RPOB_TOLAT
ID RPOB_TOLAT Reviewed; 1342 AA.
AC C4LBV2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=Tola_2783;
OS Tolumonas auensis (strain DSM 9187 / TA4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Tolumonas.
OX NCBI_TaxID=595494;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9187 / TA4;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S.,
RA Beller H.;
RT "Complete sequence of Tolumonas auensis DSM 9187.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001616; ACQ94376.1; -; Genomic_DNA.
DR AlphaFoldDB; C4LBV2; -.
DR SMR; C4LBV2; -.
DR STRING; 595494.Tola_2783; -.
DR PRIDE; C4LBV2; -.
DR EnsemblBacteria; ACQ94376; ACQ94376; Tola_2783.
DR KEGG; tau:Tola_2783; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_6; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000009073; 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; 2.
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..1342
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000214490"
SQ SEQUENCE 1342 AA; 149814 MW; 6B2D8492F93590F5 CRC64;
MVNSYTEKKR IRKDFGKRDQ VLETPYLLSI QLDSFKQFLD ADPEGAYGLE AAFRSVFPIT
SYSGTAELQY VSYRLGEPVF DVKECQIRGV TYSAPLRVKL RLVLFDKEAA AGTVKEIKEQ
EVYMGEIPLM TDNGTFVING TERVIVSQLH RSPGVFFDHD KGKTHSSGKV LYNARVIPYR
GSWLDFEFDA KDNLFVRIDR RRKLPATIIL RALEFTTEEI LTTFFETIKF EIKDGKVLME
LVPERLRGET ATFDIVAGGD VVVEKGRRIT ARHIRQLEKA GISQIEVPVE YVVGKISARD
YVNPQTGEVM INANTALSLE AIANLSQAGF KQFEVLFTNE LDHGSYISET LRIDSSTNRL
EALVEIYRMM RPGEPPTKDA AEQLFENLFF SADRYDLSTV GRMKFNSRLA RPDHIGSGIL
SQDDIVDVMK QLIAIRNGKD DVDDIDHLGN RRIRSVGEMA ENQFRVGLVR VERAVKERLS
LGDLDAIQPQ DLINAKPISA AVKEFFGSSQ LSQFMDQNNP LSEITHKRRI SALGPGGLTR
ERAGFEVRDV HPTHYGRLCP IETPEGPNIG LINSLAVYSR TNEYGFLETP YRKVIDGVIT
DEVDYLSAIE EGNFVIAQAN ANVDADARLK DELIPCRHKG ESTFMNAEQI QYMDVSPQQV
VSVAASLIPF LEHDDANRAL MGSNMQRQAV PTLRADKPLV GTGMERAVAV DSGVTVVAKR
GGTIDYVDAS RIVVKVNEDE LLPGEAGIDI YNLTKYTRSN QNTCINQRPC VSVGEPVMLG
DVLADGPSTD LGELALGQNM RVAFMPWNGY NFEDSILVSE RVVQEDRLTT IHIQELSCIA
RDTKLGPEEI TADIPNVGEA ALSKLDESGI VYVGAEVKGG DILVGKVTPK GETQLTPEEK
LLRAIFGEKA SDVKDSSLRV PNGVYGTVID VQVFTRDGVE KDKRAKEVED MQLRDAKKDL
TEEFKILEDG IFGRARSLLI ANGFGEDRLS KLDRKRWLEQ SLDDEGKQVE LEQIAEQHIA
LKEEFDRKFE AKRQKIIQGD DLAPGVLKIV KVYLAVKRRI QPGDKMAGRH GNKGVISKIC
PVEDMPYDDE GNPVDIVLNP LGVPSRMNIG QILEVHLGLA AKGIGEKIDR MVKEQRELAE
LREFLQRVYD LGGSDQQQID IATLSDDDVR TLVQNLRKGL PVATPVFDGA KESEIKELLK
LADKPESGQI TLFDGRTGMP FERVVTVGYM YMLKLNHLVD DKMHARSTGS YSLVTQQPLG
GKAQFGGQRF GEMEVWALEA YGAAYTLQEM LTVKSDDVNG RTKMYKNIVD GDHRMEPGIP
ESFNVLLKEI RSLGINIELE EE
