(data stored in SCRATCH zone)

SWISSPROT: C8W3U9_DESAS

ID   C8W3U9_DESAS            Unreviewed;       158 AA.
AC   C8W3U9;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   16-JAN-2019, entry version 68.
DE   RecName: Full=Transcription elongation factor GreA {ECO:0000256|HAMAP-Rule:MF_00105, ECO:0000256|RuleBase:RU000556, ECO:0000256|SAAS:SAAS01033802};
DE   AltName: Full=Transcript cleavage factor GreA {ECO:0000256|HAMAP-Rule:MF_00105};
GN   Name=greA {ECO:0000256|HAMAP-Rule:MF_00105};
GN   OrderedLocusNames=Dtox_0250 {ECO:0000313|EMBL:ACV61203.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61203.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61203.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: Necessary for efficient RNA polymerase transcription
CC       elongation past template-encoded arresting sites. The arresting
CC       sites in DNA have the property of trapping a certain fraction of
CC       elongating RNA polymerases that pass through, resulting in locked
CC       ternary complexes. Cleavage of the nascent transcript by cleavage
CC       factors such as GreA or GreB allows the resumption of elongation
CC       from the new 3'terminus. GreA releases sequences of 2 to 3
CC       nucleotides. {ECO:0000256|HAMAP-Rule:MF_00105,
CC       ECO:0000256|RuleBase:RU000556, ECO:0000256|SAAS:SAAS01033799}.
CC   -!- SIMILARITY: Belongs to the GreA/GreB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00105, ECO:0000256|RuleBase:RU000556,
CC       ECO:0000256|SAAS:SAAS01033218}.
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DR   EMBL; CP001720; ACV61203.1; -; Genomic_DNA.
DR   RefSeq; WP_015755924.1; NC_013216.1.
DR   STRING; 485916.Dtox_0250; -.
DR   EnsemblBacteria; ACV61203; ACV61203; Dtox_0250.
DR   KEGG; dae:Dtox_0250; -.
DR   eggNOG; ENOG4108UKH; Bacteria.
DR   eggNOG; COG0782; LUCA.
DR   HOGENOM; HOG000241145; -.
DR   KO; K03624; -.
DR   OMA; TWLTQEA; -.
DR   OrthoDB; 1536415at2; -.
DR   BioCyc; DACE485916:G1GFV-254-MONOMER; -.
DR   Proteomes; UP000002217; 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; 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.
PE   3: Inferred from homology;
DR   PRODOM; C8W3U9.
DR   SWISS-2DPAGE; C8W3U9.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00105,
KW   ECO:0000256|RuleBase:RU000556, ECO:0000256|SAAS:SAAS01033224};
KW   Elongation factor {ECO:0000313|EMBL:ACV61203.1};
KW   Protein biosynthesis {ECO:0000313|EMBL:ACV61203.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00105,
KW   ECO:0000256|RuleBase:RU000556, ECO:0000256|SAAS:SAAS01033216};
KW   Transcription regulation {ECO:0000256|HAMAP-Rule:MF_00105,
KW   ECO:0000256|RuleBase:RU000556, ECO:0000256|SAAS:SAAS01033223}.
FT   DOMAIN        6     76       GreA_GreB_N. {ECO:0000259|Pfam:PF03449}.
FT   DOMAIN       86    156       GreA_GreB. {ECO:0000259|Pfam:PF01272}.
FT   COILED       13     33       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   158 AA;  17513 MW;  CD3C999B5934E9D0 CRC64;
     MKEKEVILTV AGLKNLEEEL EQLKSVRRRE IAARIKQAIE FGDISENSEY EDAKNEQAFI
     EGRILTLEKM LRNAKIIDDE NIDIEAVHIG SKVLLKDLEF GDEFEYTIVG SVEADPGASK
     ISNESPVGKA ILGKPKGSVV EVNVPAGILK YEIMDIIA
//

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