ID   GRCA_ECO8A              Reviewed;         127 AA.
AC   B7M8J4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Autonomous glycyl radical cofactor {ECO:0000255|HAMAP-Rule:MF_00806};
GN   Name=grcA {ECO:0000255|HAMAP-Rule:MF_00806}; OrderedLocusNames=ECIAI1_2696;
OS   Escherichia coli O8 (strain IAI1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI1;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- FUNCTION: Acts as a radical domain for damaged PFL and possibly other
CC       radical proteins. {ECO:0000255|HAMAP-Rule:MF_00806}.
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DR   EMBL; CU928160; CAQ99531.1; -; Genomic_DNA.
DR   RefSeq; WP_000627807.1; NC_011741.1.
DR   AlphaFoldDB; B7M8J4; -.
DR   SMR; B7M8J4; -.
DR   GeneID; 66673531; -.
DR   KEGG; ecr:ECIAI1_2696; -.
DR   HOGENOM; CLU_133780_0_0_6; -.
DR   OMA; LGQFEYR; -.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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   3: Inferred from homology;
KW   Acetylation; Organic radical.
FT   CHAIN           1..127
FT                   /note="Autonomous glycyl radical cofactor"
FT                   /id="PRO_1000133984"
FT   DOMAIN          5..127
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00806"
FT   MOD_RES         48
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00806"
FT   MOD_RES         88
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00806"
FT   MOD_RES         92
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00806"
FT   MOD_RES         102
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00806"
SQ   SEQUENCE   127 AA;  14284 MW;  6BA617E67D6540CE CRC64;
     MITGIQITKA ANDDLLNSFW LLDSEKGEAR CIVAKAGYAE DEVVAVSKLG DIEYREVPVE
     VKPEVRVEGG QHLNVNVLRR ETLEDAVKHP EKYPQLTIRV SGYAVRFNSL TPEQQRDVIA
     RTFTESL