ID   RPOB_SHEVI              Reviewed;        1343 AA.
AC   Q9KW14;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 81.
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};
OS   Shewanella violacea.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Nakasone K., Ikegami A., Sakai Y., Kato C., Horikoshi K.;
RT   "Isolation of rpoB and rpoC genes from deep-sea piezophilic bacterium
RT   Shewanella violacea and its overexpression in Escherichia coli.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000255|HAMAP-Rule:MF_01321}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_01321};
CC   -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC       and 1 omega subunit. When a sigma factor is associated with the core
CC       the holoenzyme is formed, which can initiate transcription.
CC       {ECO:0000255|HAMAP-Rule:MF_01321}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR   EMBL; AB045725; BAA99392.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9KW14; -.
DR   SMR; Q9KW14; -.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   CDD; cd00653; RNA_pol_B_RPB2; 1.
DR   Gene3D; 2.30.150.10; -; 1.
DR   Gene3D; 2.40.270.10; -; 1.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 1.
DR   HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR   InterPro; IPR042107; DNA-dir_RNA_pol_bsu_ext_1_sf.
DR   InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
DR   InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR   InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR   InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
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; IPR037034; RNA_pol_Rpb2_2_sf.
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;
KW   DNA-directed RNA polymerase; Nucleotidyltransferase; Transcription;
KW   Transferase.
FT   CHAIN           1..1343
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047955"
SQ   SEQUENCE   1343 AA;  150104 MW;  AEA8A6022B5349DA CRC64;
     MVYSYSEKKR IRKDFGKRPK VLDIPYLLSI QLDSFKKFTD QDPTGERGFE AAFRSVFPIK
     SFSGNSELQY VSYKLGEPVF DVKECQIRGI TYAAPLRVKL RMVLYDREAA PGTVKDIKEQ
     EVYMGDIPLM TNNGTFVING TERVIVSQLH RSPGVFFDHD RGKTHSSGKV LYNARIIPYR
     GSWLDFEFDP KDALFVRIDR RRKLPASIML RALDYSTQDI LDLFFDRVNF KIKKDSLVMD
     LVPERLRGET ASYDIKDSDG SILVEKGRRV TARHIRQLEK SKTTELEVPV DYIEGKIAGQ
     DYIDPDTGEV LVSANAEITL EDLAKLSMAG IKEISTLYIN DLDNGAYMSD TLRIDSTTNR
     LEALVEIYRM MRPGEPPTKD AAEGLFQNLF FSEERYDLSK VGRMKFNRRL SIGEDEGSGI
     LSKEDIVAVM KNIITIRNGG DEVDDIDHLG NRRIRSVGEM AENQFRVGLV RVERAVRERL
     SLGDLNELMP QDLINAKPIS AAVKEFFGSS QLSQFMDQNN PLSEVTHKRR ISALGPGGLT
     RERAGFEVRD VHPTHYGRLC PIETPEGPNI GLINSLASFA RTNSYGFLET PYRKVEDGVV
     TDQIDYLSAI EEGRYVIAQA NIDIDKNGRL LEEQVACRHK GDSTFMRGTD IQYMDVSPQQ
     IISVAASLIP FLEHDDANRA LMGANMQRQA VPTLRADKPL VGTGIERIIA VDSGVVVVAK
     RGGSIDYVDA SRIVVKVNES ELRPGEAGID IYNLTKYTRS NQNTCINQRP CCSVGDPVVV
     GDVLADGPST DLGDLAFGQN MRIAFMPWNG YNFEDSILIS ERVAQEDRFT TIHIQELSCI
     ARDTKLGSEE ITADIPNVGE SALSKLDESG IVYIGAEVKG GDILVGKVTP KGETQLTPEE
     KLLRAIFGEK ASDVKDSSLR VPNSVKGTII DVQVFTRDGV EKDKRAVEIE EMHIAQAKKD
     LTEEFKILEE GVYGRARNLL LNAGFEQAQL DAIPRSHLLV QTIDDEAKQT ELEQLAEQHD
     ELKADFDKKF EIKRRKITQG DDLAPGVLKI VKVYLAVKRT IQPGDKMAGR HGNKGVISKI
     NPVEDMPYDE NGNPIDIVLN PLGVPSRMNI GQILEVHMGA AAKGIGDQIT AMLEEQRQLA
     EIRGYIKEVY ELGDEVLQRV DIDSFTDDEV LRLAKNLKGG IPIATPAFDG AKEKEIKEML
     ALAKLPTSGQ RTLYDGRTGN EFERKVTVGY MYMLKLNHLV DDKMHARSTG SYSLVTQQPL
     GGKAQFGGQR FGEMEVWALE AYGAAYTLQE MLTVKSDDVN GRTQMYKNIV DGNYQMQPGM
     PESFNVLLKE IRSLGINIEL DQD