RPOB_BAUCH
ID RPOB_BAUCH Reviewed; 1340 AA.
AC Q1LSX7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-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=BCI_0502;
OS Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX NCBI_TaxID=374463;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H.,
RA Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.;
RT "Metabolic complementarity and genomics of the dual bacterial symbiosis of
RT sharpshooters.";
RL PLoS Biol. 4:1079-1092(2006).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000238; ABF13801.1; -; Genomic_DNA.
DR RefSeq; WP_011520670.1; NC_007984.1.
DR AlphaFoldDB; Q1LSX7; -.
DR SMR; Q1LSX7; -.
DR STRING; 374463.BCI_0502; -.
DR PRIDE; Q1LSX7; -.
DR EnsemblBacteria; ABF13801; ABF13801; BCI_0502.
DR KEGG; bci:BCI_0502; -.
DR HOGENOM; CLU_000524_4_3_6; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000002427; 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; 2.40.270.10; -; 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; 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..1340
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300283"
SQ SEQUENCE 1340 AA; 151516 MW; A440D6F8FE9F23E0 CRC64;
MLYSYTEKKR IRKDFGKRSQ VLDVPYLLSI QLESFQKFIE RDNEGQHGLE AAFRSVFPIQ
SYSGNAELQY VSYHLGEPVF DVKECQTRGL TFSAPLRVIL RLIIRDATTE TPIKEQEVYM
GEIPLMTENG TFVINGTERV IVSQLHRSPG VFFDSDKGKI HSSGKVLFNA RIIPYRGSWL
DFEFDQKDHL FVRIDRRRKL PATIILRALQ LSTNQILDTF FEKVIFHLND EHIQMELVPE
RLRGETASFD IIANGTIYVN KGRRITARHI HQLKIDSIDR INVPREYLVG KIIAIDYIHD
NTGEIIVPAN IEITLEILDK LGKANFKRIE TLFTNDLDHG AYISETLRID STRDRLSALV
EIYRMMRPGE PPTREAAENL FENIFFSEDR YDLSAVGRMK FNRALLREEI EGSGLLSKSD
IIEVMKKLID IRNGKGEVDD IDHLGNRRVR SVGEMAENQF RIGLVRVERA VKERLSLSDL
ESLMPQDIIN AKPISAAIKE FFGSSQLSQF MDQNNPLSEI THKRRISALG PGGLTRERAG
FEVRDVHPTH YGRVCPIETP EGPNIGLINS LSVYAKTNEY GFLETPYRLV HNSVVTEEIH
YLSAIEEGNF IIAQANTNLD DKGNFVEELV TCRHKGESGF FSREKVHYMD VSTQQIVSVG
ASLIPFLEHD DANRALMGAN MQRQAVPTLR TDKPLVGTGM ERIVAVDSGV TVVAKRGGIV
QYVDASRIVI NVHSDEMYSG EAGIDIYHMT KYIRSNQNTC ISQKPCVTLG ELVERGNVLA
DGPSTDLGEL ALGQNMRIAF MPWNGYNFED SMLVSERVVQ KDCFTTIHIQ ELACMSRDTK
LGPEEITSDI PNVGEAALCK LDESGIVYIG AEVTSGDILV GKVTPKGETQ LTPEEKLLRA
IFGEKASDVK DSSLRVPNGY SGTVIDVQIF TRDGVKKDKR TLEIEEMQLQ QAKKDLTEER
RIFEAALFTR IRHVLGSDIT NIDIVKILKL KREDWSQFNI KDNNKYCQLE QLAEQYYELN
KVFANKLEEK RRKITQGDDL SPGVLKIVKV YIAVKRQIQP GDKMAGRHGN KGVISKINPI
EDMPYDEKGI PVDIVLNPLG VPSRMNIGQI LETHLGMAAK GIGDKINKML KQHKNAEQLR
QFIQKAYDIG DQVRQKVNLN LFSDQEILLL AENLKHGMPM ATPVFDGAKE KEIKQMLQLA
ELPVSGQITL FDGRTGEPFE RQVTVGYMYM LKLNHLVDDK MHARSTGSYS LVTQQPLGGK
AQFGGQRFGE MEVWALEAYG AAYTLQEMLT VKSDDVNGRT KMYKNIVDCN HTMEPAMPES
FNVLLKEIRS LGINIELEKN
