RPOB_CORGL
ID RPOB_CORGL Reviewed; 1165 AA.
AC Q8NT26;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
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};
GN OrderedLocusNames=Cgl0488, cg0576;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(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; BA000036; BAB97881.1; -; Genomic_DNA.
DR EMBL; BX927149; CAF19202.1; -; Genomic_DNA.
DR RefSeq; NP_599733.1; NC_003450.3.
DR RefSeq; WP_011265569.1; NC_006958.1.
DR AlphaFoldDB; Q8NT26; -.
DR SMR; Q8NT26; -.
DR STRING; 196627.cg0576; -.
DR KEGG; cgb:cg0576; -.
DR KEGG; cgl:Cgl0488; -.
DR PATRIC; fig|196627.13.peg.487; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_11; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000000582; 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..1165
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047889"
SQ SEQUENCE 1165 AA; 128785 MW; 4E36EA16EC689AED CRC64;
MLEGPILAVS RQTKSVVDIP GAPQRYSFAK VSAPIEVPGL LDLQLDSYSW LIGTPEWRAR
QKEEFGEGAR VTSGLENILE ELSPIQDYSG NMSLSLSEPR FEDVKNTIDE AKEKDINYAA
PLYVTAEFVN NTTGEIKSQT VFIGDFPMMT DKGTFIINGT ERVVVSQLVR SPGVYFDQTI
DKSTERPLHA VKVIPSRGAW LEFDVDKRDS VGVRIDRKRR QPVTVLLKAL GWTTEQITER
FGFSEIMMST LESDGVANTD EALLEIYRKQ RPGEQPTRDL AQSLLDNSFF RAKRYDLARV
GRYKINRKLG LGGDHDGLMT LTEEDIATTI EYLVRLHAGE RVMTSPNGEE IPVETDDIDH
FGNRRLRTVG ELIQNQVRVG LSRMERVVRE RMTTQDAESI TPTSLINVRP VSAAIREFFG
TSQLSQFMDQ NNSLSGLTHK RRLSALGPGG LSRERAGIEV RDVHPSHYGR MCPIETPEGP
NIGLIGSLAS YARVNPFGFI ETPYRRIIDG KLTDQIDYLT ADEEDRFVVA QANTHYDEEG
NITDETVTVR LKDGDIAMVG RNAVDYMDVS PRQMVSVGTA MIPFLEHDDA NRALMGANMQ
KQAVPLIRAE APFVGTGMEQ RAAYDAGDLV ITPVAGVVEN VSADFITIMA DDGKRETYLL
RKFQRTNQGT SYNQKPLVNL GERVEAGQVI ADGPGTFNGE MSLGRNLLVA FMPWEGHNYE
DAIILNQNIV EQDILTSIHI EEHEIDARDT KLGAEEITRD IPNVSEEVLK DLDDRGIVRI
GADVRDGDIL VGKVTPKGET ELTPEERLLR AIFGEKAREV RDTSMKVPHG ETGKVIGVRH
FSREDDDDLA PGVNEMIRIY VAQKRKIQDG DKLAGRHGNK GVVGKILPQE DMPFLPDGTP
VDIILNTHGV PRRMNIGQVL ETHLGWLASA GWSVDPEDPE NAELVKTLPA DLLEVPAGSL
TATPVFDGAS NEELAGLLAN SRPNRDGDVM VNADGKATLI DGRSGEPYPY PVSIGYMYML
KLHHLVDEKI HARSTGPYSM ITQQPLGGKA QFGGQRFGEM EVWAMQAYGA AYTLQELLTI
KSDDVVGRVK VYEAIVKGEN IPDPGIPESF KVLLKELQSL CLNVEVLSAD GTPMELAGDD
DDFDQAGASL GINLSRDERS DADTA
