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Database: UniProt
Entry: A0A1B6YJ75_9RHOB
LinkDB: A0A1B6YJ75_9RHOB
Original site: A0A1B6YJ75_9RHOB 
ID   A0A1B6YJ75_9RHOB        Unreviewed;       366 AA.
AC   A0A1B6YJ75;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN   ORFNames=A8B83_17885 {ECO:0000313|EMBL:OAN68692.1};
OS   Rhodobacteraceae bacterium EhC02.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1849170 {ECO:0000313|EMBL:OAN68692.1, ECO:0000313|Proteomes:UP000078223};
RN   [1] {ECO:0000313|EMBL:OAN68692.1, ECO:0000313|Proteomes:UP000078223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EhC02 {ECO:0000313|EMBL:OAN68692.1,
RC   ECO:0000313|Proteomes:UP000078223};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-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}.
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:OAN68692.1}.
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DR   EMBL; LXYH01000031; OAN68692.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B6YJ75; -.
DR   STRING; 1849170.A8B83_17885; -.
DR   OrthoDB; 9809679at2; -.
DR   Proteomes; UP000078223; 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; 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:UP000078223}.
FT   DOMAIN          13..77
FT                   /note="MIP18 family-like"
FT                   /evidence="ECO:0000259|Pfam:PF01883"
FT   BINDING         119..126
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   366 AA;  37667 MW;  81FFDEFA38EB00A0 CRC64;
     MSMADDPILL AAREALSGLN MPDGTPFLGA PQVSGPVVAN GRVNVSIMTN AQAAASLAGV
     RAAAEAALRD IPGVDSAFVV LTNEQSAPPR LTTPKPAVAP GAAPKVLAGV RHVVAVASGK
     GGVGKSTTAV NLALGLRAKG LRVGILDADI HGPSIPTLLA LHGRPRMGKD RRLLPMQSNG
     LLAMSMGMMV DAETAMVWRG PMVMSAITQM LADVDWGELD VLIVDMPPGT GDAQLAIAQG
     TTLAGAVIVS TPQDLALVDA RRGIAMFRKV DVPIIGLIEN MAYFTCTDCG KQHALFGTGG
     AQAEARRLGV PFLGAVPLTM DLRAASDSGQ PIVARDPDGV LGRLYTEMAE AVWSSLTAPV
     PDVLNN
//
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