GREA_CLOBB
ID GREA_CLOBB Reviewed; 160 AA.
AC B2TI25;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Transcription elongation factor GreA {ECO:0000255|HAMAP-Rule:MF_00105};
DE AltName: Full=Transcript cleavage factor GreA {ECO:0000255|HAMAP-Rule:MF_00105};
GN Name=greA {ECO:0000255|HAMAP-Rule:MF_00105}; OrderedLocusNames=CLL_A0177;
OS Clostridium botulinum (strain Eklund 17B / Type B).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=935198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eklund 17B / Type B;
RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Complete sequence of Clostridium botulinum strain Eklund.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Necessary for efficient RNA polymerase transcription
CC elongation past template-encoded arresting sites. The arresting sites
CC in DNA have the property of trapping a certain fraction of elongating
CC RNA polymerases that pass through, resulting in locked ternary
CC complexes. Cleavage of the nascent transcript by cleavage factors such
CC as GreA or GreB allows the resumption of elongation from the new
CC 3'terminus. GreA releases sequences of 2 to 3 nucleotides.
CC {ECO:0000255|HAMAP-Rule:MF_00105}.
CC -!- SIMILARITY: Belongs to the GreA/GreB family. {ECO:0000255|HAMAP-
CC Rule:MF_00105}.
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DR EMBL; CP001056; ACD23137.1; -; Genomic_DNA.
DR RefSeq; WP_012423966.1; NC_018648.1.
DR AlphaFoldDB; B2TI25; -.
DR SMR; B2TI25; -.
DR EnsemblBacteria; ACD23137; ACD23137; CLL_A0177.
DR KEGG; cbk:CLL_A0177; -.
DR PATRIC; fig|935198.13.peg.161; -.
DR HOGENOM; CLU_101379_2_1_9; -.
DR OMA; TWLTQEA; -.
DR OrthoDB; 1536415at2; -.
DR Proteomes; UP000001195; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070063; F:RNA polymerase binding; IEA:InterPro.
DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.287.180; -; 1.
DR Gene3D; 3.10.50.30; -; 1.
DR HAMAP; MF_00105; GreA_GreB; 1.
DR InterPro; IPR036953; GreA/GreB_C_sf.
DR InterPro; IPR018151; TF_GreA/GreB_CS.
DR InterPro; IPR006359; Tscrpt_elong_fac_GreA.
DR InterPro; IPR028624; Tscrpt_elong_fac_GreA/B.
DR InterPro; IPR001437; Tscrpt_elong_fac_GreA/B_C.
DR InterPro; IPR023459; Tscrpt_elong_fac_GreA/B_fam.
DR InterPro; IPR022691; Tscrpt_elong_fac_GreA/B_N.
DR InterPro; IPR036805; Tscrpt_elong_fac_GreA/B_N_sf.
DR PANTHER; PTHR30437; PTHR30437; 1.
DR Pfam; PF01272; GreA_GreB; 1.
DR Pfam; PF03449; GreA_GreB_N; 1.
DR PIRSF; PIRSF006092; GreA_GreB; 1.
DR SUPFAM; SSF46557; SSF46557; 1.
DR TIGRFAMs; TIGR01462; greA; 1.
DR PROSITE; PS00829; GREAB_1; 1.
DR PROSITE; PS00830; GREAB_2; 1.
PE 3: Inferred from homology;
KW Coiled coil; DNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..160
FT /note="Transcription elongation factor GreA"
FT /id="PRO_1000094161"
FT COILED 49..75
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00105"
SQ SEQUENCE 160 AA; 17770 MW; E795B3D004930D2B CRC64;
MSEPKQYVMT YEGVKKLEGE LEYLKTVKRK EITEKIKVAL GYGDLSENSE YDEAKNDQAF
TEGKILQLEN KLKNAVVVDE SEIPKDIVSV GSKVKVKDYD FDEEVEYSIV GSAEADPMSF
KISNESPVGN ALVGKKIGDV VEVVVPDGVS KFEILDIKRG