GREA_STAA1
ID GREA_STAA1 Reviewed; 158 AA.
AC A7X319;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=SAHV_1597;
OS Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=418127;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu3 / ATCC 700698;
RX PubMed=17954695; DOI=10.1128/aac.00534-07;
RA Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT "Mutated response regulator graR is responsible for phenotypic conversion
RT of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT resistance to vancomycin-intermediate resistance.";
RL Antimicrob. Agents Chemother. 52:45-53(2008).
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; AP009324; BAF78480.1; -; Genomic_DNA.
DR RefSeq; WP_000431312.1; NZ_CTYB01000003.1.
DR AlphaFoldDB; A7X319; -.
DR SMR; A7X319; -.
DR KEGG; saw:SAHV_1597; -.
DR HOGENOM; CLU_101379_2_1_9; -.
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..158
FT /note="Transcription elongation factor GreA"
FT /id="PRO_1000034297"
FT COILED 4..70
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00105"
SQ SEQUENCE 158 AA; 17743 MW; EC3B0F0E6238A107 CRC64;
MENQKQYPMT QEGFEKLERE LEELKTVKRP EVVEKIKVAR SFGDLSENSE YDAAKDEQGF
IEQDIQRIEH MLRNALIIED TGDNNVVKIG KTVTFVELPG DEEESYQIVG SAESDAFNGK
ISNESPMAKA LIGKGLDDEV RVPLPNGGEM NVKIVNIQ