RPOB_CLONN
ID RPOB_CLONN Reviewed; 1241 AA.
AC A0PXT8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, 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=NT01CX_1107;
OS Clostridium novyi (strain NT).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=386415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NT;
RX PubMed=17115055; DOI=10.1038/nbt1256;
RA Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA Zhou S.;
RT "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT NT.";
RL Nat. Biotechnol. 24:1573-1580(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}.
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DR EMBL; CP000382; ABK61102.1; -; Genomic_DNA.
DR RefSeq; WP_011721210.1; NC_008593.1.
DR AlphaFoldDB; A0PXT8; -.
DR SMR; A0PXT8; -.
DR STRING; 386415.NT01CX_1107; -.
DR PRIDE; A0PXT8; -.
DR EnsemblBacteria; ABK61102; ABK61102; NT01CX_1107.
DR KEGG; cno:NT01CX_1107; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000008220; 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; 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..1241
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300301"
FT REGION 1186..1210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1241 AA; 139720 MW; 46E1343774DED8C0 CRC64;
MVHPIQIGKR TRMSFSKVKE MCPMPNLIEV QLNSYDWFWK EGLNEVFDDV NPIQDYTGNL
ILEFIDYNLD KDAIKYSVEE CKERDATYAA PLKVKVRLLN KETGEVKEQE VFMGDFPLMT
QQGTFVINGA ERVIVSQLVR SPGAYYGYDV DKTGKKLFSS TVIPNRGAWL EYETDSNDII
YVRIDKTRKL PISILIRALG LGSDAEIVDW FGEEERLKAT IEKDNTKTRE EALLEIYKRL
RPGEPPTVDS ALSLINSLFF DAKRYDLSRV GRYKFNKKLA IYIRLLNQVA AEDVVNPFTG
EIIVQKGETI DREKALEIQN CAINAVNIQV EDKVIKVIGN NFVDIHKFID FDISDLKIKE
HVHYPTLKNI LDNYTDEKSI KEEIKKNIHE LIPKHIVVDD IYATISYELG LPYEIGTIDD
IDHLGNRRLR SVGELLQNQF RIGLSRMERV VKERMTIQDQ EVITPQALIN IRPVAAAIKE
FFGSSQLSQF MDQTNPLSEL THKRRLSALG PGGLSRERAG FEVRDVHHSH YGRMCPIETP
EGPNIGLINS LACYAKVNEY GFIETPYRLV DKKEARVTDE IVYLTADEED HYLVAQAKEP
LDENGCFIDE KITVRDLEDV IVVSKDQVDL MDVSPSQIVS VATAMIPFLE NDDASRALMG
SNMQRQAVPL LKPAAPIVGT GIEYKAAVDS GVLPKAEHDG VIEYVSSTEV RIRRDSDGGL
DKHKLLKYKR SNQGTCINQR PIVSKGEKVK AGDVLADGPS TDFGEIALGQ NIRMGFITWE
GYNYEDAMLV SEQLVRDDIF TSIHIEEYES EARDTKLGPE EITRDIPNVG EDALKNIDER
GIVRIGAEVR SGDILVGKVT PKGETELTAE ERLLRAIFGE KAREVRDTSL RVPHGEAGII
VDVKVFTREN GDELPPGVNE LVRCYIAQKR KISVGDKMAG RHGNKGVISR ILPEEDMPFL
PDGRPLQICL NPLGVPSRMN IGQVLEVHLG WAAGEMGWHI ATPVFNGAFE DEIVELLQEA
GYSEDGKTVL YDGRTGEPFD NRVTVGYMYI LKLHHLVDDK IHARSTGPYS LVTQQPLGGK
AQFGGQRFGE MEVWALEAYG AAHTLQEVLT VKSDDVVGRV KTYEAIVKGE NIPEPGVPES
FKVLIKELQA LCLDVKVLSD TNEEIKIKES SEEDMEDLGV NIEGTEDEIV PTAEKRSSNQ
DEEALELVDN EEFEDIKLEY DDLQLDELEN GLELEDFNDE H
