RPOB_RHOCS
ID RPOB_RHOCS Reviewed; 1397 AA.
AC B6IRP6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, 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=RC1_0701;
OS Rhodospirillum centenum (strain ATCC 51521 / SW).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=414684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51521 / SW;
RA Touchman J.W., Bauer C., Blankenship R.E.;
RT "Genome sequence of Rhodospirillum centenum.";
RL Submitted (MAR-2007) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000613; ACI98132.1; -; Genomic_DNA.
DR RefSeq; WP_012565924.1; NC_011420.2.
DR AlphaFoldDB; B6IRP6; -.
DR SMR; B6IRP6; -.
DR STRING; 414684.RC1_0701; -.
DR PRIDE; B6IRP6; -.
DR EnsemblBacteria; ACI98132; ACI98132; RC1_0701.
DR KEGG; rce:RC1_0701; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_5; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000001591; 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; 1.
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..1397
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000141727"
SQ SEQUENCE 1397 AA; 156348 MW; A63AC009397A4A77 CRC64;
MAKSFTGRKR IRKSFGRIPE VTRMPNLIEV QRSSYDHFLQ MDVPPEKRAN VGLQEVFRSV
FPIKDFSERA VLDFVRYELE QPKYDVEECQ QRGMTFAAPL KVTLRLTVFD VDEDTGLRSI
RDIKEQDVYM GDMPLMTANG TFIINGTERV IVSQMHRSPG VFFDHDKGKT HSSGKYLFAA
RVIPYRGSWL DFEFDAKDIV YVRIDRRRKL PATTLLYALD GADSAELRAE RRALGKDLLP
YEAQGMAKEE ILGYFYETIT YQRAADGWKT GFDAERMKGQ KLLTDLVDAR TGEVLASRDT
KLTPRLIRKL QDQGLQEIKV AIEDIIGRYL AIDIIDEKTG EVIYEAGDEL SATALERLEK
MGVEELPVLN VDHLNIGAYI RNTMAADRNA SREDALIDIY RVMRPGEPPT LESAEALFAG
LFFDQERYDL SAVGRVKMNA RLGFETDDQM RVLRKEDILK ILKILVELKD GRGEIDDIDH
LGNRRVRSVG ELMENQYRVG LLRMERAIRE RMSSVEIDTV MPHDLINAKP AAAAVREFFG
SSQLSQFMDQ TNPLSEITHK RRLSALGPGG LTRERAGFEV RDVHPTHYGR ICPIETPEGP
NIGLINSLAT YARVNQYGFI ESPYRKVIDG RVTDEVVYLS AMEEGRYTVA EANAPLDAGN
RFADPLVSCR KGGEYLLVRP DMIDLIDVSP KQLVSVAAAL IPFLENDDAN RALMGSNMQR
QAVPLIKADS PLVGTGMEAT VARDSGVTIV TRRAGIVDQV DATRIVIRAT EDTDPAAPGV
DIYNLLKFQR SNQNTCINQK PLVKVGDRVQ KGDIIADGPS TDLGELALGR NVLVAFMPWN
GYNFEDSILI SERIVRDDVF TSIHIEEFEV MARDTKLGQE EITRDIPNVG EEALKNLDEA
GIVYIGAEVR PGDILVGKVT PKGESPMTPE EKLLRAIFGE KASDVRDTSL RLPPGVAGTV
VEVRVFSRRG VDKDERALAI ERAEIEKLAK DRDDEKAILE RSFYTRLKEL LLGQTSVSGP
KGMKGGETIT DETLAGLTRG QWRHISVEND QVMEIIEQTG KVFDDSVQRL QERFENKVEK
LQRGDELPPG VMKMVKVFVA VKRKLQPGDK MAGRHGNKGV ISRITPIEDM PYLEDGRNVD
IVLNPLGVPS RMNVGQILET HLGWAAAGIG RQIGEMLDRM RAATVEAADK ARTAEDLKER
LRSIYGEAVY ESDIAPMSEA QLMELAGNLR RGIPFATPVF DGAREDDICR MLEAAGLDRS
GQSTLIDGRT GEPFDRRVTV GYIYMLKLHH LVDDKIHARS IGPYSLVTQQ PLGGKAQFGG
QRFGEMEVWA LEAYGAAYTL QEMLTVKSDD VSGRTKVYEA IVRGDDNFEA GIPESFNVLV
KELRSLGLNV ELNQRTY
