AC   MF_00105;
DC   Protein; auto
TR   HAMAP; MF_00105; -; 1; level=0
XX
Names: GreA_GreB
XX
ID   GREA
DE   RecName: Full=Transcription elongation factor GreA;
DE   AltName: Full=Transcript cleavage factor GreA;
GN   Name=greA;
XX
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   -!- SIMILARITY: Belongs to the GreA/GreB family.
XX
DR   PROSITE; PS00829; GREAB_1; 1; trigger=no
DR   PROSITE; PS00830; GREAB_2; 1; trigger=no
DR   Pfam; PF01272; GreA_GreB; 1; trigger=no
DR   Pfam; PF03449; GreA_GreB_N; 1; trigger=no
DR   NCBIfam; TIGR01462; greA; 1; trigger=no
DR   PIRSF; PIRSF006092; GreA_GreB; 1; trigger=no
DR   General; Coiled_coil; -; 0-unlimited; trigger=yes
XX
KW   Transcription
KW   Transcription regulation
KW   DNA-binding
XX
GO   GO:0003677; F:DNA binding
GO   GO:0032784; P:regulation of DNA-templated transcription elongation
XX
FT   None
XX
Size: 140-266;
Related: MF_00930!;
Template: P0A6W5;
Scope:
 Bacteria
Fusion:
 Nter: <GRAD1>; <GRAD2>
 Cter: None
Duplicate: None
Plasmid: None
Comments: In CHLPN and CHLTR the protein is fused to a N-terminal domain, GRAD1.
 In BORBU the protein is fused to both the GRAD1 domain and another N-terminal domain, GRAD2.
 Duplicate copy is called greB (annotated by MF_00930).
XX
# Revision 1.24 2023/06/01
//