RPOB_CLAMS
ID RPOB_CLAMS Reviewed; 1162 AA.
AC B0RB25;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=CMS0269;
OS Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744
OS / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum).
OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Clavibacter.
OX NCBI_TaxID=31964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1;
RX PubMed=18192393; DOI=10.1128/jb.01598-07;
RA Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA Parkhill J., Ishimaru C.A.;
RT "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT sepedonicus suggests recent niche adaptation.";
RL J. Bacteriol. 190:2150-2160(2008).
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; AM849034; CAQ00390.1; -; Genomic_DNA.
DR RefSeq; WP_012297742.1; NZ_MZMM01000001.1.
DR AlphaFoldDB; B0RB25; -.
DR SMR; B0RB25; -.
DR STRING; 31964.CMS0269; -.
DR PRIDE; B0RB25; -.
DR EnsemblBacteria; CAQ00390; CAQ00390; CMS0269.
DR KEGG; cms:CMS0269; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_11; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000001318; 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..1162
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000086365"
SQ SEQUENCE 1162 AA; 128600 MW; 54C51E47FA9FCB83 CRC64;
MAAARNATPT PQNGRDASRL SFAKITDTLT VPDLLALQTE SFDWLVGSDA WKRRVEEGTK
QGRTDLALNS GLEEIFEEIS PIEDLGETMQ LGFTNPYLEE QKYSIDECKE RGKTYSAPLY
VEAEFMNHLT GEIKTQTVFM GDFPLMTEKG TFIINGTERV VVSQLVRSPG VYFERQQEKT
SDKDIYSARV IPSRGAWLEF EIDKRDQVGV RIDRKRKQSV TVFLKALGLT SEQILEEFKG
VASIELTLEK DSILTKEEAL KDIYRKLRPG EQVAAEAARA LLDNFYFNPK RYDLAKVGRY
KINRKLGIDK QLTDSVLTVE DILATIKYLV SLHANETKMN GTRDGKPVEL RLDVDDIDHF
GNRRIRAVGE LIQNQVRTGL SRMERVVRER MTTQDIEAIT PQTLINVRPV VAAIKEFFGT
SQLSQFMDQN NPLAGLTHKR RLSALGPGGL SRERAGVEVR DVHPSHYGRM CPIETPEGPN
IGLIGSLASF ARINSFGFIE TPYRRVVDGV VTDQIDYLTA SEEDEFLVAQ ANAPLTKDFR
FAEDRVLVRP KGGEVELVAK ENVHYMDVSP RQMVSVATSL IPFLEHDDAN RALMGANMQR
QAVPLLRSES PLVGTGMEGY AAIDAGDVLT ADASGVVAEV SAEVVTIQLD EGGTQTYYLR
KFDRSNQGTS YNHRVLVSAG DRIEAGEVIA DGPATENGEL ALGKNLLVAF MPWEGHNFED
AIILSQNLVK DDTLSSIHIE EYEVDARDTK LGKEEITRDL PNVSPELLAD LDERGIIRIG
AEVRPGDILV GKVTPKGETE LSAEERLLRA IFNEKSREVR DTSLKVPHGE QGTIIGVKVF
DSQDGDDELG SGVNQRVVVF IAQKRKITEG DKLAGRHGNK GVISKILPVE DMPFLADGTP
VDVILNPLGI PGRMNFGQVL ETHLGWSAKQ GWEVEGKPKW AERLPDHARQ APAGTKVATP
VFDGALEEEI AGLLDSTTVT RDGDRLIGSS GKTRLFDGRS GEPFPEPVSV GYMYILKLHH
LVDDKIHARS TGPYSMITQQ PLGGKAQFGG QRFGEMEVWA LEAYGAAYAL QELLTIKSDD
ILGRVKVYEA IVKGENIQEP GIPESFKVLI KEMQSLCLNV EVLSADGQAV SLRDTDDEVF
RAAEELGINI STRFESSSID DI