ID   GREA_CAMJR              Reviewed;         161 AA.
AC   Q5HWI0;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=CJE0335;
OS   Campylobacter jejuni (strain RM1221).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=195099;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM1221;
RX   PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
RA   Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
RA   Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
RA   Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
RA   Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
RA   Nelson K.E.;
RT   "Major structural differences and novel potential virulence mechanisms from
RT   the genomes of multiple Campylobacter species.";
RL   PLoS Biol. 3:72-85(2005).
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; CP000025; AAW34925.1; -; Genomic_DNA.
DR   RefSeq; WP_002858660.1; NC_003912.7.
DR   AlphaFoldDB; Q5HWI0; -.
DR   SMR; Q5HWI0; -.
DR   KEGG; cjr:CJE0335; -.
DR   HOGENOM; CLU_101379_2_0_7; -.
DR   OMA; TWLTQEA; -.
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..161
FT                   /note="Transcription elongation factor GreA"
FT                   /id="PRO_0000176916"
FT   COILED          45..73
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00105"
SQ   SEQUENCE   161 AA;  18010 MW;  132C7DEC962A3239 CRC64;
     MQKEPMSQFG YDKLAAELKD LKDNQRPAVV IEIDTARSHG DLKENAEYHA AREKQALIES
     RIAELSDLLA RAQVIDPSSY EHDSVKFGSS VVIMDLDTEK ESKYTLVGIC EGNLDKGYIS
     IASPIAKAML GKKEGDDFKV RLPKGESEFE ILSINYEPLK F