RPOB_CORK4
ID RPOB_CORK4 Reviewed; 1168 AA.
AC C4LL71;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=ckrop_1858;
OS Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 /
OS CCUG 35717).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=645127;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717;
RX PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S.,
RA Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT revealed insights into the physiology of a lipophilic corynebacterium that
RT lacks mycolic acids.";
RL J. Biotechnol. 136:22-30(2008).
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; CP001620; ACR18576.1; -; Genomic_DNA.
DR RefSeq; WP_012732463.1; NC_012704.1.
DR AlphaFoldDB; C4LL71; -.
DR SMR; C4LL71; -.
DR STRING; 645127.ckrop_1858; -.
DR EnsemblBacteria; ACR18576; ACR18576; ckrop_1858.
DR KEGG; ckp:ckrop_1858; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_11; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000001473; 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; 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..1168
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000214472"
SQ SEQUENCE 1168 AA; 129067 MW; 821C1CD5200A50FB CRC64;
MLEGPILAVS RQTSLTSGIP GATKRYSFAK IKEPIEVPGL LDLQRDSFAW LIGAPEWRAK
KQAESEEGAR ITSGLEDILE ELSPIEDYSG NMSLTLSEPR FDDVKNTIDE AKDKDINYSA
PLYVTAEFTN AMSGEIKSQT VFIGDFPMMT DKGTFIINGT ERVIVSQLVR SPGVYFDESI
DKSTERPLHS VKVIPSRGAW LEFDIDKRDT VGVRIDRKRR QPVTVLLKAL GLSTQDITDR
FGFSELMMST LEHDGVANTD EALLEIYRKQ RPGESPTRDS AQALLDNSFF NPKRYDLAKV
GRYKVNRKLG LGGGSTTGEH TLTEEDILTT IEYLVRLHAG ERTMESPDGT ELMIATDDID
HFGNRRLRTV GELVQNQVRV GLSRMERVVR ERMTTQDAES ITPTSLINVR PVSAAIREFF
GTSQLSQFMD QNNSLSGLTH KRRLSALGPG GLSRERAGLD VRDVHASHYG RMCPIETPEG
PNIGLIGSLA SYARVNPFGF IETPYRRVEN GQATDVVDYL TADEEDRHIV AQANTKMDSE
GRFVEDTVEV RMKGGNVEVV PASEVDYMDV SPRQMVSVAT AMIPFLEHDD ANRALMGANM
QRQAVPLLRN EAPFVGTGME LRAAHDAGDV VIARRSGVVE TVCADFITTL GDDGQRDTFL
LRKFERTNQG TCYNQKPLVE AGDRIEEGQA LADGPGTENG EMALGRNLLV AFMPWEGHNY
EDAIILNQRI VEEDVLTSIH IEEHEIDARD TKLGPEEITR DIPNASEDIL ADLDERGIVR
IGADVRDGDI LVGKVTPKGE TELTPEERLL RAIFGEKARE VRDTSMKVPH GETGKVIGVR
VFSREDDDDL APGVNQMVRV YVAQKRKIQD GDKLSGRHGN KGVVGKILPA EDMPFLPDGT
PVDVILNTHG VPRRMNIGQV LELHLGMLAK SGWKVDPESQ DPAIKAMLET LPEDLYDVPA
DSRVATPVFD GTTNEELSGL MRSSRPNRDG DQMVNEFGKS TLIDGRTGEP FQQPISVGYM
YMLKLHHLVD EKIHARSTGP YSMITQQPLG GKAQFGGQRF GEMEVWAMQA YGAAYTLQEL
LTIKSDDVVG RVKVYEAIVK GDNIPDPGIP ESFKVLLKEL QSLCLNVEVL SADGTPVDLG
ADDDDLDQAN ASLGINLSRD ERFDADAV
