RPOB_ALBFT
ID RPOB_ALBFT Reviewed; 1370 AA.
AC Q21SF7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 87.
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=Rfer_3592;
OS Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS (Rhodoferax ferrireducens).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=338969;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL Submitted (FEB-2006) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD71296.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000267; ABD71296.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041790955.1; NC_007908.1.
DR AlphaFoldDB; Q21SF7; -.
DR SMR; Q21SF7; -.
DR STRING; 338969.Rfer_3592; -.
DR PRIDE; Q21SF7; -.
DR EnsemblBacteria; ABD71296; ABD71296; Rfer_3592.
DR KEGG; rfr:Rfer_3592; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_4; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000008332; 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..1370
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300386"
SQ SEQUENCE 1370 AA; 152755 MW; E0CDA6317D83FD5F CRC64;
MAYSYTERKR IRKNFGSRDS VLEIPYLLQM QKDAYTAFLQ ADVHPKKRTA EGLQAAFEAA
FPIISHNGFV EMKYLEYNLA KPAFDVRECQ TRGLTFASAV RAKVQLFIYD RESSTSQNKV
IKEVKEQEVY MGEVPLMTTK GSFIINGTER VIVSQLHRSP GVFFEHDKGK THSSGKLLFS
ARIIPYRGSW LDFEFDPKDF LYFRVDRRRK MPVTILLKAI GLNHESILAN FFVNDNFRLM
DSGAQMEFVA ERLRGEVARF DITDKSGKVI VAKEKRVTAR HTRELEQSGT THISVPEDFL
LGRVVARNIV DTDTGEILAK ANEELTEALI KKLRLAGVQD LPCIYTNELD QGAYISQTLR
SDETVDEFAA RVAIYRMMRP GEPPTEDAVQ ALFQRLFYNP DTYDLSRVGR MKFNAKMGRP
ESTGPMVLTN EDILAVVKIL VDLRNGRGDV DDIDHLGNRR VRCVGELAEN QYRTGLARIE
KAVKERLGQA EQEPLMPHDL INSKPISAAL KEFFGASQLS QFMDQTNPLS EITHKRRVSA
LGPGGLTRER AGFEVRDVHV THYGRVCPIE TPEGPNIGLI NSLALYARLN DYGFIETPYR
RVVDGKVTME IDYLSAIEEG KFVIAQANAV LDKDGKLTGE MISAREAGET IFAGPERVQY
MDVSPAQIVS VAASLVPFLE HDDANRALMG ANMSRQAVPI LRPEKPMVGT GIERVAAIDS
GTVVTATRGG MVDYVDATRV VIRVNDDEAQ AGEVGVDIYN LIKYQRSNQN TNIHQRPIVK
KGDMLAKGDV IADGASTDLG ELALGQNMLI GFMTWNGYNF EDSILISERV VADDRYTSIH
IEELVVMARD TKLGCEEITR DIPNLSEQQL NRLDESGIIY VGAEVQPGDT LVGKVTPKGE
TTLTPEEKLL RAIFGEKASD VKDTSLRVDQ GSQGTVIDVQ VFTREGIVRD RRAQQIIDDE
LKRFRLDLND QLRLVEADSF DRIEKLLVGK VANGGPQKLA KGTTIDKAYL TSVEKHHWFD
IRPAEDDVAA QLESIKNSME QTRHSFDLAF EEKRKKLTQG DELPAGVLKM VKVYLAVKRH
LQPGDKMAGR HGNKGVVSKI VPVEDMPFMA DGTPCDIVLN PLGVPSRMNI GQVLEVHLGW
AAKGIGQRIG DMLQAEAKVA ELRKFLDELY NGTGRKEDLA QLSDDEVLEM AGNLTSGVPF
ATPVFDGASE ADIGAMLKLA YPEDAIRQKG LTPARTQAYL YDGRTGDPFE RPTTIGYMHY
LKLHHLVDDK MHARSTGPYS LVTQQPLGGK AQFGGQRFGE MEVWALEAYG AAYTLQEMLT
VKSDDVQGRT KVYESIVKGE HSIEAGMPES FNVLVKEIRS LGIDIELERG