ID F8GK16_NITSI Unreviewed; 182 AA.
AC F8GK16;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Transcription elongation factor GreB {ECO:0000256|HAMAP-Rule:MF_00930};
DE AltName: Full=Transcript cleavage factor GreB {ECO:0000256|HAMAP-Rule:MF_00930};
GN Name=greB {ECO:0000256|HAMAP-Rule:MF_00930};
GN OrderedLocusNames=Nit79A3_3088 {ECO:0000313|EMBL:AEJ02826.1};
OS Nitrosomonas sp. (strain Is79A3).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=261292 {ECO:0000313|EMBL:AEJ02826.1};
RN [1] {ECO:0000313|EMBL:AEJ02826.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Is79A3 {ECO:0000313|EMBL:AEJ02826.1};
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., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Bollmann A., Norton J.,
RA Suwa Y., Klotz M., Stein L., Laanbroek H., Arp D., Woyke T.;
RT "Complete sequence of Nitrosomonas sp. Is79A3.";
RL Submitted (JUN-2011) 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. GreB releases sequences of up to 9 nucleotides in length.
CC {ECO:0000256|HAMAP-Rule:MF_00930}.
CC -!- SIMILARITY: Belongs to the GreA/GreB family. GreB subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00930}.
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DR EMBL; CP002876; AEJ02826.1; -; Genomic_DNA.
DR AlphaFoldDB; F8GK16; -.
DR STRING; 261292.Nit79A3_3088; -.
DR KEGG; nii:Nit79A3_3088; -.
DR eggNOG; COG0782; Bacteria.
DR HOGENOM; CLU_101379_3_0_4; -.
DR OrthoDB; 5511940at2; -.
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 HAMAP; MF_00930; GreB; 1.
DR InterPro; IPR036953; GreA/GreB_C_sf.
DR InterPro; IPR018151; TF_GreA/GreB_CS.
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 InterPro; IPR006358; Tscrpt_elong_fac_GreB.
DR NCBIfam; TIGR01461; greB; 1.
DR PANTHER; PTHR30437; TRANSCRIPTION ELONGATION FACTOR GREA; 1.
DR PANTHER; PTHR30437:SF6; TRANSCRIPTION ELONGATION FACTOR GREB; 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; PS00830; GREAB_2; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00930}; Elongation factor {ECO:0000313|EMBL:AEJ02826.1};
KW Protein biosynthesis {ECO:0000313|EMBL:AEJ02826.1};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00930};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW Rule:MF_00930}.
FT DOMAIN 27..97
FT /note="Transcription elongation factor GreA/GreB N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF03449"
FT DOMAIN 106..179
FT /note="Transcription elongation factor GreA/GreB C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01272"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 182 AA; 20567 MW; 8014BD1378339D79 CRC64;
MSKAFTKESE DDDELDGTPK LPQGLKNYIT PAGHQRLKEE FDQLWKVERP ELVKTITWAA
SNGDRSENGD YIYGKRRLRE IDRRLRFLSK RLENAEVVDP AQRGECDQVF FGATVTVCNA
QGEEHTYSIV GLDEVDPGHG RISWISPLAK ALLKAREGDT VKLHTPAGVE DLEVVEIRYV
AL
//
