74054.1, ECO:0000313|Proteomes:UP000184148};
RN   [1] {ECO:0000313|EMBL:SHE74054.1, ECO:0000313|Proteomes:UP000184148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12395 {ECO:0000313|EMBL:SHE74054.1,
RC   ECO:0000313|Proteomes:UP000184148};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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}.
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DR   EMBL; FQUY01000005; SHE74054.1; -; Genomic_DNA.
DR   RefSeq; WP_073236787.1; NZ_FQUY01000005.1.
DR   AlphaFoldDB; A0A1M4VYC8; -.
DR   STRING; 1121429.SAMN02745133_01041; -.
DR   OrthoDB; 9809679at2; -.
DR   Proteomes; UP000184148; 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; 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; 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}.
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         47..54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   282 AA;  30439 MW;  8D98BDCF91C7B444 CRC64;
     MSRDNGQCST CEEMRDGTCG GEKCSPPPKL YPGGQSKIGR VIAVMSGKGG VGKSSVTSLM
     AVNLQRMGHK VGILDADITG PSIPRMFGIK RAPQSRGMLL PAKSRTGISI MSLNLLLEKE
     DEPVIWRGPI LAGAVKQFWT DVNWGELDYL LLDLPPGTGD IPLTVLQQIP VDGIVVVTSP
     QDLAVMVVKK AVKMAGIMET PILGFVQNMA YVTCPKCGEK FEIYGKSLRK GDTLEELPVL
     EVLPIDPEFT RLCDNGLVED TATVAFKDIP NLIKSKTRAN VN
//
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