APBC_DEIRA
ID APBC_DEIRA Reviewed; 350 AA.
AC Q9RVM9;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000255|HAMAP-Rule:MF_02040};
GN Name=mrp; OrderedLocusNames=DR_0998;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(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; AE000513; AAF10574.1; -; Genomic_DNA.
DR PIR; F75448; F75448.
DR RefSeq; NP_294722.1; NC_001263.1.
DR RefSeq; WP_010887641.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RVM9; -.
DR SMR; Q9RVM9; -.
DR STRING; 243230.DR_0998; -.
DR EnsemblBacteria; AAF10574; AAF10574; DR_0998.
DR KEGG; dra:DR_0998; -.
DR PATRIC; fig|243230.17.peg.1187; -.
DR eggNOG; COG0489; Bacteria.
DR HOGENOM; CLU_024839_0_0_0; -.
DR InParanoid; Q9RVM9; -.
DR OMA; NMAYFTP; -.
DR OrthoDB; 1413173at2; -.
DR Proteomes; UP000002524; Chromosome I.
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..350
FT /note="Iron-sulfur cluster carrier protein"
FT /id="PRO_0000184931"
FT BINDING 99..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02040"
SQ SEQUENCE 350 AA; 36913 MW; EC0579B8EF522CAB CRC64;
MNDALLRALS TVNDPELHRD LVSLGMIERA ELSGDVAQVK VNLTTPACPL KGQIELDVRS
ALLQVPGVRD VQIEFGAMVR AATQPALPGV KHVVLVGSGK GGVGKSSVAV NLAASLARDG
ARVGLLDADV YGPSVAHMLG QGQARVTANE DRKMRPIEAH GVRFISMANL SPAGQALVWR
GPMLHSAIQQ FLKDSAWGEL DYLIVDLPPG TGDVQLSLTQ TVQVTGAVIV TTPQDVALID
AARAIDMFRK ASVPVLGVVE NMSYFVAPDT GLTYDIFGRG GSRKLGEQYP LLGEIPLDVE
VRKDADAGAP AILAHPESVA AQALRAVART LAGQISVRTL SELPEQLPVL