ID Q64J77_CORAM Unreviewed; 1116 AA. AC Q64J77; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 28-JUN-2023, entry version 85. 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; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; 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:14527, Rhea:RHEA- CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; CC EC=2.7.7.6; Evidence={ECO:0000256|ARBA:ARBA00024550, 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 AlphaFoldDB; Q64J77; -. DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC. DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro. DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro. DR CDD; cd00653; RNA_pol_B_RPB2; 1. DR Gene3D; 2.40.50.100; -; 1. DR Gene3D; 2.40.50.150; -; 1. DR Gene3D; 3.90.1100.10; -; 1. DR Gene3D; 2.30.150.10; DNA-directed RNA polymerase, beta subunit, external 1 domain; 1. DR Gene3D; 2.40.270.10; DNA-directed RNA polymerase, subunit 2, domain 6; 1. DR Gene3D; 3.90.1800.10; RNA polymerase alpha subunit dimerisation domain; 1. DR Gene3D; 3.90.1110.10; RNA polymerase Rpb2, domain 2; 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; DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2; 1. DR PANTHER; PTHR20856:SF20; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 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 SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 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 polymerase beta subunit protrusion" FT /evidence="ECO:0000259|Pfam:PF04563" FT DOMAIN 160..357 FT /note="RNA polymerase Rpb2" FT /evidence="ECO:0000259|Pfam:PF04561" FT DOMAIN 416..484 FT /note="RNA polymerase Rpb2" FT /evidence="ECO:0000259|Pfam:PF04565" FT DOMAIN 494..560 FT /note="DNA-directed RNA polymerase beta subunit external 1" FT /evidence="ECO:0000259|Pfam:PF10385" FT DOMAIN 624..1041 FT /note="DNA-directed RNA polymerase subunit 2 hybrid- FT binding" FT /evidence="ECO:0000259|Pfam:PF00562" FT DOMAIN 1043..1115 FT /note="RNA polymerase Rpb2" 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 //