GREA_CLOBA
ID GREA_CLOBA Reviewed; 160 AA.
AC B2UXU9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=CLH_0170;
OS Clostridium botulinum (strain Alaska E43 / Type E3).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=508767;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alaska E43 / Type E3;
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 genome sequence of Clostridium botulinum E3 str. Alaska E43.";
RL Submitted (MAY-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; CP001078; ACD53886.1; -; Genomic_DNA.
DR RefSeq; WP_003371947.1; NC_010723.1.
DR AlphaFoldDB; B2UXU9; -.
DR SMR; B2UXU9; -.
DR KEGG; cbt:CLH_0170; -.
DR HOGENOM; CLU_101379_2_1_9; -.
DR OMA; TWLTQEA; -.
DR OrthoDB; 1536415at2; -.
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_1000094160"
FT COILED 49..75
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00105"
SQ SEQUENCE 160 AA; 17798 MW; 97E5A7F3C1FFD87B CRC64;
MSEPKQYVMT YEGVKKLEGE LEYLKTVKRK EITEKIKVAL GYGDLSENSE YDEAKNDQAF
TEGKILQLEN KLKNAVVVDE SEIPKDIVSV GSKVKVKDYD FDEEVEYSIV GSAEADPMSF
KISNESPVGK ALVGKKIGDI VDVVVPDGIS KFEILDIQRG