RPOB_RHOOB
ID RPOB_RHOOB Reviewed; 1168 AA.
AC C1AYV9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, 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=ROP_16400;
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=632772;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4;
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-2009) 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; AP011115; BAH49887.1; -; Genomic_DNA.
DR RefSeq; WP_012688855.1; NC_012522.1.
DR AlphaFoldDB; C1AYV9; -.
DR SMR; C1AYV9; -.
DR STRING; 632772.ROP_16400; -.
DR EnsemblBacteria; BAH49887; BAH49887; ROP_16400.
DR KEGG; rop:ROP_16400; -.
DR PATRIC; fig|632772.20.peg.1721; -.
DR HOGENOM; CLU_000524_4_1_11; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000002212; 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_1000165817"
SQ SEQUENCE 1168 AA; 128199 MW; 123C89FEB44DE076 CRC64;
MLEGRILAVS SQTKAVSGIP GAPKRVSFAK IREPLEVPGL LDLQTDSFEW LIGAQSWRER
AAARGDSAIS GGLEDILAEL SPIEDFSGSM SLSFSDPRFD EVKASTDECK DKDMTYAAPL
FVTAEFINNN TGEIKSQTVF MGDFPMMTDK GTFIINGTER VVVSQLVRSP GVYFDHSVDK
GTEKDLHSVK VIPGRGAWLE FDVDKRDTVG VRIDRKRRQP VTVLLKALGW TTEQIAERFG
FSEILMATLE KDNTAGTDEA LLDIYRKLRP GEPPTKESAQ TLLENLFFKD KRYDLARVGR
YKINKKLGLN TGQPIVASTL TEEDIVATIE YLVRLHAGDT EMTAPGGVAV PVEVDDIDHF
GNRRLRTVGE LIQNQIRVGL SRMERVVRER MTTQDVEAIT PQTLINIRPV VAAIKEFFGT
SQLSQFMDQN NPLSGLTHKR RLSALGPGGL SRERAGLEVR DVHPSHYGRM CPIETPEGPN
IGLIGSLSVY ARVNPFGFIE TPYRKVEGGQ VTDQVDYLTA DEEDRHVVAQ ANSAVDANGH
FTDDRILVRR KGGEVEFVSS AEIDYMDVSP RQMVSVATAM IPFLEHDDAN RALMGANMQR
QAVPLVRSEA PLVGTGMELR AAVDAGDVIV TEKTGVVEEV SADYVTVMAD DGSRKTYRMR
KFARSNQGTC ANQRPIVDEG QRVESGQVLA DGPCTENGEM ALGKNLLVAI MPWEGHNYED
AIILSQRLVE EDVLTSIHIE EHEIDARDTK LGAEEITRDI PNVSDEVLAD LDERGIIRIG
AEVRDGDVLV GKVTPKGETE LTPEERLLRA IFGEKAREVR DTSLKVPHGE TGKVIGIRVF
SRDDDDDLPP GVNELVRVYV AQKRKIQDGD KLAGRHGNKG VIGKILPQED MPFLPDGTPI
DIILNTHGVP RRMNIGQILE THLGWIGKTG WNVQIAGDGS RPDWAEQLPE EMLSAPSDSN
IATPVFDGAK EDELTGLLGS TLPNRDGEVM VASDGKATLF DGRSGEPFPY PVSVGYMYII
KLHHLVDDKI HARSTGPYSM ITQQPLGGKA QFGGQRFGEM ECWAMQAYGA AYTLQELLTI
KSDDVVGRVK VYEAIVKGEN IPEPGIPESF KVLLKELQSL CLNVEVLSSD GAAIAMADGD
DEDLERAAAN LGINLSRNEA ATVDDLAN
