(data stored in ACNUC7421 zone)

SWISSPROT: RPOB_EDWI9

ID   RPOB_EDWI9              Reviewed;        1342 AA.
AC   C5BHE3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 57.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE            Short=RNAP subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321};
DE   AltName: Full=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE   AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
GN   Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321};
GN   OrderedLocusNames=NT01EI_0174;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC       of DNA into RNA using the four ribonucleoside triphosphates as
CC       substrates. {ECO:0000255|HAMAP-Rule:MF_01321}.
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1). {ECO:0000255|HAMAP-Rule:MF_01321}.
CC   -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1
CC       beta' and 1 omega subunit. When a sigma factor is associated with
CC       the core the holoenzyme is formed, which can initiate
CC       transcription. {ECO:0000255|HAMAP-Rule:MF_01321}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01321}.
DR   EMBL; CP001600; ACR67421.1; -; Genomic_DNA.
DR   RefSeq; WP_015869633.1; NC_012779.2.
DR   SMR; C5BHE3; -.
DR   STRING; 634503.NT01EI_0174; -.
DR   PRIDE; C5BHE3; -.
DR   EnsemblBacteria; ACR67421; ACR67421; NT01EI_0174.
DR   GeneID; 7958766; -.
DR   KEGG; eic:NT01EI_0174; -.
DR   PATRIC; fig|634503.3.peg.157; -.
DR   eggNOG; ENOG4107QIH; Bacteria.
DR   eggNOG; COG0085; LUCA.
DR   HOGENOM; HOG000218612; -.
DR   KO; K03043; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; POG091H01MI; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00653; RNA_pol_B_RPB2; 1.
DR   Gene3D; 2.40.270.10; -; 1.
DR   Gene3D; 2.40.50.150; -; 1.
DR   HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR   InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
DR   InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR   InterPro; IPR007120; DNA-dir_RNA_pol_su2_6.
DR   InterPro; IPR010243; RNA_pol_bsu_bac.
DR   InterPro; IPR007121; RNA_pol_bsu_CS.
DR   InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR   InterPro; IPR007642; RNA_pol_Rpb2_2.
DR   InterPro; IPR007645; RNA_pol_Rpb2_3.
DR   InterPro; IPR007641; RNA_pol_Rpb2_7.
DR   InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR   PANTHER; PTHR20856; PTHR20856; 1.
DR   Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR   Pfam; PF04561; RNA_pol_Rpb2_2; 2.
DR   Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR   Pfam; PF10385; RNA_pol_Rpb2_45; 1.
DR   Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR   Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR   TIGRFAMs; TIGR02013; rpoB; 1.
DR   PROSITE; PS01166; RNA_POL_BETA; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BHE3.
DR   SWISS-2DPAGE; C5BHE3.
KW   Complete proteome; DNA-directed RNA polymerase;
KW   Nucleotidyltransferase; Reference proteome; Transcription;
KW   Transferase.
FT   CHAIN         1   1342       DNA-directed RNA polymerase subunit beta.
FT                                /FTId=PRO_1000214477.
SQ   SEQUENCE   1342 AA;  150610 MW;  73F5D65D84491F35 CRC64;
     MVYSYTEKKR IRKDFGKRPQ VLDVPYLLSI QLDSFQKFIE QDPEGQYGLE AAFRSVFPIQ
     SYSGNSELQY VSYRLGEPVF DVKECQIRGV TYSAPLRVKL RLVIYEREAP EGTVKDIKEQ
     EVYMGEIPLM TENGTFVING TERVIVSQLH RSPGVFFDSD KGKTHSSGKV LYNARIIPYR
     GSWLDFEFDP KDNLFVRIDR RRKLPATIIL RALDFTTEQI LDLFFDKVIF EIRDNKLQME
     LVPERLRGET ASFDIEANGK VYVEKGRRIT ARHIRQLEKD DVTLIEVPVE YIVGKVAAKD
     YIDESTGELI CAANMELSLD LLAKLSQSGY KRIDTLFTND LDHGPYMSET LRVDPTNDRL
     SALVEIYRMM RPGEPPTREA AENLFENLFF SEDRYDLSAV GRMKFNRSLM RDEIEGSGIL
     SKNDIIEVMK KLIDIRNGKG EVDDIDHLGN RRIRSVGEMA ENQFRVGLVR VERAVKERLS
     LGDLDMLMPQ DMINAKPISA AVKEFFGSSQ LSQFMDQNNP LSEITHKRRI SALGPGGLTR
     ERAGFEVRDV HPTHYGRVCP IETPEGPNIG LINSLSVYAQ TNEYGFLETP YRRVRDGIVT
     DEIHYLSAIE EGNFVIAQAN SNLDDEGRFV EDLVTCRSKG ESSLFSRDQV DYMDVSTQQV
     VSVGASLIPF LEHDDANRAL MGANMQRQAV PTLRADKPLV GTGMERAVAV DSGVTSVAKR
     GGMVQYVDAS RIVIKVNEDE MFPGEAGIDI YNLTKYTRSN QNTCISQMPC VSLGEPIERG
     DVLADGPSTD LGELALGQNM RVAFMPWNGY NFEDSILVSE RVVQEDRFTS IHIQELACVS
     RDTKLGPEEI TADIPNVGEA ALSKLDESGI VYIGAEVKGG DILVGKVTPK GETQLTPEEK
     LLRAIFGEKA SDVKDSSLRV PNSVSGTVID VQVFTRDGVE KDKRALEIEE MQLKQAKKDL
     TEELQILEAG LFARIHDVLV AGGVEAEKLE KLPRDRWLEL GLADEAKQNQ LEQLAEQYDE
     LKAEFEKKLE AKRRKITQGD DLAPGVLKIV KVYLAVKRQI QPGDKMAGRH GNKGVISKIN
     PIEDMPYDEN GTPVDIVLNP LGVPSRMNIG QILETHLGMA AKGIGDKINA MLKQQQEVAK
     LREFIQRAYD LGDNTRQQVD LNTFSDDEVL RLAENLKKGL PVATPVFDGA KEREIKGLLE
     LGGIPTSGQI TLYDGRTGER FERQVTVGYM YMLKLNHLVD DKMHARSTGS YSLVTQQPLG
     GKAQFGGQRF GEMEVWALEA YGAAYTLQEM LTVKSDDVNG RTKMYKNIVD GSHQMEPGMP
     ESFNVLLKEI RSLGINIELE DE
//

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