ID   GREA_ECOLI              Reviewed;         158 AA.
AC   P0A6W5; P21346; P78111; Q2M931; Q8X9K9;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   24-JAN-2024, entry version 148.
DE   RecName: Full=Transcription elongation factor GreA;
DE   AltName: Full=Transcript cleavage factor GreA;
GN   Name=greA; OrderedLocusNames=b3181, JW3148;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2243801; DOI=10.1093/nar/18.21.6443;
RA   Sparkowski J., Das A.;
RT   "The nucleotide sequence of greA, a suppressor gene that restores growth of
RT   an Escherichia coli RNA polymerase mutant at high temperature.";
RL   Nucleic Acids Res. 18:6443-6443(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RA   Wang R., Kushner S.R.;
RL   Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX   PubMed=7854424; DOI=10.1038/373636a0;
RA   Stebbins C.E., Borukhov S., Orlova M., Polyakov A., Goldfarb A.,
RA   Darst S.A.;
RT   "Crystal structure of the GreA transcript cleavage factor from Escherichia
RT   coli.";
RL   Nature 373:636-640(1995).
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. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA57982.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X54718; CAA38521.1; -; Genomic_DNA.
DR   EMBL; U01376; AAA97506.1; -; Genomic_DNA.
DR   EMBL; U18997; AAA57982.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC76213.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77225.1; -; Genomic_DNA.
DR   PIR; G65108; G65108.
DR   RefSeq; NP_417648.4; NC_000913.3.
DR   RefSeq; WP_001148001.1; NZ_STEB01000012.1.
DR   PDB; 1GRJ; X-ray; 2.20 A; A=1-158.
DR   PDBsum; 1GRJ; -.
DR   AlphaFoldDB; P0A6W5; -.
DR   SMR; P0A6W5; -.
DR   BioGRID; 4262064; 36.
DR   DIP; DIP-35800N; -.
DR   IntAct; P0A6W5; 52.
DR   STRING; 511145.b3181; -.
DR   jPOST; P0A6W5; -.
DR   PaxDb; 511145-b3181; -.
DR   EnsemblBacteria; AAC76213; AAC76213; b3181.
DR   GeneID; 83578150; -.
DR   GeneID; 947696; -.
DR   KEGG; ecj:JW3148; -.
DR   KEGG; eco:b3181; -.
DR   PATRIC; fig|1411691.4.peg.3551; -.
DR   EchoBASE; EB0410; -.
DR   eggNOG; COG0782; Bacteria.
DR   HOGENOM; CLU_101379_2_0_6; -.
DR   InParanoid; P0A6W5; -.
DR   OMA; TWLTQEA; -.
DR   OrthoDB; 9808774at2; -.
DR   PhylomeDB; P0A6W5; -.
DR   BioCyc; EcoCyc:EG10415-MONOMER; -.
DR   EvolutionaryTrace; P0A6W5; -.
DR   PRO; PR:P0A6W5; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0001108; F:bacterial-type RNA polymerase holo enzyme binding; IDA:EcoCyc.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070063; F:RNA polymerase binding; IEA:InterPro.
DR   GO; GO:0006354; P:DNA-templated transcription elongation; IDA:EcoCyc.
DR   GO; GO:0032784; P:regulation of DNA-templated transcription elongation; IDA:EcoCyc.
DR   Gene3D; 3.10.50.30; Transcription elongation factor, GreA/GreB, C-terminal domain; 1.
DR   Gene3D; 1.10.287.180; Transcription elongation factor, GreA/GreB, N-terminal domain; 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   NCBIfam; TIGR01462; greA; 1.
DR   PANTHER; PTHR30437; TRANSCRIPTION ELONGATION FACTOR GREA; 1.
DR   PANTHER; PTHR30437:SF4; TRANSCRIPTION ELONGATION FACTOR GREA; 1.
DR   Pfam; PF01272; GreA_GreB; 1.
DR   Pfam; PF03449; GreA_GreB_N; 1.
DR   PIRSF; PIRSF006092; GreA_GreB; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   SUPFAM; SSF46557; GreA transcript cleavage protein, N-terminal domain; 1.
DR   PROSITE; PS00829; GREAB_1; 1.
DR   PROSITE; PS00830; GREAB_2; 1.
DR   SWISS-2DPAGE; P0A6W5; -.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..158
FT                   /note="Transcription elongation factor GreA"
FT                   /id="PRO_0000176921"
FT   STRAND          4..7
FT                   /evidence="ECO:0007829|PDB:1GRJ"
FT   HELIX           8..23
FT                   /evidence="ECO:0007829|PDB:1GRJ"
FT   HELIX           25..37
FT                   /evidence="ECO:0007829|PDB:1GRJ"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:1GRJ"
FT   HELIX           46..71
FT                   /evidence="ECO:0007829|PDB:1GRJ"
FT   STRAND          72..75
FT                   /evidence="ECO:0007829|PDB:1GRJ"
FT   HELIX           77..79
FT                   /evidence="ECO:0007829|PDB:1GRJ"
FT   STRAND          91..96
FT                   /evidence="ECO:0007829|PDB:1GRJ"
FT   TURN            97..100
FT                   /evidence="ECO:0007829|PDB:1GRJ"
FT   STRAND          101..108
FT                   /evidence="ECO:0007829|PDB:1GRJ"
FT   TURN            110..112
FT                   /evidence="ECO:0007829|PDB:1GRJ"
FT   HELIX           115..117
FT                   /evidence="ECO:0007829|PDB:1GRJ"
FT   STRAND          119..124
FT                   /evidence="ECO:0007829|PDB:1GRJ"
FT   HELIX           125..130
FT                   /evidence="ECO:0007829|PDB:1GRJ"
FT   STRAND          150..156
FT                   /evidence="ECO:0007829|PDB:1GRJ"
SQ   SEQUENCE   158 AA;  17641 MW;  9E7DFAFE838AC340 CRC64;
     MQAIPMTLRG AEKLREELDF LKSVRRPEII AAIAEAREHG DLKENAEYHA AREQQGFCEG
     RIKDIEAKLS NAQVIDVTKM PNNGRVIFGA TVTVLNLDSD EEQTYRIVGD DEADFKQNLI
     SVNSPIARGL IGKEEDDVVV IKTPGGEVEF EVIKVEYL
//