ID   RPOB_SORC5              Reviewed;        1378 AA.
AC   A9GRB1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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}; OrderedLocusNames=sce0410;
OS   Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS   ce56)).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; Sorangiineae;
OC   Polyangiaceae; Sorangium.
OX   NCBI_TaxID=448385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=So ce56;
RX   PubMed=17965706; DOI=10.1038/nbt1354;
RA   Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA   Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA   Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA   Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA   Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA   Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA   Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA   Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA   Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA   Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA   Puehler A., Mueller R.;
RT   "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL   Nat. Biotechnol. 25:1281-1289(2007).
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; AM746676; CAN90567.1; -; Genomic_DNA.
DR   RefSeq; WP_012233045.1; NC_010162.1.
DR   AlphaFoldDB; A9GRB1; -.
DR   SMR; A9GRB1; -.
DR   STRING; 448385.sce0410; -.
DR   PRIDE; A9GRB1; -.
DR   EnsemblBacteria; CAN90567; CAN90567; sce0410.
DR   KEGG; scl:sce0410; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_0_7; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   BioCyc; SCEL448385:SCE_RS02160-MON; -.
DR   Proteomes; UP000002139; Chromosome.
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; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..1378
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_1000086383"
SQ   SEQUENCE   1378 AA;  155046 MW;  ACD6B806924BAD95 CRC64;
     MPSVVQSNFR VRKNLGRVRR IIDVPNLIDI QKSSYDKFLQ MSVPPNEREE VGLQAVFRSV
     FPIKDFNGTS ELVFVSYNLE PPKYDVDECR QRGMTYSAPI KVTNQLMIYD TRDGGERIVR
     DIKEQEVYFG ELPLMTETGT FIINGTERVV VSQLHRSPGV FFDHDKGKTH SSGKLLYSAR
     VIPYRGSWLD FEFDPKDIIY VRIDRRRKMH ATVLLRALGY STQDLLNYFY STETVYLEKG
     GKYAKSIEYD LLAGQRTTRD IKIGNDVIVK KNTKFTRAAI RKMKEAKLER LSLEPEELVG
     KVAAHDIVDP ETGEVVVEVN EELTEAKLER LRDANIEQFR ILFIDGLNVG SYLRDTLLTD
     KVKTMEDSIL EIYRRLRPGD PPTLETAKTL FHNLFFNAER YDLSKVGRLK LNYKFYRDVP
     EDERPGLDLT VLTPQDILET VRHLIELKNG RGSVDDIDHL GNRRVRAVGE LMENQYRIGL
     VRMERAIKER MSMSQEIDTL MPHDLINAKP VSAVVKEYFG SSQLSQFMDQ TNPLSEVTHK
     RRLSALGPGG LTRERAGFEV RDVHATHYGR ICPIETPEGP NIGLIASLST FARVNEFGFV
     ETPYRKVENG RVTEDVIWLS ALEEEGKYIA QATVNLDEGG RFKESLVSAR YNGEFKIVTP
     EMVELMDVAP NQMVSVAAAL VPFLEHDDAN RALMGANMQR QAVPLVQSHA PLVGTGMEER
     LARDSGVCVI ARRPGVVESV DATRIVVRAE GEGAEVPDIY HLMKFQRSNQ STCYTQKPVV
     RTGEVVKKGD VLADGPSTDM GELALGQNVL VAFMPWQGYN FEDSILVSER IAKDDVFTSI
     HIEEFECVAR DTKLGKEEIT RDIPNVGEEA LKDLDDSGIV RIGAEVRPGD ILVGKITPKG
     ETQLSPEEKL LRAIFGEKAG DVRDSSLKVP PGVGGIVINA RVFSRKGTEK DDRARDIEDQ
     ERARIERTRD EEIKILRDSF FRRIRELLLG KEATGKLVDD KGKVLFQKGA IIDEPSLAEI
     PRKYWGEIPV DDAERVQQIL RDLEELVRTR EEHFRDKIDR LSKGDELPPG VIKMVKVYIA
     IKRKLQVGDK MAGRHGNKGV ISRILPEEDM PYLQDGRPVD LVLNPLGVPS RMNVGQILEI
     HLGWGAFELG NQLQRMIEQQ RASAEIKEHL KAIYAGDETM NGFFDNLDDG DVKRFVKTVD
     EGVFMGSPVF DGAHESDIKG ALDLAGLPTS GQAILFDGRT GDAFDQNVTV GIMYMLKLHH
     LVDDKIHARS IGPYSLVTQQ PLGGKAQFGG QRLGEMEVWA MEAYGAAYAL QEFLTVKSDD
     VMGRTRMYEA IVKGDYTLEA GLPESFNVLI KELQSLCLNV ELVETSAGVE ASAAEEEE