ID   APBC_MYCTO              Reviewed;         381 AA.
AC   P9WJN6; L0T7N6; O33225; P65441;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000255|HAMAP-Rule:MF_02040};
GN   Name=mrp; OrderedLocusNames=MT1267;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(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: In the N-terminal section; belongs to the MIP18 family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the Mrp/NBP35 ATP-
CC       binding proteins family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK45525.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK45525.1; ALT_INIT; Genomic_DNA.
DR   PIR; H70508; H70508.
DR   AlphaFoldDB; P9WJN6; -.
DR   SMR; P9WJN6; -.
DR   EnsemblBacteria; AAK45525; AAK45525; MT1267.
DR   KEGG; mtc:MT1267; -.
DR   HOGENOM; CLU_024839_0_0_11; -.
DR   Proteomes; UP000001020; 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; 3.30.300.130; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_02040; Mrp_NBP35; 1.
DR   InterPro; IPR034904; FSCA_dom_sf.
DR   InterPro; IPR002744; MIP18-like.
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; PF01883; FeS_assembly_P; 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..381
FT                   /note="Iron-sulfur cluster carrier protein"
FT                   /id="PRO_0000427797"
FT   BINDING         125..132
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   381 AA;  40084 MW;  4EEB863B79D6B91A CRC64;
     MSGTRDGDLN AAIRTALGKV IDPELRRPIT ELGMVKSIDT GPDGSVHVEI YLTIAGCPKK
     SEITERVTRA VADVPGTSAV RVSLDVMSDE QRTELRKQLR GDTREPVIPF AQPDSLTRVY
     AVASGKGGVG KSTVTVNLAA AMAVRGLSIG VLDADIHGHS IPRMMGTTDR PTQVESMILP
     PIAHQVKVIS IAQFTQGNTP VVWRGPMLHR ALQQFLADVY WGDLDVLLLD LPPGTGDVAI
     SVAQLIPNAE LLVVTTPQLA AAEVAERAGS IALQTRQRIV GVVENMSGLT LPDGTTMQVF
     GEGGGRLVAE RLSRAVGADV PLLGQIPLDP ALVAAGDSGV PLVLSSPDSA IGKELHSIAD
     GLSTRRRGLA GMSLGLDPTR R