RPOB_THISH
ID RPOB_THISH Reviewed; 1358 AA.
AC B8GV65;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=Tgr7_2331;
OS Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=396588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-EbGR7;
RX PubMed=21475584; DOI=10.4056/sigs.1483693;
RA Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL Stand. Genomic Sci. 4:23-35(2011).
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; CP001339; ACL73411.1; -; Genomic_DNA.
DR RefSeq; WP_012638887.1; NC_011901.1.
DR AlphaFoldDB; B8GV65; -.
DR SMR; B8GV65; -.
DR STRING; 396588.Tgr7_2331; -.
DR PRIDE; B8GV65; -.
DR EnsemblBacteria; ACL73411; ACL73411; Tgr7_2331.
DR KEGG; tgr:Tgr7_2331; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_6; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000002383; 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; -; 2.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 2.
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..1358
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000165832"
SQ SEQUENCE 1358 AA; 151564 MW; 2E0623629A24C8C5 CRC64;
MAYSYTEKKR IRKDFGKRPQ ILDVPYLLTT QLDSYRQFLQ ADRSEDNRQD VGLHAAFKTV
FPIVSYSGTV ELEYVSYRLG KPVFDVKECQ LRGMTYAAPL RVLLRLVIYD KDAPAGSRVV
KDIKEQEVYM GELPLMTENG TFVINGTERV IVSQLHRSPG VFFDHDKGKT HSSGKLLFNA
RVIPYRGSWL DFEFDPKDSV FVRIDRRRKL PATVLLRALG METEEILATF FETNTVSITK
DGFDMELIPE RLRGEVAAFD FKVKNKVLVE SGRRITARHV RELEAAGIKS LEVPAEYLVG
KVLAHAVIDE DSGELVANAN DEITDELLKK LRAAGIKSFK TLYTNDLDHG PYISTTLNID
TCRSQLEAQV EIYRMMRPGE PPTKEAAENL FNNLFFTEER YDLSAVGRMK FNRRVGREEI
TGPGVLDKDD ILAVLKTLID IRNGNGQVDD IDHLGNRRVR SVGEMAENVF RVGLVRVERA
VKERLSVAES EGLMPQELIN AKPVAAAVKE FFGSSQLSQF MDQNNPLSEV THKRRISALG
PGGLTRERAG FEVRDVHPTH YGRVCPIETP EGPNIGLINS LAVYARTNDY GFLETPYRKV
ENGKVTNEIV YLSAIEEGQY VIAQANASLD AKGNLVDELV SCRHANEFTM STPDKIEFMD
ISPKQIVSVA AALIPFLEHD DANRALMGSN MQRQAVPCLR AETAVVGTGI ERTVAIDSGS
SIVARRGGVV DSVDAARIVV RVNDDETEAG EPGVDIYNLT KYTRSNQNTC INQRPLVNVG
DVLARGDVLA DGSSTDLGEM ALGQNMMVAF MPWNGYNFED SILISERVVQ EDRFTSIHIE
ELTCVARDTK LGPEEISADI PNVSESLLSK LDESGIVYVG AEVKPNDILV GKVTPKGETQ
LTPEEKLLRA IFGEKASDVK DTSLRVPSGM EGTVIDVRVF TRDGVDKDKR ALQIEEAALA
AVRKDLKDQL RIYEDDIYDR VEKLLVGKLA AGGPNKLKDG TKVTKTYLTE VPREKWFEVR
MRTEEVNEQL EKMAASLKEQ HEAFETRFKE QKEKLTQGDD LAPGVLKMVK VYLAVKRRMQ
PGDKMAGRHG NKGVVSMIVP VEDMPYLEDG TPVDIVLNPL GVPSRMNVGQ VLETHLGWAA
KGLGQKIGRM VEAKAKIDEL RKFLDKIYNH SAKKVDLSDF SDEEILKLCA NLKKGVPMAT
PVFDGAEEEE IKAMLKLADL PESGQTTLFD GRTGESFDRP VTVGYMHMLK LNHLVDDKMH
ARSTGPYSLV TQQPLGGKAQ FGGQRFGEME VWALEAYGAA YTLQEMLTVK SDDVQGRNKM
YKNIVDGDHR MEANIPESFN VLMKEIRSLA INIELEQD
