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RPOE_LIMRJ
ID   RPOE_LIMRJ              Reviewed;         185 AA.
AC   B2G5K4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Probable DNA-directed RNA polymerase subunit delta {ECO:0000255|HAMAP-Rule:MF_00357};
DE   AltName: Full=RNAP delta factor {ECO:0000255|HAMAP-Rule:MF_00357};
GN   Name=rpoE {ECO:0000255|HAMAP-Rule:MF_00357}; OrderedLocusNames=LAR_0220;
OS   Limosilactobacillus reuteri (strain JCM 1112) (Lactobacillus reuteri).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=557433;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 1112;
RX   PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA   Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA   Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T.,
RA   Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T.,
RA   Hattori M.;
RT   "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus
RT   fermentum reveal a genomic island for reuterin and cobalamin production.";
RL   DNA Res. 15:151-161(2008).
CC   -!- FUNCTION: Participates in both the initiation and recycling phases of
CC       transcription. In the presence of the delta subunit, RNAP displays an
CC       increased specificity of transcription, a decreased affinity for
CC       nucleic acids, and an increased efficiency of RNA synthesis because of
CC       enhanced recycling. {ECO:0000255|HAMAP-Rule:MF_00357}.
CC   -!- SUBUNIT: RNAP is composed of a core of 2 alpha, a beta and a beta'
CC       subunits. The core is associated with a delta subunit and one of
CC       several sigma factors. {ECO:0000255|HAMAP-Rule:MF_00357}.
CC   -!- SIMILARITY: Belongs to the RpoE family. {ECO:0000255|HAMAP-
CC       Rule:MF_00357}.
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DR   EMBL; AP007281; BAG24736.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2G5K4; -.
DR   SMR; B2G5K4; -.
DR   KEGG; lrf:LAR_0220; -.
DR   HOGENOM; CLU_116648_0_0_9; -.
DR   OMA; TWGLRSW; -.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.10.1250; -; 1.
DR   HAMAP; MF_00357; RNApol_bact_RpoE; 1.
DR   InterPro; IPR007759; Asxl_HARE-HTH.
DR   InterPro; IPR038087; RNAP_delta_N_dom_sf.
DR   InterPro; IPR029757; RpoE.
DR   Pfam; PF05066; HARE-HTH; 1.
DR   TIGRFAMs; TIGR04567; RNAP_delt_lowGC; 1.
DR   PROSITE; PS51913; HTH_HARE; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Nucleotidyltransferase; Transcription;
KW   Transferase.
FT   CHAIN           1..185
FT                   /note="Probable DNA-directed RNA polymerase subunit delta"
FT                   /id="PRO_1000120565"
FT   DOMAIN          14..81
FT                   /note="HTH HARE-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01261"
FT   REGION          90..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..185
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   185 AA;  21208 MW;  20BE7D279D270629 CRC64;
     MDLKVFDGQD KSELSMIEVA HAILAHHGKA MAFVDLTNEV QQYLGKSDEE IRERLAQFYT
     DLNVDGSFIS LGDNTWGLRA WYPFESIDEA TVGENEEDEE DDRPKKKRRK VNAFLADTDD
     DDDVIDYDND DPEDEDLDTD DDADSEDDYD DDTDDFSDDD DDLDDGIEGQ LSELHDEEDE
     DEDDE
 
 
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