APBC_HELPY
ID APBC_HELPY Reviewed; 368 AA.
AC O24999;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000255|HAMAP-Rule:MF_02040};
GN Name=mrp; OrderedLocusNames=HP_0207;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AE000511; AAD07271.1; -; Genomic_DNA.
DR PIR; G64545; G64545.
DR RefSeq; NP_207006.1; NC_000915.1.
DR AlphaFoldDB; O24999; -.
DR SMR; O24999; -.
DR STRING; 85962.C694_01035; -.
DR PaxDb; O24999; -.
DR EnsemblBacteria; AAD07271; AAD07271; HP_0207.
DR KEGG; hpy:HP_0207; -.
DR PATRIC; fig|85962.47.peg.223; -.
DR eggNOG; COG0489; Bacteria.
DR OMA; NMAYFTP; -.
DR PhylomeDB; O24999; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..368
FT /note="Iron-sulfur cluster carrier protein"
FT /id="PRO_0000184935"
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; 40028 MW; 369E6804B2C48066 CRC64;
MLTQEDVLNA LKTIIYPNFE KDIVSFGFVK NITLHDDQLG LLIEIPSSSE ETSAILRENI
SKAMQEKGVK ALNLDIKTPP KPQAPKPTTK NLAKNIKHVV MISSGKGGVG KSTTSVNLSI
ALANLNQKVG LLDADVYGPN IPRMMGLQSA DVIMDPSGKK LIPLKAFGVS VMSMGLLYDE
GQSLIWRGPM LMRAIEQMLS DIIWGDLDVL VVDMPPGTGD AQLTLAQAVP LSAGITVTTP
QIVSLDDAKR SLDMFKKLHI PIAGIVENMG SFVCEHCKKE SEIFGSNSMS ELLEAYHTQI
LAKLPLEPKV RLGGDRGEPI VISHPNSVSA KIFEKMAQDL SAFLERVKKE KLADNKDIQP
TQTHACSH