ID   APBC_ECOL6              Reviewed;         369 AA.
AC   P0AF09; P21590;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000255|HAMAP-Rule:MF_02040};
GN   Name=mrp; OrderedLocusNames=c2641;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN81097.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN81097.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001005448.1; NC_004431.1.
DR   AlphaFoldDB; P0AF09; -.
DR   SMR; P0AF09; -.
DR   STRING; 199310.c2641; -.
DR   PRIDE; P0AF09; -.
DR   EnsemblBacteria; AAN81097; AAN81097; c2641.
DR   GeneID; 66673991; -.
DR   KEGG; ecc:c2641; -.
DR   eggNOG; COG0489; Bacteria.
DR   HOGENOM; CLU_024839_0_0_6; -.
DR   OMA; NMAYFTP; -.
DR   Proteomes; UP000001410; 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; IPR034904; FSCA_dom_sf.
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; SSF117916; SSF117916; 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..369
FT                   /note="Iron-sulfur cluster carrier protein"
FT                   /id="PRO_0000184933"
FT   BINDING         115..122
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   369 AA;  39938 MW;  F3437F3A6408042E CRC64;
     MNEQSQAKSP EALRAMVAGT LANFQHPTLK HNLTTLKALH HVAWMDDTLH VELVMPFVWH
     SAFEELKEQC SAELLRITGA KAIDWKLSHN IATLKRVKNQ PGINGVKNII AVSSGKGGVG
     KSSTAVNLAL ALAAEGAKVG ILDADIYGPS IPTMLGAENQ RPTSPDGTHM APIMSHGLAT
     NSIGYLVTDD NAMVWRGPMA SKALMQMLQE TLWPDLDYLV LDMPPGTGDI QLTLAQNIPV
     TGAVVVTTPQ DIALIDAKKG IVMFEKVEVP VLGIVENMSV HICSNCGHHE PIFGTGGAEK
     LAEKYHTQLL GQMPLHISLR EDLDKGTPTV ISRPESEFTA IYRQLADRVA AQLYWQGEVI
     PGEISFRAV