RPOB_CLOK1
ID RPOB_CLOK1 Reviewed; 1234 AA.
AC B9DYA1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-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=CKR_0175;
OS Clostridium kluyveri (strain NBRC 12016).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=583346;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 12016;
RA Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K., Vertes A.A.,
RA Yukawa H.;
RT "Complete genome sequence of Clostridium kluyveri and comparative genomics
RT of Clostridia species.";
RL Submitted (SEP-2005) 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; AP009049; BAH05226.1; -; Genomic_DNA.
DR RefSeq; WP_011988796.1; NC_011837.1.
DR AlphaFoldDB; B9DYA1; -.
DR SMR; B9DYA1; -.
DR EnsemblBacteria; BAH05226; BAH05226; CKR_0175.
DR KEGG; ckr:CKR_0175; -.
DR HOGENOM; CLU_000524_4_1_9; -.
DR Proteomes; UP000007969; 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; Transcription;
KW Transferase.
FT CHAIN 1..1234
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000165801"
FT REGION 1189..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1212
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1234 AA; 139107 MW; 8E14A0895B5025D3 CRC64;
MVHPVRVGKR TRMSFSRLKE IGHMPNLIEV QLDSYNWFLK EGLQEVFEDI NPIQDYTANL
NLEFVGYKLD MDNIKYSVEE CKERDSTYAA PLKVKVRLLN KETGEVKEQE VFMGDFPLMT
EQGTFIINGA ERVIVSQLVR SPGVYYDVSV DKTGKNLFSS TVIPNRGAWL EYETDSNNII
YVRIDKTRKL PITILVRAMG HGTDTEITNF FGEDERLKAT IEKDNTKTHE EALLEIYKRL
RPGEPPTVDS ARSLIESLFF DPKRYDLSRV GRYKFNKKLS LHLRIVNQIS TGDVVNPETG
EILVQKGEKI DREKAVQIQQ CGINSVDIEI EDTTLRVIGN NFVNINNFID FNIDDLNIKE
SVYYPALKQI LDNYSSEESI REQIKKNIHN LIPKHIIRDD IYATVSYELG LAYGVGHTDD
IDHLGNRRLR SVGELLQNQF RIGLSRMERV VKERMTIQDQ EVITPQALIN IRPVAASIKE
FFGSSQLSQF MDQTNPLSEL THKRRLSALG PGGLSRERAG FEVRDVHHSH YGRMCPIETP
EGPNIGLINS LATYAKVNEY GFIETPYRKV NKKEKIVTNE IVYMTADEED EYLIGRANEP
IDENGKFVDS KITVRDKEDV IVVPAEDVDY MDLSPRQLVS VATAMIPFLE NDDASRALMG
SNMQRQAVPL LKPQAPVVGT GIEYKAAVDS GVLPKARNAG VVSYVCANEI RVRRDSDGGT
DIYRLLKFQR SNQGTCINQR PIVEKGEIVQ QGTVLADGPS TDLGEIALGK NIRMGFTTWE
GYNYEDAMLI SEELVKKDVF TSIHIEEYES EARDTKLGPE EITRDIPNVG EDALKDIDDR
GIIKIGAEVR AGDILVGKVT PKGETELTAE ERLLRAIFGE KAREVRDTSL RVPHGEAGII
VDVKVFTRKN GDELSPGVNK LVRCYIAQKR KISVGDKMAG RHGNKGVISR VLPEEDMPFL
PDGRPLEICL NPLGVPSRMN IGQVLEVHLG WAASELGWHI ATPVFDGATE EDIIECLKKA
GYREDGKTIL YDGRTGEPFN RPVTVGYMYI LKLAHLVDDK IHARSTGPYS LVTQQPLGGK
AQFGGQRFGE MEVWALEAYG AAHTLQEILT VKSDDVVGRV KTYEAIVKGE NIPEPGVPES
FKVLIKELQA LCLDVKVLND DNQEIKLKES VDEEIENLDV NIEGNEDFVL SSQDNDYEEP
EENDEEDELN LDYDDLTLDD LKDDLKIEDF NDEH
