RPOB_ARTS2
ID RPOB_ARTS2 Reviewed; 1171 AA.
AC A0JZ93;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
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=Arth_2984;
OS Arthrobacter sp. (strain FB24).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=290399;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB24;
RX PubMed=24501649; DOI=10.4056/sigs.4438185;
RA Nakatsu C.H., Barabote R., Thompson S., Bruce D., Detter C., Brettin T.,
RA Han C., Beasley F., Chen W., Konopka A., Xie G.;
RT "Complete genome sequence of Arthrobacter sp. strain FB24.";
RL Stand. Genomic Sci. 9:106-116(2013).
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; CP000454; ABK04363.1; -; Genomic_DNA.
DR RefSeq; WP_011692816.1; NC_008541.1.
DR AlphaFoldDB; A0JZ93; -.
DR SMR; A0JZ93; -.
DR STRING; 290399.Arth_2984; -.
DR PRIDE; A0JZ93; -.
DR EnsemblBacteria; ABK04363; ABK04363; Arth_2984.
DR KEGG; art:Arth_2984; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_11; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000000754; 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..1171
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300278"
SQ SEQUENCE 1171 AA; 128726 MW; 526EDE3873387C02 CRC64;
MVASSTSNVN NATAINADST DGATRRLSFA KIHEPLDVPN LLALQTDSFD WLVGNERWQA
RVAKAVEEGD LSVATSSGLS DIFEEISPIE DFQGTMSLSF SDPEFADPKY TMAECKDRDA
TYSAPLYVKA EFMNNNTGEI KQQTVFMGDF PLMTEKGTFV VNGTERVVVS QLVRSPGAYF
ERTADKTSDK DIFTAKIIPS RGAWFELEID KRDQVGVRLD RKRKQSVTVL LKALGWTEGQ
ILEEFGQYDS MRATLEKDAT ETREDALLDI YRKLRPGEPP TVEAAQSLLD NLYFNSKRYD
LAKVGRYKIN RKLGIDRSLG DKEASVLHVE DIVAMIKFLV ALHAGEKTLT GKRDGQDHEL
RVEIDDIDHF GNRRIRAVGE LIENQVRTGL SRMERVVRER MTTQDVEAIT PQTLINIRPV
VAAIKEFFGT SQLSQFMDQN NPLSGLTHKR RLSALGPGGL SRDRAGMEVR DVHPSHYGRM
CPIETPEGPN IGLIGSLASY GRINPFGFIE TPYRLVSEGV VSDEVQYLTA DDEAEVLIAQ
ANAPLDENKK FAEETVLVRA RGGGGEPVLV PAADVEFMDV SPRQMVSVAT ALIPFLEHDD
ANRALMGANM QRQAVPLVRS EAPFVGTGME RAAAVDAGDV VIAKKAGVVT EVSAELVIML
NDDGTETNYR INKFARSNQG NCYNHRVLVS EGQRLEVGGI IADGPATDQG ELALGKNLLV
AFMSWEGHNF EDAIILSQRI VAEDVLSSIH IEEHEIDARD TKLGAEEITR DIPNVSEEVL
AGLDERGIIH IGAEVEAGDI LVGKVTPKGE TELTPEERLL RAIFGEKSRE VRDTSLKVPH
GESGTVIGVR VFDRDNDDEL PPGVNQLVRV YVAAKRKITD GDKLAGRHGN KGVISKILPI
EDMPFLADGT PVDIVLNPLG VPGRMNVGQV LETHLGWVAK TGWKIEGEPE WVKQLPNLPR
ESGSTTVATP VFDGAREEEI TGLLDSTNVT RDGDRLINSS GKTRLFDGRS GEPFPDPISV
GYMYILKLHH LVDDKIHARS TGPYSMITQQ PLGGKAQFGG QRFGEMEVWA LEAYGAAYTL
QELLTIKSDD IHGRVKVYEA IVKGENIPEP GVPESFKVLI KEMQSLCLNV EVLSTDGTTI
EMRDSDDAVF TAAEELGIDL SRAEPSSVEE V