RPOB_RHOE4
ID RPOB_RHOE4 Reviewed; 1168 AA.
AC C0ZVQ6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, 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=RER_17330;
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC Rhodococcus erythropolis group.
OX NCBI_TaxID=234621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887;
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2005) 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; AP008957; BAH32441.1; -; Genomic_DNA.
DR RefSeq; WP_019744305.1; NC_012490.1.
DR AlphaFoldDB; C0ZVQ6; -.
DR SMR; C0ZVQ6; -.
DR STRING; 234621.RER_17330; -.
DR EnsemblBacteria; BAH32441; BAH32441; RER_17330.
DR GeneID; 57488127; -.
DR KEGG; rer:RER_17330; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_11; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000002204; 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; Transcription;
KW Transferase.
FT CHAIN 1..1168
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000214485"
SQ SEQUENCE 1168 AA; 128340 MW; 11B2A4838DBFC92E CRC64;
MLEGRILAVS SQTKAVSGIP GAPKRVSFAK VREPLEVPGL LDVQTDSFEW LIGAQSWRER
AAALGDNAVS GGLEDILAEL SPIEDFNGTM SLSFSDPRFD EVKASTDECK DKDMTYAAPL
FVTAEFINNN TGEIKSQTVF MGDFPMMTDK GTFIINGTER VVVSQLVRSP GVYFDMSVDK
STEKDLHSVK VIPGRGAWLE FDVDKRDTVG VRIDRKRRQP VTVLLKALGW TTEQITERFG
FSEILMATLE KDNTAGTDEA LLDIYRKLRP GEPPTKESAQ TLLENLFFKD KRYDLARVGR
YKINKKLGLN AGQPIVASTL TEEDIVATVE YLVRLHAGDT SMTAPGGVEV PVEVDDIDHF
GNRRLRTVGE LIQNQIRVGL SRMERVVRER MTTQDVEAIT PQTLINIRPV VAAIREFFGT
SQLSQFMDQN NPLSGLTHKR RLSALGPGGL SRERAGLEVR DVHPSHYGRM CPIETPEGPN
IGLIGSLSVY ARVNPFGFIE TPYRRVVDGQ VTDEVDYLTA DEEDRHVVAQ ANSAIDREGR
FTDSKILVRR KGGEVEFVAS SDIDYMDVSP RQMVSVATAM IPFLEHDDAN RALMGANMQR
QAVPLVRSEA PLVGTGMELR AAVDAGDVII TEKTGVVEEI SADYVTVMAD DGSRKTYRMR
KFARSNQGTC ANQRPIVDEG QRVEAGQVLA DGPCTENGEM ALGKNLLVAI MPWEGHNYED
AIILSQRLVE EDVLTSIHIE EHEIDARDTK LGAEEITRDI PNVSDEVLAD LDERGIIRIG
AEVRDGDVLV GKVTPKGETE LTPEERLLRA IFGEKAREVR DTSLKVPHGE TGKVIGIRVF
SRDEDDDLPP GVNELVRVYV AQKRKIQDGD KLAGRHGNKG VIGKILPQED MPFLSDGTPV
DIILNTHGVP RRMNIGQVLE THLGWIGKTG WNIQIASDGT RPDWAATLPE EMLSAPADSN
IATPVFDGAK EDELTGLLGA TLPNRDGEQM VGPDGKATLF DGRSGEPFPY PVSVGYMYII
KLHHLVDDKI HARSTGPYSM ITQQPLGGKA QFGGQRFGEM ECWAMQAYGA AYTLQELLTI
KSDDVVGRVK VYEAIVKGEN IPEPGIPESF KVLLKELQSL CLNVEVLSSD GAAITMADGD
DEDLERAAAN LGINLSRNEA ATVDDLAN
