APBC_CLOPE
ID APBC_CLOPE Reviewed; 284 AA.
AC P53381;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000255|HAMAP-Rule:MF_02040};
GN Name=mrp; OrderedLocusNames=CPE2512;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 50-189.
RC STRAIN=CPN50;
RX PubMed=7559358; DOI=10.1128/jb.177.19.5680-5685.1995;
RA Katayama S., Dupuy B., Garnier T., Cole S.T.;
RT "Rapid expansion of the physical and genetic map of the chromosome of
RT Clostridium perfringens CPN50.";
RL J. Bacteriol. 177:5680-5685(1995).
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}.
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DR EMBL; BA000016; BAB82218.1; -; Genomic_DNA.
DR EMBL; X86509; CAA60227.1; -; Genomic_DNA.
DR RefSeq; WP_003450706.1; NC_003366.1.
DR AlphaFoldDB; P53381; -.
DR SMR; P53381; -.
DR STRING; 195102.gene:10491846; -.
DR EnsemblBacteria; BAB82218; BAB82218; BAB82218.
DR GeneID; 29570049; -.
DR KEGG; cpe:CPE2512; -.
DR HOGENOM; CLU_024839_0_2_9; -.
DR OMA; QHITFKD; -.
DR Proteomes; UP000000818; 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; 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; 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..284
FT /note="Iron-sulfur cluster carrier protein"
FT /id="PRO_0000184930"
FT BINDING 46..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02040"
SQ SEQUENCE 284 AA; 30835 MW; 8CB32FBBF0510EAF CRC64;
MGSCASCANK DKCSSASKDG GCSSSVPAKL GTNYGNIKNV IGVISGKGGV GKSTVTGILA
TQLAKKGYKV GVLDADITGP SMPRFFGINE KRADIVAMDS EGKQVKFVPV KTELGIKVIS
MNLLMEVEDD PVIWRGPMVT GVLNQMFKDT DWEELDYLLI DMPPGTSDIT LTVMQTFPIK
ELVIVSTPQD MVSMIVKKLV TMAHKMNVCV RGVVENMAYI ECECGKKMRV FSKKSSEEHA
EYLGLPLIGE LPINLDLTEA LENGKAEEYV AENPLYSLIF EGLY