RPOB_ERYLH
ID RPOB_ERYLH Reviewed; 1396 AA.
AC Q2N5Q7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=ELI_14460;
OS Erythrobacter litoralis (strain HTCC2594).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=314225;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2594;
RX PubMed=19168610; DOI=10.1128/jb.00026-09;
RA Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL J. Bacteriol. 191:2419-2420(2009).
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; CP000157; ABC64984.1; -; Genomic_DNA.
DR RefSeq; WP_011415806.1; NC_007722.1.
DR AlphaFoldDB; Q2N5Q7; -.
DR SMR; Q2N5Q7; -.
DR STRING; 314225.ELI_14460; -.
DR PRIDE; Q2N5Q7; -.
DR EnsemblBacteria; ABC64984; ABC64984; ELI_14460.
DR KEGG; eli:ELI_14460; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_5; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000008808; 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..1396
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300310"
SQ SEQUENCE 1396 AA; 154476 MW; FA549A3FF42EF5D3 CRC64;
MASKAKNTAA AAKAEGTAKR RIRKIFGDIH EVVKMPNLIE VQRESYEQFL RSNKEIDYVS
GLEKTLRSVF PIRDFAGTAE LDFVHYELEP PKYDTTECRQ RGITYAAPMK VTLRLIVFEV
DQETETRSVL DIKEQDVYMG DMPLMTGNGT FIINGTERVI VSQMHRSPGV LFDHDRGKTH
SSGKLLFAAR VIPYRGSWLD FEFDAKDIVN VRIDRKRKLP VTALLYALGL DSEEILHFFY
NTVTWKRAGG KKGEGWKIPF EPEAWRGQKP TFALVDAKTG EEVFPANQKI SPRAANKAQK
DGLKDLLLPT EEVFARYAAK DMIDEKTGRI YIEAGDEVGP DHLEALDAAG IDELELLDID
EINTGPWIRN TLKVDKAENR DEGLEAIYKV MRPGEPPTKE TAEALFEGLF FDGERYDLSA
VGRVKLNMRL DLDAEDTVTT LRKEDILAVV KELVGLKDGK GDVDDIDNLG NRRVRSVGEL
LENQYRVGLL RMERAVKERM SSVDVSTVMP NDLINAKPAV AAVREFFGSS QLSQFMDQTN
PLSEVTHKRR VSALGPGGLT RERAGFEVRD VHPTHYGRIC PIETPEGPNI GLINSLSTFA
RVNKYGFIET PYRVVKDGKV TSEVIYLSAM EEQKHTVAQA SAELTEDGTF VEELISARQN
GDNLMAPSET VTLMDVSPKQ LVSVAASLIP FLENDDANRA LMGSNMQRQA VPLVKAEAPW
VGTGMEETVA RDSGAAITAT RGGIVDQVDA TRIVIRAIGD VEPGQSGVDI YTLQKFQRSN
QNTCINQRPL VKVGETVEAG DVIADGPSTD LGELALGKNT LVAFMPWNGY NYEDSILISE
RIVKDDVFTS IHIEEFEVMA RDTKLGPEDI TRDIPNVGEE ALRNLDEAGI VYIGAEVHPG
DILCGKITPK GESPMTPEEK LLRAIFGEKA SDVRDTSLRL PPGVAGTVVE VRVFNRHGIE
VDDRTRAIQQ EEIERLRKDS QDERTILNRA TYNRLRDMLL GQTASAAPKG VKKGVKIDEA
LLEGIDRHEW FKFAVADDNR QQQIEAVKSQ YDEAAKGIDD KFEDRKEKLE RGDELAPGVL
KMVKVFVAVK RKLQPGDKMA GRHGNKGVIS RILPVEDMPF LEDGTPVDIV LNPLGVPSRM
NVGQIFETHL GFAARGLGQQ VKNALEDWRA ANPDPEAGKP PEAVKETLQR VYGDRYEDDI
AGRSNAEIIE LASNLTAGVP MGTPVFDGAR EGDVTTQLEA AGIDSSGQSV LYDGRTGEAF
DRKVTVGIIY MLKLHHLVDD KIHARSIGPY SLVTQQPLGG KAQFGGQRFG EMEVWALQAY
GAAYTLQEML TVKSDDVVGR TKVYEAIVKG DDTFEAGIPE SFNVLVKEMR SLGLNVELSS
LTDGDEDDDG LQIAAE
