ID Q64J77_CORAM Unreviewed; 1116 AA. AC Q64J77; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 12-AUG-2020, entry version 77. DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000256|RuleBase:RU363031}; DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU363031}; DE Flags: Fragment; GN Name=rpoB {ECO:0000313|EMBL:AAS89205.1}; OS Corynebacterium ammoniagenes (Brevibacterium ammoniagenes). OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=1697 {ECO:0000313|EMBL:AAS89205.1}; RN [1] {ECO:0000313|EMBL:AAS89205.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIP 101283 {ECO:0000313|EMBL:AAS89205.1}; RX PubMed=15364970; DOI=10.1128/JCM.42.9.3925-3931.2004; RA Khamis A., Raoult D., La Scola B.; RT "rpoB gene sequencing for identification of Corynebacterium species."; RL J. Clin. Microbiol. 42:3925-3931(2004). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of CC DNA into RNA using the four ribonucleoside triphosphates as substrates. CC {ECO:0000256|RuleBase:RU363031}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA- CC COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400; CC EC=2.7.7.6; Evidence={ECO:0000256|ARBA:ARBA00000097, CC ECO:0000256|RuleBase:RU363031}; 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:0000256|RuleBase:RU363031}. CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family. CC {ECO:0000256|RuleBase:RU000434}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY492243; AAS89205.1; -; Genomic_DNA. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro. 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 {ECO:0000256|ARBA:ARBA00022478, KW ECO:0000256|RuleBase:RU363031}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, KW ECO:0000256|RuleBase:RU363031}; KW Transcription {ECO:0000256|ARBA:ARBA00023163, KW ECO:0000256|RuleBase:RU363031}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363031}. FT DOMAIN 74..402 FT /note="RNA_pol_Rpb2_1" FT /evidence="ECO:0000259|Pfam:PF04563" FT DOMAIN 160..357 FT /note="RNA_pol_Rpb2_2" FT /evidence="ECO:0000259|Pfam:PF04561" FT DOMAIN 416..484 FT /note="RNA_pol_Rpb2_3" FT /evidence="ECO:0000259|Pfam:PF04565" FT DOMAIN 494..560 FT /note="RNA_pol_Rpb2_45" FT /evidence="ECO:0000259|Pfam:PF10385" FT DOMAIN 624..1041 FT /note="RNA_pol_Rpb2_6" FT /evidence="ECO:0000259|Pfam:PF00562" FT DOMAIN 1043..1115 FT /note="RNA_pol_Rpb2_7" FT /evidence="ECO:0000259|Pfam:PF04560" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAS89205.1" FT NON_TER 1116 FT /evidence="ECO:0000313|EMBL:AAS89205.1" SQ SEQUENCE 1116 AA; 124301 MW; 01A5E71051C249A0 CRC64; SRQTKSVANI PGAPKRYSFA KISEPIAVPG LLDLQLESFA WLIGTSEWRE RQQEERGEEH VSSGLEDILA ELSPIQDYSG NMSLSLSEPR FEPVKNTVDE CKEKDINYSA PLYVTAEFIN NDTQEIKSQT VFIGDFPMMT DEGTFIVNGT ERVVVSQLVR SPGVYFDQTI DKSTERPLHS VKVIPSRGAW LEFDVDKRDT VGVRIDRKRR QPVTVLLKAL GWTEQQIRDR FGFSELMMST LESDGIANTD EALLEIYRKQ RPGEQPTRDL AQSLLDNSFF RAKRYDLARV GRYKVNRKLG LGGDHEGLMT LTEEDIAVTL EYLVRLHTGE REMKAPNGEM IPVNTDDIDH FGNRRLRTVG ELIQNQVRVG LSRMERVVRE RMTTQDAESI TPTSLINVRP VSAAIREFFG TSQLSQFMDQ NNSLSGLTHK RRLSALGPGG LSRERAGIEV RDVHPSHYGR MCPIETPEGP NIGLIGSLAS YARVNAFGFI ETPYRKVENG RVTDEVRYLT ADEEDRYSIA QAEVEQDADG NIVGDRIEVR LKDGDIGVTD ANGVDYVDVS PRQMVSVGTA MIPFLEHDDA NRALMGANMQ KQAVPLVRGE APYVGTGMEL RAAYDAGDMV ISPKAGVVEN VNADLITIMD DEGVRDTYML RKFERTNQGT NYNQTPLVNM GDRVEAGQVL ADGPGTHNGE MSLGRNLLVA FMPWEGHNYE DAIILSQRIV EEDVLTSIHI EEHEIDARDT KLGAEEITRE IPNVSEDVLR DLDDRGIIRI GADVRAGDIL VGKVTPKGET ELTPEERLLR AIFGEKAREV RDTSMKVPHG ETGKVIGVAR FSREDDDDLA PGVNEMIRVY VAQKRKIQDG DKLAGRHGNK GVVGKVLPPE DMPFMADGTP VDVILNTHGV PRRMNIGQVL ELHLGWLAHT GWTVDTEDPK NEELLKTLPE ELYDVPADSL TATPVFDGAT NEEISRLLAS SKPNRDGDVM VDEDGKTVLF DGRSGEPYQY PISVGFMYIL KLHHLIDEKI HARSTGPYSM ITQQPLGGKA QFGGQRFGEM EVWAMQAYGA AYTLQELLTI KSDDVVGRVK VYEAIVKGDN IPDPGIPESF KVLLKELQSL CLNVEV //