RPOB_CLOBJ
ID RPOB_CLOBJ Reviewed; 1232 AA.
AC C1FMV9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=CLM_3956;
OS Clostridium botulinum (strain Kyoto / Type A2).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=536232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kyoto / Type A2;
RA Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001581; ACO83795.1; -; Genomic_DNA.
DR RefSeq; WP_003357408.1; NC_012563.1.
DR AlphaFoldDB; C1FMV9; -.
DR SMR; C1FMV9; -.
DR STRING; 536232.CLM_3956; -.
DR EnsemblBacteria; ACO83795; ACO83795; CLM_3956.
DR KEGG; cby:CLM_3956; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000001374; 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; Transcription;
KW Transferase.
FT CHAIN 1..1232
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000165800"
FT REGION 1170..1232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1232
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1232 AA; 138919 MW; 55AF0F1E3D23B72F CRC64;
MVHPVQVGKR TRMSFSRLKE VGQMPNLIEV QLDSYDWFLK EGLQEVFDDI NPIQDYTGNL
NLEFVGYKLD LDSIKYSVEE CKERDSTYAA PLKVKVRLLN KETGEIKEQE VFMGDFPLMT
EQGTFIINGA ERVIVSQLVR SPGVYYDMTV DKTGSKLFSA TVIPNRGAWL EYETDSNNII
YVRIDKTRKL PITILARALG YGTDAEIIEF FGEDERLKAT IEKDNTKTRE EALLEIYKRL
RPGEPPTVDS AESLIESLFF DAKRYDLSRV GRYKFNKKLA IHLRITNQIA DQDIVNPQTG
EILVQKGEKI DKDKAIEIQN CGINEVYIKI DDKSFKVIGN HFVDIHSLVP FDISDLNIKE
YVFYPVLKEI LDNYADEESI KEEIRKNIYR LIPKHIIRED IYATINYELG LSYDIGYKDD
IDHLGNRRLR SVGELLQNQF RIGLSRMERV VKERMTIQDQ EVITPQALIN IRPVAASIKE
FFGSSQLSQF MDQTNPLSEL THKRRLSALG PGGLSRERAG FEVRDVHHSH YGRMCPIETP
EGPNIGLINS LATFAKVNEY GFIETPYRRI DPKNKRATND IVYMTADEED LYVIARSDEP
IDENGYFIDD KVTVRAKEEV LVVPVSEVEY MDISPRQLVS VATAMIPFLE NDDASRALMG
SNMQRQAVPL LKPQAPIVGT GIEYKAATDS GVLPKAKNAG TVVYVSADEI RVRRDSDGGI
DKYKLLKFKR SNQGTCINQR PIVSKGEVVA KETLLADGPS TDLGEIALGK NILMGFITWE
GYNYEDAMLI SEQLVKEDVF TSIHIEEYEA EARDTKLGPE EITRDIPNVG EEALKDIDER
GIIRIGAEVR SGDILVGKVT PKGETELTAE ERLLRAIFGE KAREVRDTSL RVPHGEAGII
VDVKIFTREN GDELPPGVNK LVRCYIAQKR KISVGDKMAG RHGNKGVISR VLPEEDMPFL
PDGRPLQICL NPLGVPSRMN IGQVLEVHLG LAASKLGWHI ATPVFDGAIE SDIVDCLRKA
GYSEDGKTVL YDGRTGEPFD NRVTVGYMYI LKLAHLVDDK IHARSTGPYS LVTQQPLGGK
AQFGGQRFGE MEVWALEAYG AAHTLQEILT VKSDDVVGRV KTYEAIVKGE NIPEPGVPES
FKVLIKELQA LCLDVKVLND DNQEIKLKES VDEDADELEV NIEGTENQPE EKEEKEKEDS
DEYDDLREED VEPDLEELSL DDLDLDDFGD EH
