GRCA_ECOLI
ID GRCA_ECOLI Reviewed; 127 AA.
AC P68066; P33633;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Autonomous glycyl radical cofactor;
GN Name=grcA; Synonyms=yfiD; OrderedLocusNames=b2579, JW2563;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Nashimoto H.;
RT "Non-ribosomal proteins affecting the assembly of ribosomes in Escherichia
RT coli.";
RL (In) Nierhaus K.H. (eds.);
RL The translational apparatus, pp.185-195, Plenum Press, New York (1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Nashimoto H., Saito N.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-76.
RX PubMed=2836397; DOI=10.1016/s0021-9258(18)68566-7;
RA Varshney U., Hutcheon T., de Sande J.H.;
RT "Sequence analysis, expression, and conservation of Escherichia coli uracil
RT DNA glycosylase and its gene (ung).";
RL J. Biol. Chem. 263:7776-7784(1988).
RN [7]
RP PROTEIN SEQUENCE OF 1-10.
RC STRAIN=K12;
RX PubMed=9868784; DOI=10.1111/j.1574-6968.1998.tb13343.x;
RA Wasinger V.C., Humphery-Smith I.;
RT "Small genes/gene-products in Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 169:375-382(1998).
RN [8]
RP PROTEIN SEQUENCE OF 1-4.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [9]
RP IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [11]
RP INDUCTION.
RX PubMed=11932447; DOI=10.1099/00221287-148-4-1015;
RA Wyborn N.R., Messenger S.L., Henderson R.A., Sawers G., Roberts R.E.,
RA Attwood M.M., Green J.;
RT "Expression of the Escherichia coli yfiD gene responds to intracellular pH
RT and reduces the accumulation of acidic metabolic end products.";
RL Microbiology 148:1015-1026(2002).
RN [12]
RP FUNCTION.
RX PubMed=11444864; DOI=10.1006/bbrc.2001.5186;
RA Wagner A.F.V., Schultz S., Bomke J., Pils T., Lehmann W.D., Knappe J.;
RT "YfiD of Escherichia coli and Y06I of bacteriophage T4 as autonomous glycyl
RT radical cofactors reconstituting the catalytic center of oxygen-fragmented
RT pyruvate formate-lyase.";
RL Biochem. Biophys. Res. Commun. 285:456-462(2001).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48; LYS-88 AND LYS-92, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [14]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=22412352; DOI=10.1371/journal.pbio.1001281;
RA Erental A., Sharon I., Engelberg-Kulka H.;
RT "Two programmed cell death systems in Escherichia coli: an apoptotic-like
RT death is inhibited by the mazEF-mediated death pathway.";
RL PLoS Biol. 10:E1001281-E1001281(2012).
CC -!- FUNCTION: Acts as a radical domain for damaged PFL and possibly other
CC radical proteins. {ECO:0000269|PubMed:11444864}.
CC -!- INTERACTION:
CC P68066; P0A9K9: slyD; NbExp=3; IntAct=EBI-561424, EBI-369251;
CC -!- INDUCTION: By acid stress. {ECO:0000269|PubMed:11932447}.
CC -!- DISRUPTION PHENOTYPE: Cells undergo an apoptotic-like death upon DNA
CC damage characterized by membrane depolarization; further disruption of
CC recA prevents membrane depolarization. {ECO:0000269|PubMed:22412352}.
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DR EMBL; D13169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D64044; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U00096; AAC75632.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16465.1; -; Genomic_DNA.
DR EMBL; J03725; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B65036; B65036.
DR RefSeq; NP_417074.1; NC_000913.3.
DR RefSeq; WP_000627807.1; NZ_STEB01000011.1.
DR PDB; 6OWR; NMR; -; A=1-127.
DR PDBsum; 6OWR; -.
DR AlphaFoldDB; P68066; -.
DR SMR; P68066; -.
DR BioGRID; 4263475; 8.
DR DIP; DIP-47913N; -.
DR IntAct; P68066; 18.
DR STRING; 511145.b2579; -.
DR iPTMnet; P68066; -.
DR SWISS-2DPAGE; P68066; -.
DR jPOST; P68066; -.
DR PaxDb; P68066; -.
DR PRIDE; P68066; -.
DR EnsemblBacteria; AAC75632; AAC75632; b2579.
DR EnsemblBacteria; BAA16465; BAA16465; BAA16465.
DR GeneID; 66673531; -.
DR GeneID; 947068; -.
DR KEGG; ecj:JW2563; -.
DR KEGG; eco:b2579; -.
DR PATRIC; fig|1411691.4.peg.4155; -.
DR EchoBASE; EB1732; -.
DR eggNOG; COG3445; Bacteria.
DR HOGENOM; CLU_133780_0_0_6; -.
DR OMA; LGQFEYR; -.
DR PhylomeDB; P68066; -.
DR BioCyc; EcoCyc:EG11784-MON; -.
DR PRO; PR:P68066; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008861; F:formate C-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0006567; P:threonine catabolic process; IBA:GO_Central.
DR HAMAP; MF_00806; GrcA; 1.
DR InterPro; IPR019777; Form_AcTrfase_GR_CS.
DR InterPro; IPR001150; Gly_radical.
DR InterPro; IPR011140; Glycyl_radical_cofactor_GrcA.
DR Pfam; PF01228; Gly_radical; 1.
DR PIRSF; PIRSF000378; Gly_radicl_yfiD; 1.
DR TIGRFAMs; TIGR04365; spare_glycyl; 1.
DR PROSITE; PS00850; GLY_RADICAL_1; 1.
DR PROSITE; PS51149; GLY_RADICAL_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Organic radical;
KW Reference proteome; Stress response.
FT CHAIN 1..127
FT /note="Autonomous glycyl radical cofactor"
FT /id="PRO_0000166697"
FT DOMAIN 5..127
FT /note="Glycine radical"
FT MOD_RES 48
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 88
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 92
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 102
FT /note="Glycine radical"
FT /evidence="ECO:0000250"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:6OWR"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:6OWR"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6OWR"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:6OWR"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:6OWR"
FT HELIX 112..120
FT /evidence="ECO:0007829|PDB:6OWR"
SQ SEQUENCE 127 AA; 14284 MW; 6BA617E67D6540CE CRC64;
MITGIQITKA ANDDLLNSFW LLDSEKGEAR CIVAKAGYAE DEVVAVSKLG DIEYREVPVE
VKPEVRVEGG QHLNVNVLRR ETLEDAVKHP EKYPQLTIRV SGYAVRFNSL TPEQQRDVIA
RTFTESL
