ID   GREA_CLOBJ              Reviewed;         160 AA.
AC   C1FNC6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=CLM_4005;
OS   Clostridium botulinum (strain Kyoto / Type A2).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=536232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kyoto / Type A2;
RA   Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA   Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT   "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL   Submitted (OCT-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; CP001581; ACO84451.1; -; Genomic_DNA.
DR   RefSeq; WP_003359344.1; NC_012563.1.
DR   AlphaFoldDB; C1FNC6; -.
DR   SMR; C1FNC6; -.
DR   STRING; 536232.CLM_4005; -.
DR   EnsemblBacteria; ACO84451; ACO84451; CLM_4005.
DR   KEGG; cby:CLM_4005; -.
DR   eggNOG; COG0782; Bacteria.
DR   HOGENOM; CLU_101379_2_1_9; -.
DR   OMA; TWLTQEA; -.
DR   Proteomes; UP000001374; 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_1000118956"
FT   COILED          12..76
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00105"
SQ   SEQUENCE   160 AA;  17946 MW;  47F0E16A5DE9222F CRC64;
     MSEAKKYVMT YEGVKKLEEE LEFLKTVKRK EITEKIKVAL SFGDLSENSE YDEAKNEQAF
     VEGRIIQLEN MLKNASIVDE NEVPKDIVSV GSIVKVKDYE FDEEVEYIIV GSAEADPMNN
     KISNESPVGH GLIGKKVGDI IEVTVPDGVS KYEILEVNRA