ID G2NLZ8_STREK Unreviewed; 165 AA.
AC G2NLZ8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Transcription elongation factor GreA {ECO:0000256|ARBA:ARBA00013729, ECO:0000256|HAMAP-Rule:MF_00105};
DE AltName: Full=Transcript cleavage factor GreA {ECO:0000256|HAMAP-Rule:MF_00105};
GN Name=greA {ECO:0000256|HAMAP-Rule:MF_00105};
GN ORFNames=SACTE_4210 {ECO:0000313|EMBL:AEN12050.1};
OS Streptomyces sp. (strain SirexAA-E / ActE).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN12050.1, ECO:0000313|Proteomes:UP000001397};
RN [1] {ECO:0000313|EMBL:AEN12050.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA Adams S., Book A., Currie C., Woyke T.;
RT "Complete sequence of Streptomyces sp. SirexAA-E.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEN12050.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RX PubMed=24710170; DOI=10.1371/journal.pone.0094166;
RA Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F.,
RA Book A.J., Currie C.R., Fox B.G.;
RT "Biochemical properties and atomic resolution structure of a
RT proteolytically processed beta-mannanase from cellulolytic Streptomyces sp.
RT SirexAA-E.";
RL PLoS ONE 9:e94166-E94166(2014).
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:0000256|ARBA:ARBA00024916, ECO:0000256|HAMAP-Rule:MF_00105,
CC ECO:0000256|RuleBase:RU000556}.
CC -!- SIMILARITY: Belongs to the GreA/GreB family.
CC {ECO:0000256|ARBA:ARBA00008213, ECO:0000256|HAMAP-Rule:MF_00105,
CC ECO:0000256|RuleBase:RU000556}.
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DR EMBL; CP002993; AEN12050.1; -; Genomic_DNA.
DR RefSeq; WP_014048009.1; NC_015953.1.
DR AlphaFoldDB; G2NLZ8; -.
DR STRING; 862751.SACTE_4210; -.
DR KEGG; ssx:SACTE_4210; -.
DR PATRIC; fig|862751.12.peg.4376; -.
DR eggNOG; COG0782; Bacteria.
DR HOGENOM; CLU_101379_0_0_11; -.
DR OrthoDB; 9797227at2; -.
DR Proteomes; UP000001397; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070063; F:RNA polymerase binding; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0032784; P:regulation of DNA-templated transcription elongation; IEA:UniProtKB-UniRule.
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.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00105}; Elongation factor {ECO:0000313|EMBL:AEN12050.1};
KW Protein biosynthesis {ECO:0000313|EMBL:AEN12050.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001397};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00105};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW Rule:MF_00105}.
FT DOMAIN 10..79
FT /note="Transcription elongation factor GreA/GreB N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF03449"
FT DOMAIN 85..160
FT /note="Transcription elongation factor GreA/GreB C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01272"
SQ SEQUENCE 165 AA; 17989 MW; 0687572FBBB524A3 CRC64;
MTQTSDNVTW LTQEAYNQLK AELEYLSGPA RTEISVKIAA AREEGDLREN GGYHAAKEEQ
GKMELRVRQL TQLLEHAKVG EPPADDGVVE PGMVVTIAFD GDPDDTLTFL LASREYATGD
IETYSPQSPL GTGVNGKRMG EEAEYELPNG KKATVKILTA KPYTG
//
