RPOB_CUPPJ
ID RPOB_CUPPJ Reviewed; 1368 AA.
AC Q46WD4;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=Reut_A3189;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
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; CP000090; AAZ62549.1; -; Genomic_DNA.
DR RefSeq; WP_011299319.1; NC_007347.1.
DR AlphaFoldDB; Q46WD4; -.
DR SMR; Q46WD4; -.
DR STRING; 264198.Reut_A3189; -.
DR EnsemblBacteria; AAZ62549; AAZ62549; Reut_A3189.
DR KEGG; reu:Reut_A3189; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_4; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
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..1368
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000224099"
SQ SEQUENCE 1368 AA; 152559 MW; 47CAB3FFBD7388C1 CRC64;
MAYSFTEKKR IRKSFAKRAT VHQVPFLLAT QIESYTQFLQ AETPAARRKT EGLQAAFNAI
FPIASHNGLA RMEFVSYHLS NPPFDVKECQ QRGLTFHSAL RAKVRLIIND RENPGKVKEV
KEQEVYMGEI PLMTSTGSFV INGTERVIVS QLHRSPGVFF EHDKGKTHSS GKLLFSARII
PYRGSWLDFE FDPKDILYFR VDRRRKMPVT ILLKSIGLTP EQILAHFFVF DNFTLQSEGA
QLEFVPERLR GEVARFDIAD KNGRVVVEKD KRINAKHIRD LDSAGTKLIS VPEDYLLGRV
LAKNIIDPDT GEVIANANDE LTETVLENLR EAGVKQIQTL YTNDLDQGPY MSQTLRVDET
ADQTAARIAI YRMMRPGEPP TEEAVEALFQ RLFYSEESYD LSRVGRMKVN SRLSRPSGEG
SMVLQDEDIL ETIKILVNLR NGKGEVDDID HLGNRRVRCV GELAENQFRA GLSRVERAVK
ERLGQAETEN LMPHDLINSK PISSAIREFF GSSQLSQFMD QTNPLSEITH KRRVSALGPG
GLTRERAGFE VRDVHPTHYG RVCPIETPEG PNIGLINSLA LYARLNEYGF LETPYRKVEN
SKLTDQVDYL SAIEEGKYVV AQANATVDAE GNLTDELVSA REGSERETRM VTPDRVQYID
VAPSQIVSAA ASLVPFLEHD DANRALMGAN MQRQAVPCLR PDKPLVGTGI ERTVAVDSGT
AVQAMRGGVV DYVDAMRIVI RVNDDEAVAG EVGVDIYNLI KYTRSNQNTN INQRPMVKVG
DIVARGDVVA DGASTDLGEL ALGQNMLVAF MPWNGYNFED SILISERVVA EDRYTSIHIE
ELSVVARDTK LGPEEITRDI SNLAEAQLAR LDESGITYIG AEVEAGDVLV GKVTPKGETQ
LTPEEKLLRA IFGEKASDVK DTSLRVPSGM SGIVIDVQVF TREGVTRDKR AQSIIDDELK
RYRLDLNDQL RIVEGDAFQR LERLLIDKTV NGGPKKLAKG AKLTKEYLAE IDKYHWFDIR
PADEEVAAQL EAVKEAIEQK RHEFDLAFEE KRKKLTQGDE LPPGVIKMVK VYLAVKRRLQ
PGDKMAGRHG NKGVVSKIVP IEDMPYMADG TPADIVLNPL GVPSRMNVGQ ILETHLGWAA
RGLGQRIGDM LKASAKAQEL RPLLAQIYNE SGKAEDLDSL SDAEVLELAT NLKKGVPFAT
PVFDGAHEDE IRRMLDLAYP DDIAKEKGLT ASKQQVTLHD GRTGEAFERP VTLGVMHMLK
LHHLVDDKMH ARSTGPYSLV TQQPLGGKAQ FGGQRFGEME VWALEAYGAS YVLQEMLTVK
SDDVNGRTKV YENIVKGEHS IDAGMPESFN VLVKEIRSLG IDIDLDRY