RPOB_COREF
ID RPOB_COREF Reviewed; 1171 AA.
AC Q8FS97;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=CE0497;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(2003).
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; BA000035; BAC17307.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8FS97; -.
DR SMR; Q8FS97; -.
DR STRING; 196164.23492333; -.
DR EnsemblBacteria; BAC17307; BAC17307; BAC17307.
DR KEGG; cef:CE0497; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_11; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000001409; 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..1171
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047888"
SQ SEQUENCE 1171 AA; 129483 MW; 641022FA9E5D219B CRC64;
MIHPREVLEG PILAVSRQTK SVVDIPGAPK RYSFAKVSAP IEVPGLLDLQ LDSFAWLIGT
PEWRARQQEE FGEGARITSG LENILEELSP IQDYSGNMSL SLSEPRFEPV KNTIDEAKEK
DINYAAPLYV TAEFVNNTTG EIKSQTVFIG DFPMMTDKGT FIINGTERVV VSQLVRSPGV
YFDQTIDKST ERPLHAVKVI PSRGAWLEFD VDKRDSVGVR IDRKRRQPVT VLLKALGWTT
EQITERFGFS EIMMSTLESD GVANTDEALL EIYRKQRPGE QPTRDLAQSL LDNSFFKAKR
YDLAKVGRYK INRKLGLGGD NDGLMTLTEE DIATAIEYLV RLHAGERVMT SPTGEEIPVE
TDDIDHFGNR RLRTVGELIQ NQVRVGLSRM ERVVRERMTT QDAESITPTS LINVRPVSAA
IREFFGTSQL SQFMDQNNSL SGLTHKRRLS ALGPGGLSRE RAGIEVRDVH PSHYGRMCPI
ETPEGPNIGL IGSLASYARV NPFGFIETPY RRVIDGKLTD QIDYLTADEE DRFVVAQANT
HYDEDGVITD ESVTVRLKDG DIAMVSRTDV DYMDVSPRQM VSVGTAMIPF LEHDDANRAL
MGANMQKQAV PLVRAEAPFV GTGMELRAAY DAGDLVITPK AGVVENVTAD IVTIMDDEGK
RDTYVLRKFQ RTNQGTSYNQ KPLVNQGDRV EAGQVIADGP GTFNGEMSLG RNLLVAFMPW
EGHNYEDAII LNQNIVEQDI LTSIHIEEHE IDARDTKLGA EEITRDIPNV SEEVLKDLDE
RGIVRIGADV RDGDILVGKV TPKGETELTP EERLLRAIFG EKAREVRDTS MKVPHGETGK
VIGVRRFSRE DDDDLAPGVN EMIRVYVAQK RKIQDGDKLA GRHGNKGVVG KILPQEDMPF
LPDGTPVDII LNTHGVPRRM NIGQVLETHL GWLAAAGWSV DPEDPKNAEL IKTLPKELYD
VPAGSLTATP VFDGASNEEL AGLLANSRPN RDGDVMVNAD GKATLIDGRS GEPYPYPVSI
GYMYMLKLHH LVDEKIHARS TGPYSMITQQ PLGGKAQFGG QRFGEMEVWA MQAYGAAYTL
QELLTIKSDD VVGRVKVYEA IVKGENIPDP GIPESFKVLL KELQSLCLNV EVLSADGTPM
ELAGDDDDFD QAGASLGINL SRDERSDADT A
