ID   APBC_RICTY              Reviewed;         318 AA.
AC   Q68XP6;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000255|HAMAP-Rule:MF_02040};
GN   Name=mrp; OrderedLocusNames=RT0110;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
CC   -!- FUNCTION: Binds and transfers iron-sulfur (Fe-S) clusters to target
CC       apoproteins. Can hydrolyze ATP. {ECO:0000255|HAMAP-Rule:MF_02040}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02040}.
CC   -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC       {ECO:0000255|HAMAP-Rule:MF_02040}.
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DR   EMBL; AE017197; AAU03596.1; -; Genomic_DNA.
DR   RefSeq; WP_011190583.1; NC_006142.1.
DR   AlphaFoldDB; Q68XP6; -.
DR   SMR; Q68XP6; -.
DR   STRING; 257363.RT0110; -.
DR   EnsemblBacteria; AAU03596; AAU03596; RT0110.
DR   KEGG; rty:RT0110; -.
DR   eggNOG; COG0489; Bacteria.
DR   HOGENOM; CLU_024839_0_0_5; -.
DR   OMA; QHITFKD; -.
DR   OrthoDB; 1413173at2; -.
DR   Proteomes; UP000000604; 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   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_02040; Mrp_NBP35; 1.
DR   InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR   InterPro; IPR000808; Mrp_CS.
DR   InterPro; IPR044304; NUBPL-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR033756; YlxH/NBP35.
DR   PANTHER; PTHR42961; PTHR42961; 1.
DR   Pfam; PF10609; ParA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS01215; MRP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Hydrolase; Iron; Iron-sulfur; Metal-binding;
KW   Nucleotide-binding.
FT   CHAIN           1..318
FT                   /note="Iron-sulfur cluster carrier protein"
FT                   /id="PRO_0000281001"
FT   BINDING         105..112
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   318 AA;  35466 MW;  1CBDA0B6964B21B1 CRC64;
     MANLHQQQII DKIQNITFKD GTFLNEVISD IIIKGNNIGF SIDISGKNKL EAEEIRLKAI
     NELNNIKDVN NITIVFTQKK TIDKKAQKPK HFVENVKKII LVASGKGGVG KSTISALIAQ
     QLSLENYQVG IVDADIYGPS IPHIFGINEI PKTVEGRIIP ILAQNIQIIS IGFFVKAHSA
     IIYRGPMASK IIYQLLSNTR WNNLDYLIID MPPGTGDIHL SMLENYHLDG VIVVTTPQKI
     SEIDVIRSID LYRKLGLPIL GIIENMIYML ESDRCGHLSK KYNIPLIAKI PIIPQIANAC
     DKSLPLTNLL TLPLEKYL