CSDE_ECOLI
ID CSDE_ECOLI Reviewed; 147 AA.
AC P0AGF2; Q2MA23; Q46926;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Sulfur acceptor protein CsdE;
GN Name=csdE; Synonyms=ygdK; OrderedLocusNames=b2811, JW2782;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP FUNCTION, GENE NAME, INTERACTION WITH CSDA, SUBUNIT, SULFHYDRATION AT
RP CYS-61, AND MUTAGENESIS OF CYS-61.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15901727; DOI=10.1074/jbc.m504067200;
RA Loiseau L., Ollagnier-de Choudens S., Lascoux D., Forest E., Fontecave M.,
RA Barras F.;
RT "Analysis of the heteromeric CsdA-CsdE cysteine desulfurase, assisting Fe-S
RT cluster biogenesis in Escherichia coli.";
RL J. Biol. Chem. 280:26760-26769(2005).
RN [4]
RP FUNCTION, INTERACTION WITH CSDA AND TCDA, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=20054882; DOI=10.1111/j.1365-2958.2009.06954.x;
RA Trotter V., Vinella D., Loiseau L., Ollagnier de Choudens S., Fontecave M.,
RA Barras F.;
RT "The CsdA cysteine desulphurase promotes Fe/S biogenesis by recruiting Suf
RT components and participates in a new sulphur transfer pathway by recruiting
RT CsdL (ex-YgdL), a ubiquitin-modifying-like protein.";
RL Mol. Microbiol. 74:1527-1542(2009).
RN [5]
RP FUNCTION, ROLE IN CT(6)A37 FORMATION, AND DISRUPTION PHENOTYPE.
RX PubMed=23242255; DOI=10.1038/nchembio.1137;
RA Miyauchi K., Kimura S., Suzuki T.;
RT "A cyclic form of N6-threonylcarbamoyladenosine as a widely distributed
RT tRNA hypermodification.";
RL Nat. Chem. Biol. 9:105-111(2013).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=15930006; DOI=10.1110/ps.041322705;
RA Liu G., Li Z., Chiang Y., Acton T., Montelione G.T., Murray D.,
RA Szyperski T.;
RT "High-quality homology models derived from NMR and X-ray structures of E.
RT coli proteins YgdK and SufE suggest that all members of the YgdK/SufE
RT protein family are enhancers of cysteine desulfurases.";
RL Protein Sci. 14:1597-1608(2005).
CC -!- FUNCTION: Stimulates the cysteine desulfurase activity of CsdA.
CC Contains a cysteine residue (Cys-61) that acts to accept sulfur
CC liberated via the desulfurase activity of CsdA. May be able to transfer
CC sulfur to TcdA/CsdL. Seems to support the function of TcdA in the
CC generation of cyclic threonylcarbamoyladenosine at position 37
CC (ct(6)A37) in tRNAs that read codons beginning with adenine. Does not
CC appear to participate in Fe/S biogenesis. {ECO:0000269|PubMed:15901727,
CC ECO:0000269|PubMed:20054882, ECO:0000269|PubMed:23242255}.
CC -!- SUBUNIT: Homodimer. Forms a heterodimer with CsdA. Interacts with CsdA
CC and with TcdA/CsdL. {ECO:0000269|PubMed:15901727,
CC ECO:0000269|PubMed:20054882}.
CC -!- INTERACTION:
CC P0AGF2; Q46925: csdA; NbExp=8; IntAct=EBI-1130454, EBI-545660;
CC P0AGF2; Q46927: tcdA; NbExp=3; IntAct=EBI-1130454, EBI-1130463;
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene display a high decrease
CC in the level of ct(6)A modification in tRNAs, and show the t(6)A
CC modification instead. They also show no defects in motility, fitness or
CC antibiotic sensitivity, in contrast to csdA mutants.
CC {ECO:0000269|PubMed:20054882, ECO:0000269|PubMed:23242255}.
CC -!- SIMILARITY: Belongs to the SufE family. {ECO:0000305}.
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DR EMBL; U29581; AAB40461.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75853.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76883.1; -; Genomic_DNA.
DR PIR; G65063; G65063.
DR RefSeq; NP_417291.1; NC_000913.3.
DR RefSeq; WP_000184261.1; NZ_SSUV01000026.1.
DR PDB; 1NI7; NMR; -; A=1-147.
DR PDB; 5EEP; X-ray; 2.40 A; A=1-147.
DR PDB; 5FT8; X-ray; 2.50 A; B/D/F/H/J/L/N/P=1-147.
DR PDB; 5NQ6; X-ray; 2.40 A; A/B=1-147.
DR PDBsum; 1NI7; -.
DR PDBsum; 5EEP; -.
DR PDBsum; 5FT8; -.
DR PDBsum; 5NQ6; -.
DR AlphaFoldDB; P0AGF2; -.
DR BMRB; P0AGF2; -.
DR SMR; P0AGF2; -.
DR BioGRID; 4261123; 398.
DR BioGRID; 851604; 1.
DR ComplexPortal; CPX-2138; cdsA-cdsE complex.
DR DIP; DIP-12143N; -.
DR IntAct; P0AGF2; 5.
DR STRING; 511145.b2811; -.
DR jPOST; P0AGF2; -.
DR PaxDb; P0AGF2; -.
DR PRIDE; P0AGF2; -.
DR EnsemblBacteria; AAC75853; AAC75853; b2811.
DR EnsemblBacteria; BAE76883; BAE76883; BAE76883.
DR GeneID; 947274; -.
DR KEGG; ecj:JW2782; -.
DR KEGG; eco:b2811; -.
DR PATRIC; fig|1411691.4.peg.3922; -.
DR EchoBASE; EB2892; -.
DR eggNOG; COG2166; Bacteria.
DR HOGENOM; CLU_124502_1_0_6; -.
DR InParanoid; P0AGF2; -.
DR OMA; HYFLADS; -.
DR PhylomeDB; P0AGF2; -.
DR BioCyc; EcoCyc:G7455-MON; -.
DR BioCyc; MetaCyc:G7455-MON; -.
DR EvolutionaryTrace; P0AGF2; -.
DR PRO; PR:P0AGF2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990221; C:L-cysteine desulfurase complex; IPI:ComplexPortal.
DR GO; GO:1990228; C:sulfurtransferase complex; IPI:ComplexPortal.
DR GO; GO:0097163; F:sulfur carrier activity; IMP:EcoCyc.
DR GO; GO:0061504; P:cyclic threonylcarbamoyladenosine biosynthetic process; IMP:EcoCyc.
DR GO; GO:0019448; P:L-cysteine catabolic process; IDA:ComplexPortal.
DR InterPro; IPR017763; Cysteine_desulfurase_CsdE.
DR InterPro; IPR003808; Fe-S_metab-assoc_dom.
DR PANTHER; PTHR43597; PTHR43597; 1.
DR Pfam; PF02657; SufE; 1.
DR TIGRFAMs; TIGR03391; FeS_syn_CsdE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome.
FT CHAIN 1..147
FT /note="Sulfur acceptor protein CsdE"
FT /id="PRO_0000202136"
FT ACT_SITE 61
FT /note="Cysteine persulfide intermediate"
FT MOD_RES 61
FT /note="Cysteine persulfide"
FT /evidence="ECO:0000269|PubMed:15901727"
FT MUTAGEN 61
FT /note="C->S: Unable to exert a stimulatory effect on the
FT cysteine desulfurase activity of CsdA and to accept sulfur.
FT Retains the ability to interact with CsdA."
FT /evidence="ECO:0000269|PubMed:15901727"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:5EEP"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:5EEP"
FT HELIX 30..41
FT /evidence="ECO:0007829|PDB:5EEP"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:5EEP"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:5EEP"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:1NI7"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:5EEP"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1NI7"
FT STRAND 77..85
FT /evidence="ECO:0007829|PDB:5EEP"
FT HELIX 86..99
FT /evidence="ECO:0007829|PDB:5EEP"
FT HELIX 104..109
FT /evidence="ECO:0007829|PDB:5EEP"
FT HELIX 114..119
FT /evidence="ECO:0007829|PDB:5EEP"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:5NQ6"
FT HELIX 127..145
FT /evidence="ECO:0007829|PDB:5EEP"
SQ SEQUENCE 147 AA; 15940 MW; EECAB64427D42C41 CRC64;
MTNPQFAGHP FGTTVTAETL RNTFAPLTQW EDKYRQLIML GKQLPALPDE LKAQAKEIAG
CENRVWLGYT VAENGKMHFF GDSEGRIVRG LLAVLLTAVE GKTAAELQAQ SPLALFDELG
LRAQLSASRS QGLNALSEAI IAATKQV
