FRA_BACSU
ID FRA_BACSU Reviewed; 123 AA.
AC Q797E6; O05499;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Intracellular iron chaperone frataxin;
DE AltName: Full=Fra;
DE AltName: Full=Iron channeling protein frataxin;
GN Name=fra; Synonyms=ydhG; OrderedLocusNames=BSU05750;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=9202461; DOI=10.1099/00221287-143-6-1861;
RA Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y.,
RA Ogasawara N.;
RT "Nucleotide sequence and analysis of the phoB-rrnE-groESL region of the
RT Bacillus subtilis chromosome.";
RL Microbiology 143:1861-1866(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, SUBUNIT, AND IRON-BINDING.
RC STRAIN=168 / ATCC 23857D;
RX PubMed=20087498; DOI=10.1039/b911975b;
RA Qi W., Cowan J.A.;
RT "A structural and functional homolog supports a general role for frataxin
RT in cellular iron chemistry.";
RL Chem. Commun. (Camb.) 46:719-721(2010).
RN [4]
RP FUNCTION, IRON-BINDING, COFACTOR, SUBCELLULAR LOCATION, IDENTIFICATION BY
RP MASS SPECTROMETRY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 21332 / IAM 1213;
RX PubMed=21744456; DOI=10.1002/cbic.201100190;
RA Albrecht A.G., Landmann H., Nette D., Burghaus O., Peuckert F., Seubert A.,
RA Miethke M., Marahiel M.A.;
RT "The frataxin homologue Fra plays a key role in intracellular iron
RT channeling in Bacillus subtilis.";
RL ChemBioChem 12:2052-2061(2011).
RN [5]
RP FUNCTION, INTERACTION WITH CPFC, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=25826316; DOI=10.1371/journal.pone.0122538;
RA Mielcarek A., Blauenburg B., Miethke M., Marahiel M.A.;
RT "Molecular insights into frataxin-mediated iron supply for heme
RT biosynthesis in Bacillus subtilis.";
RL PLoS ONE 10:e0122538-e0122538(2015).
RN [6]
RP FUNCTION, AND INTERACTION WITH SUFU AND SUFS.
RC STRAIN=168;
RX PubMed=27382962; DOI=10.1371/journal.pone.0158749;
RA Blauenburg B., Mielcarek A., Altegoer F., Fage C.D., Linne U., Bange G.,
RA Marahiel M.A.;
RT "Crystal Structure of Bacillus subtilis Cysteine Desulfurase SufS and Its
RT Dynamic Interaction with Frataxin and Scaffold Protein SufU.";
RL PLoS ONE 11:e0158749-e0158749(2016).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of hypothetical protein (NP_388456.1) from Bacillus
RT subtilis at 1.75 A resolution.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Plays an essential role in iron intracellular trafficking to
CC iron cofactor biogenesis systems including iron-sulfur cluster (Fe-S)
CC or heme assembly (PubMed:21744456, PubMed:25826316). Promotes the
CC biosynthesis of iron-sulfur clusters by delivering Fe to the complex
CC composed of the cysteine desulfurase SufS and the zinc-dependent
CC sulfurtransferase SufU (PubMed:27382962). Also plays a critical role in
CC coproporphyrin-dependent heme b biogenesis and thus provides an
CC essential function for the bacterial global metabolism.
CC {ECO:0000269|PubMed:20087498, ECO:0000269|PubMed:21744456,
CC ECO:0000269|PubMed:25826316, ECO:0000269|PubMed:27382962}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:20087498, ECO:0000269|PubMed:21744456};
CC Note=Binds 1.0 Fe(2+) (PubMed:20087498) to 1.5 to 3.2 Fe(2+) per
CC monomer (PubMed:21744456). {ECO:0000269|PubMed:20087498,
CC ECO:0000269|PubMed:21744456};
CC -!- SUBUNIT: Homodimer, upon Fe(2+) binding (PubMed:20087498). Interacts
CC with the SufS/SufU complex (PubMed:27382962). Interacts with CpfC
CC (PubMed:25826316). {ECO:0000269|PubMed:20087498,
CC ECO:0000269|PubMed:25826316, ECO:0000269|PubMed:27382962}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21744456}.
CC -!- DISRUPTION PHENOTYPE: Reduced growth in rich medium, unable to grow in
CC minimal medium. Reduced activity of Fe-S-dependent aconitase (citB).
CC Reactive oxygen species are drastically reduced. No bacillibactin (BB),
CC an endogenous siderophore, produced. 20% higher intracellular iron
CC concentrations. {ECO:0000269|PubMed:21744456}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA19699.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D88802; BAA19699.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB12394.1; -; Genomic_DNA.
DR PIR; C69784; C69784.
DR RefSeq; NP_388456.1; NC_000964.3.
DR RefSeq; WP_003244145.1; NZ_JNCM01000031.1.
DR PDB; 2OC6; X-ray; 1.75 A; A/B=1-123.
DR PDBsum; 2OC6; -.
DR AlphaFoldDB; Q797E6; -.
DR SMR; Q797E6; -.
DR STRING; 224308.BSU05750; -.
DR PaxDb; Q797E6; -.
DR PRIDE; Q797E6; -.
DR EnsemblBacteria; CAB12394; CAB12394; BSU_05750.
DR GeneID; 938031; -.
DR KEGG; bsu:BSU05750; -.
DR PATRIC; fig|224308.179.peg.618; -.
DR eggNOG; COG5646; Bacteria.
DR InParanoid; Q797E6; -.
DR OMA; IAWNQPM; -.
DR PhylomeDB; Q797E6; -.
DR BioCyc; BSUB:BSU05750-MON; -.
DR EvolutionaryTrace; Q797E6; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR InterPro; IPR014922; DUF1801.
DR Pfam; PF08818; DUF1801; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Ion transport; Iron; Iron transport;
KW Metal-binding; Reference proteome; Transport.
FT CHAIN 1..123
FT /note="Intracellular iron chaperone frataxin"
FT /id="PRO_0000386478"
FT HELIX 1..4
FT /evidence="ECO:0007829|PDB:2OC6"
FT HELIX 5..9
FT /evidence="ECO:0007829|PDB:2OC6"
FT HELIX 14..30
FT /evidence="ECO:0007829|PDB:2OC6"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:2OC6"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:2OC6"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:2OC6"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:2OC6"
FT HELIX 68..73
FT /evidence="ECO:0007829|PDB:2OC6"
FT HELIX 75..81
FT /evidence="ECO:0007829|PDB:2OC6"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:2OC6"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:2OC6"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:2OC6"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:2OC6"
SQ SEQUENCE 123 AA; 14418 MW; 8F6082B87D704912 CRC64;
MDVFSEYLAG IADPFHRERT EEVLTWIKNK YPNLHTEIKW NQPMFTDHGT FIIGFSVSKK
HLAVAPEKVT IAHVEDDIVK AGYDYTEQLI RIPWNGPVDY TLLEKMIEFN ILDKADCSTF
WRK
