RPOB_RALPJ
ID RPOB_RALPJ Reviewed; 1368 AA.
AC B2UEN6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=Rpic_3314;
OS Ralstonia pickettii (strain 12J).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=402626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12J;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT "Complete sequence of chromosome 1 of Ralstonia pickettii 12J.";
RL Submitted (MAY-2008) 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; CP001068; ACD28436.1; -; Genomic_DNA.
DR RefSeq; WP_004634457.1; NC_010682.1.
DR AlphaFoldDB; B2UEN6; -.
DR SMR; B2UEN6; -.
DR STRING; 402626.Rpic_3314; -.
DR PRIDE; B2UEN6; -.
DR EnsemblBacteria; ACD28436; ACD28436; Rpic_3314.
DR KEGG; rpi:Rpic_3314; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_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_1000141724"
SQ SEQUENCE 1368 AA; 152264 MW; E6704370EDF762AF CRC64;
MAYSFTEKKR IRKSFAKRAT VHQVPFLLAT QIQSYAQFLQ ENAPVAQRKS EGLQAAFNAI
FPIVSHNGLA RMEFVSYHLS NPPFDVKECQ QRGLTFHSAL RAKVRLIIND RENPTKVKEI
KEQEVYMGEI PLMTSTGSFV INGTERVIVS QLHRSPGVFF EHDKGKTHSS GKLLFSARII
PYRGSWLDFE FDPKDILYFR VDRRRKMPVT ILLKSIGLTP EQILAHFFVF DNFTLKTEGA
LMEFVPERLR GEVARFDISD KNGKVVVEKD KRINAKHIRD LDSAGTKLIS VPEDYLLGRV
LAKNIVDPDT GEVLANANDE LTEGVLEKLR DAGVKEIQTL YTNDLDQGPY MSATLRTDDT
ADQTAARIAI YRMMRPGEPP TEDAVEALFQ RLFYSEDSYD LSRVGRMKVN SRLNRSSGTG
PMVLTDEDIL DTIKLLVNLR NGKGEVDDID HLGNRRVRCV GELAENQFRA GLSRVERAVK
ERLGQAETEN LMPHDLINSK PISSAIREFF GSSQLSQFMD QTNPLSEVTH KRRISALGPG
GLTRERAGFE VRDVHPTHYG RVCPIETPEG PNIGLINSLA LYAQLNDYGF LETPYRKVEN
GKLTDQVDYL SAIEEGKYVV AQANATLDKD GNLIDELVSA REGSERETRM VTPDRVQYID
VAPSQIVSAA ASLVPFLEHD DANRALMGAN MQRQAVPCLR ADKPLVGTGV ERTVAVDSGT
AVQATRGGVV DYVDANRVVI RVNDAEAVAG EVGVDIYNLI KYTRSNQNTN INQRPMVKVG
DVVARGDVIA DGASTDMGEL ALGQNMLVAF MPWNGYNFED SILISERVVA EDRYTSIHIE
ELSVVARDTK LGPEEITRDI SNLAEAQLAR LDESGITYIG AEVEAGDVMV GKVTPKGETQ
LTPEEKLLRA IFGEKASDVK DTSLRVPSGM SGTVIDVQVF TREGVVRDKR AQSIIDEELK
RYRLDLNDQL RIVEGDAFQR LERLLVGKIA NGGPKKLAKG TALTKEYLAD LDKWHWFDIR
PAEDEVALQL EAVKVAIEQK RHDFDLAFEE KRKKLTQGDE LPPGVIKMVK VYLAVKRRLQ
PGDKMAGRHG NKGVVSKITP IEDMPYMADG TPADIVLNPL GVPSRMNVGQ ILETHLGWAA
RGLGERIGNM LKAQAKAAEI RKLLGQIYNE SGKVEDLDSL SDAEILELAE NLKKGVPFAT
PVFDGAHEDE IRRMLDLAYP EDIAKEKGLT ASKQQVTLFD GRTGEAFERP VTLGVMHMLK
LHHLVDDKMH ARSTGPYSLV TQQPLGGKAQ FGGQRFGEME VWALEAYGAS YVLQEMLTVK
SDDVNGRTKV YENIVKGEHS IDAGMPESFN VLVKEIRSLG IDIDLERN
