CYAY_ECOLI
ID CYAY_ECOLI Reviewed; 106 AA.
AC P27838; Q2M8B2;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Iron-sulfur cluster assembly protein CyaY {ECO:0000255|HAMAP-Rule:MF_00142, ECO:0000305};
DE AltName: Full=Bacterial frataxin ortholog {ECO:0000303|PubMed:15530368};
GN Name=cyaY {ECO:0000255|HAMAP-Rule:MF_00142, ECO:0000303|PubMed:8874804};
GN OrderedLocusNames=b3807, JW3779;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6393056; DOI=10.1093/nar/12.24.9427;
RA Aiba H., Mori K., Tanaka M., Ooi T., Roy A., Danchin A.;
RT "The complete nucleotide sequence of the adenylate cyclase gene of
RT Escherichia coli.";
RL Nucleic Acids Res. 12:9427-9440(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8874804; DOI=10.1016/0300-9084(96)82192-4;
RA Trotot P., Sismeiro O., Vivares C., Glaser P., Bresson-Roy A., Danchin A.;
RT "Comparative analysis of the cya locus in enterobacteria and related Gram-
RT negative facultative anaerobes.";
RL Biochimie 78:277-287(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP IDENTIFICATION.
RX PubMed=8418825;
RA Danchin A.;
RT "Phylogeny of adenylyl cyclases.";
RL Adv. Second Messenger Phosphoprotein Res. 27:109-162(1993).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=10452520; DOI=10.1016/s0014-5793(99)00896-0;
RA Li D.S., Ohshima K., Jiralerspong S., Bojanowski M.W., Pandolfo M.;
RT "Knock-out of the cyaY gene in Escherichia coli does not affect cellular
RT iron content and sensitivity to oxidants.";
RL FEBS Lett. 456:13-16(1999).
RN [8]
RP FUNCTION, IRON-BINDING, SUBUNIT, AND INTERACTION WITH ISCS.
RX PubMed=16603772; DOI=10.1074/jbc.m513569200;
RA Layer G., Ollagnier-de Choudens S., Sanakis Y., Fontecave M.;
RT "Iron-sulfur cluster biosynthesis: characterization of Escherichia coli
RT CyaY as an iron donor for the assembly of [2Fe-2S] clusters in the scaffold
RT IscU.";
RL J. Biol. Chem. 281:16256-16263(2006).
RN [9]
RP IRON-BINDING, AND ACTIVITY REGULATION.
RX PubMed=17244611; DOI=10.1074/jbc.m609665200;
RA Ding H., Yang J., Coleman L.C., Yeung S.;
RT "Distinct iron binding property of two putative iron donors for the iron-
RT sulfur cluster assembly: IscA and the bacterial frataxin ortholog CyaY
RT under physiological and oxidative stress conditions.";
RL J. Biol. Chem. 282:7997-8004(2007).
RN [10]
RP FUNCTION, INTERACTION WITH ISCS, AND MUTAGENESIS OF GLU-18; GLU-19; ASP-22;
RP ASP-31 AND TRP-61.
RX PubMed=19305405; DOI=10.1038/nsmb.1579;
RA Adinolfi S., Iannuzzi C., Prischi F., Pastore C., Iametti S., Martin S.R.,
RA Bonomi F., Pastore A.;
RT "Bacterial frataxin CyaY is the gatekeeper of iron-sulfur cluster formation
RT catalyzed by IscS.";
RL Nat. Struct. Mol. Biol. 16:390-396(2009).
RN [11]
RP FUNCTION.
RX PubMed=21799759; DOI=10.1371/journal.pone.0021992;
RA Iannuzzi C., Adinolfi S., Howes B.D., Garcia-Serres R., Clemancey M.,
RA Latour J.M., Smulevich G., Pastore A.;
RT "The role of CyaY in iron sulfur cluster assembly on the E. coli IscU
RT scaffold protein.";
RL PLoS ONE 6:E21992-E21992(2011).
RN [12]
RP FUNCTION, AND INTERACTION WITH ISCS.
RX PubMed=25430730; DOI=10.1111/mmi.12888;
RA Roche B., Huguenot A., Barras F., Py B.;
RT "The iron-binding CyaY and IscX proteins assist the ISC-catalyzed Fe-S
RT biogenesis in Escherichia coli.";
RL Mol. Microbiol. 95:605-623(2015).
RN [13]
RP SUBUNIT.
RX PubMed=28931050; DOI=10.1371/journal.pone.0184961;
RA Fekry M., Alshokry W., Grela P., Tchorzewski M., Ahlgren E.C.,
RA Soederberg C.A., Gakh O., Isaya G., Al-Karadaghi S.;
RT "SAXS and stability studies of iron-induced oligomers of bacterial frataxin
RT CyaY.";
RL PLoS ONE 12:E0184961-E0184961(2017).
RN [14] {ECO:0007744|PDB:1EW4}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS).
RX PubMed=10908679; DOI=10.1073/pnas.160270897;
RA Cho S.J., Lee M.G., Yang J.K., Lee J.Y., Song H.K., Suh S.W.;
RT "Crystal structure of Escherichia coli CyaY protein reveals a previously
RT unidentified fold for the evolutionarily conserved frataxin family.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:8932-8937(2000).
RN [15] {ECO:0007744|PDB:1SOY}
RP STRUCTURE BY NMR, IRON-BINDING, AND MUTAGENESIS OF GLU-18; GLU-19 AND
RP ASP-22.
RX PubMed=15530368; DOI=10.1016/j.str.2004.08.012;
RA Nair M., Adinolfi S., Pastore C., Kelly G., Temussi P., Pastore A.;
RT "Solution structure of the bacterial frataxin ortholog, CyaY: mapping the
RT iron binding sites.";
RL Structure 12:2037-2048(2004).
RN [16] {ECO:0007744|PDB:2EFF, ECO:0007744|PDB:2P1X}
RP X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS), AND METAL-BINDING.
RX PubMed=17651435; DOI=10.1111/j.1742-4658.2007.05946.x;
RA Pastore C., Franzese M., Sica F., Temussi P., Pastore A.;
RT "Understanding the binding properties of an unusual metal-binding protein--
RT a study of bacterial frataxin.";
RL FEBS J. 274:4199-4210(2007).
CC -!- FUNCTION: Involved in iron-sulfur (Fe-S) cluster assembly
CC (PubMed:16603772, PubMed:19305405, PubMed:21799759, PubMed:25430730).
CC May act as a regulator of Fe-S biogenesis (PubMed:19305405,
CC PubMed:21799759, PubMed:25430730). Can bind both Fe(2+) and Fe(3+) ions
CC (PubMed:15530368, PubMed:16603772, PubMed:17244611, PubMed:17651435).
CC In vivo, has a positive effect on Fe-S cluster biogenesis under iron-
CC rich growth conditions (PubMed:25430730). In vitro, can inhibit IscS
CC cysteine desulfurase activity and the formation of Fe-S clusters on
CC IscU (PubMed:19305405, PubMed:21799759). In vitro, in the presence of
CC IscS and cysteine, Fe(3+)-CyaY can be used as an iron donor during Fe-S
CC cluster assembly on the scaffold protein IscU (PubMed:16603772).
CC {ECO:0000269|PubMed:15530368, ECO:0000269|PubMed:16603772,
CC ECO:0000269|PubMed:17244611, ECO:0000269|PubMed:17651435,
CC ECO:0000269|PubMed:19305405, ECO:0000269|PubMed:21799759,
CC ECO:0000269|PubMed:25430730}.
CC -!- ACTIVITY REGULATION: Binds iron under oxidative stress conditions, but
CC not under conditions emulating the intracellular redox potential.
CC {ECO:0000269|PubMed:17244611}.
CC -!- SUBUNIT: Monomer (PubMed:16603772, PubMed:19305405, PubMed:28931050).
CC Forms homodimers and higher oligomers in the presence of iron
CC (PubMed:16603772, PubMed:28931050). Interacts with IscS
CC (PubMed:16603772, PubMed:19305405, PubMed:25430730).
CC {ECO:0000269|PubMed:16603772, ECO:0000269|PubMed:19305405,
CC ECO:0000269|PubMed:25430730, ECO:0000269|PubMed:28931050}.
CC -!- INTERACTION:
CC P27838; P0A6B7: iscS; NbExp=2; IntAct=EBI-9146621, EBI-550055;
CC -!- DISRUPTION PHENOTYPE: Cells are not affected in cellular iron content
CC and sensitivity to oxidants. {ECO:0000269|PubMed:10452520}.
CC -!- SIMILARITY: Belongs to the frataxin family. {ECO:0000255|HAMAP-
CC Rule:MF_00142, ECO:0000305}.
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DR EMBL; X66782; CAA47281.1; -; Genomic_DNA.
DR EMBL; M87049; AAA67603.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76810.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77494.1; -; Genomic_DNA.
DR PIR; S30697; S30697.
DR RefSeq; NP_418251.1; NC_000913.3.
DR RefSeq; WP_000999947.1; NZ_STEB01000021.1.
DR PDB; 1EW4; X-ray; 1.40 A; A=1-106.
DR PDB; 1SOY; NMR; -; A=1-106.
DR PDB; 2EFF; X-ray; 1.80 A; A=1-106.
DR PDB; 2P1X; X-ray; 1.42 A; A=1-106.
DR PDBsum; 1EW4; -.
DR PDBsum; 1SOY; -.
DR PDBsum; 2EFF; -.
DR PDBsum; 2P1X; -.
DR AlphaFoldDB; P27838; -.
DR SASBDB; P27838; -.
DR SMR; P27838; -.
DR BioGRID; 4260671; 116.
DR BioGRID; 852066; 2.
DR DIP; DIP-9356N; -.
DR IntAct; P27838; 3.
DR STRING; 511145.b3807; -.
DR TCDB; 9.B.21.2.1; the frataxin (frataxin) family.
DR jPOST; P27838; -.
DR PaxDb; P27838; -.
DR PRIDE; P27838; -.
DR EnsemblBacteria; AAC76810; AAC76810; b3807.
DR EnsemblBacteria; BAE77494; BAE77494; BAE77494.
DR GeneID; 66672289; -.
DR GeneID; 947754; -.
DR KEGG; ecj:JW3779; -.
DR KEGG; eco:b3807; -.
DR PATRIC; fig|1411691.4.peg.2901; -.
DR EchoBASE; EB1606; -.
DR eggNOG; COG1965; Bacteria.
DR HOGENOM; CLU_080880_3_0_6; -.
DR InParanoid; P27838; -.
DR OMA; EPMHEIW; -.
DR PhylomeDB; P27838; -.
DR BioCyc; EcoCyc:EG11653-MON; -.
DR BioCyc; MetaCyc:EG11653-MON; -.
DR EvolutionaryTrace; P27838; -.
DR PRO; PR:P27838; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008199; F:ferric iron binding; IDA:EcoCyc.
DR GO; GO:0008198; F:ferrous iron binding; IDA:EcoCyc.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:EcoliWiki.
DR Gene3D; 3.30.920.10; -; 1.
DR HAMAP; MF_00142; CyaY; 1.
DR InterPro; IPR002908; Frataxin/CyaY.
DR InterPro; IPR036524; Frataxin/CyaY_sf.
DR InterPro; IPR020895; Frataxin_CS.
DR PANTHER; PTHR16821; PTHR16821; 1.
DR Pfam; PF01491; Frataxin_Cyay; 1.
DR SMART; SM01219; Frataxin_Cyay; 1.
DR SUPFAM; SSF55387; SSF55387; 1.
DR TIGRFAMs; TIGR03421; FeS_CyaY; 1.
DR PROSITE; PS01344; FRATAXIN_1; 1.
DR PROSITE; PS50810; FRATAXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Iron; Metal-binding; Reference proteome.
FT CHAIN 1..106
FT /note="Iron-sulfur cluster assembly protein CyaY"
FT /id="PRO_0000193936"
FT MUTAGEN 18
FT /note="E->K: Abolishes iron binding and increases kinetics
FT of Fe-S formation on IscU; when associated with K-19 and K-
FT 22."
FT /evidence="ECO:0000269|PubMed:15530368,
FT ECO:0000269|PubMed:19305405"
FT MUTAGEN 19
FT /note="E->K: Abolishes iron binding and increases kinetics
FT of Fe-S formation on IscU; when associated with K-18 and K-
FT 22."
FT /evidence="ECO:0000269|PubMed:15530368,
FT ECO:0000269|PubMed:19305405"
FT MUTAGEN 22
FT /note="D->K: Abolishes iron binding and increases kinetics
FT of Fe-S formation on IscU; when associated with K-18 and K-
FT 19."
FT /evidence="ECO:0000269|PubMed:15530368,
FT ECO:0000269|PubMed:19305405"
FT MUTAGEN 31
FT /note="D->K: Increases kinetics of Fe-S formation on IscU."
FT /evidence="ECO:0000269|PubMed:19305405"
FT MUTAGEN 61
FT /note="W->R: Increases kinetics of Fe-S formation on IscU."
FT /evidence="ECO:0000269|PubMed:19305405"
FT HELIX 3..22
FT /evidence="ECO:0007829|PDB:1EW4"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:1EW4"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:1EW4"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:1EW4"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:1EW4"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:1EW4"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:1EW4"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:1EW4"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:1EW4"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1EW4"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:1EW4"
SQ SEQUENCE 106 AA; 12231 MW; 03EA6F330A48F711 CRC64;
MNDSEFHRLA DQLWLTIEER LDDWDGDSDI DCEINGGVLT ITFENGSKII INRQEPLHQV
WLATKQGGYH FDLKGDEWIC DRSGETFWDL LEQAATQQAG ETVSFR
