ID   APBC_HELPJ              Reviewed;         368 AA.
AC   Q9ZMM5;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000255|HAMAP-Rule:MF_02040};
GN   Name=mrp; OrderedLocusNames=jhp_0193;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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}.
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DR   EMBL; AE001439; AAD05776.1; -; Genomic_DNA.
DR   PIR; H71962; H71962.
DR   AlphaFoldDB; Q9ZMM5; -.
DR   SMR; Q9ZMM5; -.
DR   STRING; 85963.jhp_0193; -.
DR   EnsemblBacteria; AAD05776; AAD05776; jhp_0193.
DR   KEGG; hpj:jhp_0193; -.
DR   PATRIC; fig|85963.30.peg.828; -.
DR   eggNOG; COG0489; Bacteria.
DR   OMA; NMAYFTP; -.
DR   Proteomes; UP000000804; 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..368
FT                   /note="Iron-sulfur cluster carrier protein"
FT                   /id="PRO_0000184936"
FT   BINDING         105..112
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   368 AA;  39965 MW;  7B524B695BF5AD12 CRC64;
     MLTQEDVLNA LKTIIYPNFE KDIVSFGFVK NITLHDNQLG LLIEIPSSSE ETSAILRENI
     SKAMQEKGVK ALNLDIKTPP KPQAPKPTTK NLAKNIKHVV MISSGKGGVG KSTTSVNLSI
     ALANLNQKVG LLDADVYGPN IPRMMGLQNA DVIMDPSGKK LIPLKAFGVS VMSMGLLYDE
     GQSLIWRGPM LMRAIEQMLS DIIWGDLDVL VVDMPPGTGD AQLTLAQAVP LSAGITVTTP
     QIVSLDDAKR SLDMFKKLHI PIAGIVENMG SFVCEHCKKE SEIFGSNSMS GLLEAYNTQI
     LAKLPLEPKV RLGGDKGEPI VISHPTSVSA KIFEKMAKDL SAFLDKVERE KLADNKDIQP
     TQTHAYSH