RPOB_CHRVO
ID RPOB_CHRVO Reviewed; 1390 AA.
AC Q7NQE6;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=CV_4193;
OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS 12614 / NCIMB 9131 / NCTC 9757).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=243365;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC
RC 9757;
RX PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T.,
RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R.,
RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F.,
RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S.,
RA Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M.,
RA Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P.,
RA Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S.,
RA Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N.,
RA Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P.,
RA Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R.,
RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J.,
RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F.,
RA Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z.,
RA de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F.,
RA Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C.,
RA Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M.,
RA Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT "The complete genome sequence of Chromobacterium violaceum reveals
RT remarkable and exploitable bacterial adaptability.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
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; AE016825; AAQ61853.1; -; Genomic_DNA.
DR RefSeq; WP_011137740.1; NC_005085.1.
DR AlphaFoldDB; Q7NQE6; -.
DR SMR; Q7NQE6; -.
DR STRING; 243365.CV_4193; -.
DR PRIDE; Q7NQE6; -.
DR EnsemblBacteria; AAQ61853; AAQ61853; CV_4193.
DR GeneID; 66366335; -.
DR KEGG; cvi:CV_4193; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_4; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000001424; 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; -; 2.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 2.
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..1390
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047883"
SQ SEQUENCE 1390 AA; 155556 MW; 49D002DC3E5BD0D5 CRC64;
MSYSFTEKKR IRKSFAKRAS VLDVPFLLAT QIDSYTEFLQ LGTPLDERKD VGLQAAFKSI
FPIVSHNGYA RLDFAHYVLG EPPFDVQECQ LRGITFAAPL RARIRLTIFD KESSKPVVKE
VRENEVYMGE IPLMTANGSF IINGTERVIV SQLHRSPGVF FEHDRGKTHS SGKLLFSARV
IPYRGSWLDF EFDPKDLLYF RIDRRRKMPV TILLKALGYT NEEILSEFYS FDTFYLTKSG
VFMRVVPERL KGEVAKFDIV AADGKLIVAK DKRITAKHIR DIQTAELDRI EVPADALLGK
MLAHNVVNQN TGEVIARANE EVTEEILAKL ALAEVEQVEV LFTNDLDQGA YISQTLRTDD
IQDQTQARVA IYRMMRPGEP PTEDAVEALF QRLFFSDETY DLSRVGRMKF SSRTYQYKFD
DKTPEWFKTL IGEKFASRRD VMEGTLATED IVSVIAILTE LRNGRGEVDD IDHLGNRRVR
SVGELAENQF RAGLVRVERA VKERLNQAES DNLMPHDLIN AKPVSAAIKE FFGSSQLSQF
MDQTNPLSEI THKRRVSALG PGGLTRERAG FEVRDVHPTH YGRVCPIETP EGPNIGLINS
LSVYARTNEF GFLETPYRKV VDGKVTNEID YLSAIEEGRY VIAQANAELD GEGALIDELV
TCREKGETIL ATPDRVQYMD VATGQVVSVA ASLIPFLEHD DANRALMGAN MQRQAVPCLR
PEKAFVGTGI ERSVAVDSGT TVVARRGGVV DYVDAGRVVV RVNDEEATAG EVGVDIYNLT
KFTRSNQNTN INQRPVVKVG DHIARGDVVA DGASTDLGEL ALGQNMTIAF MPWNGYNYED
SILISEKLVA EDRYTSIHIE ELSVVARDTK LGPEEITRDI PNLSERMAGR LDESGIVYIG
AEVEAGDVLV GKVTPKGETQ LTPEEKLLRA IFGEKASDVK DTSLRVPTGT VGTVIDVQVF
TREGIERDKR AQSIIDAELK RYRLDLNDQL RIFDNDAFSR IERLIVGKAA NGGPKRLAKG
TVIDQEYLAG LPTKHDWFDI RMADEDIAKQ LELIKESLAQ KREEFDLKFE DKKRKLTQGD
ELPPGVQKMV KVYLAVKRRL QAGDKMAGRH GNKGVVSRIL PVEDMPYMGD GRPVDIVLNP
LGVPSRMNIG QILEVHLGWA AKGIGERINR MVREQSAAEI RAYLERIYNE TGKPEEIAAL
SDAEVMQLAQ NLSKGMTFAT PVFDGAKEAE IKHMLDLAYP DGDELTEKMG FNESKTQMTL
FDGRSGEAFD RKVTVGVMHY LKLHHLVDDK MHARSTGPYS LVTQQPLGGK AQFGGQRFGE
MEVWALEAYG AAYTLQEMLT VKSDDVTGRT KVYENIVKGE HKIDAGMPES FNVLVKEIRS
LGLDMDLERY