RPOB_RHOJR
ID RPOB_RHOJR Reviewed; 1168 AA.
AC Q0SFB3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 110.
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};
GN OrderedLocusNames=RHA1_ro01962;
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=101510;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1;
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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; CP000431; ABG93773.1; -; Genomic_DNA.
DR RefSeq; WP_011594854.1; NC_008268.1.
DR AlphaFoldDB; Q0SFB3; -.
DR SMR; Q0SFB3; -.
DR STRING; 101510.RHA1_ro01962; -.
DR EnsemblBacteria; ABG93773; ABG93773; RHA1_ro01962.
DR KEGG; rha:RHA1_ro01962; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_11; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000008710; 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..1168
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300385"
SQ SEQUENCE 1168 AA; 128316 MW; C5B9D7CA7A302DAF CRC64;
MLEGRILAVS SQTKAVSGIP GAPKRVSFAK IREPLEVPGL LDVQTDSFEW LIGAQSWRER
AAARGDSAIS GGLEDILAEL SPIEDFSGSM SLSFSDPRFD EVKASTDECK DKDMTYAAPL
FVTAEFINNN TGEIKSQTVF MGDFPMMTDK GTFIINGTER VVVSQLVRSP GVYFDHSVDK
GTEKDLHSVK VIPGRGAWLE FDVDKRDTVG VRIDRKRRQP VTVLLKALGW TTEQITERFG
FSEILMATLE KDNTAGTDEA LLDIYRKLRP GEPPTKESAQ TLLENLFFKD KRYDLARVGR
YKINKKLGLN LGQPIVASTL TEEDIVATIE YLVRLHAGDT EMTAPGGSAV PVEVDDIDHF
GNRRLRTVGE LIQNQIRVGL SRMERVVRER MTTQDVEAIT PQTLINIRPV VAAIKEFFGT
SQLSQFMDQN NPLSGLTHKR RLSALGPGGL SRERAGLEVR DVHPSHYGRM CPIETPEGPN
IGLIGSLSVY ARVNPFGFIE TPYRKVENGQ VTDQVDYLTA DEEDRHVVAQ ANSALDANGH
FTDDRILVRR KGGEVEFVSS AEIDYMDVSP RQMVSVATAM IPFLEHDDAN RALMGANMQR
QAVPLVRSEA PLVGTGMELR AAVDAGDVIV TEKTGVVEEV SADYVTVMAD DGSRKTYRMR
KFARSNQGTC ANQRPIVDEG QRVEFGQVLA DGPCTENGEM ALGKNLLVAI MPWEGHNYED
AIILSQRLVE EDVLTSIHIE EHEIDARDTK LGAEEITRDI PNVSDEVLAD LDERGIIRIG
AEVRDGDVLV GKVTPKGETE LTPEERLLRA IFGEKAREVR DTSLKVPHGE TGKVIGIRVF
SRDDDDDLPP GVNELVRVYV AQKRKIQDGD KLAGRHGNKG VIGKILPQED MPFLPDGTPV
DIILNTHGVP RRMNIGQILE THLGWIGKTG WNVQIAGDGS RPDWAEQLPE EMLSAPADSN
IATPVFDGAK EDELTGLLGS TLPNRDGEVM VASDGKATLF DGRSGEPFPY PVSVGYMYII
KLHHLVDDKI HARSTGPYSM ITQQPLGGKA QFGGQRFGEM ECWAMQAYGA AYTLQELLTI
KSDDVVGRVK VYEAIVKGEN IPEPGIPESF KVLLKELQSL CLNVEVLSSD GAAIAMADGD
DEDLERAAAN LGINLSRNEA ATVDDLAN
