RPOB_MYCTA
ID RPOB_MYCTA Reviewed; 1177 AA.
AC A5U052;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 74.
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=MRA_0676;
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=419947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA Wang H., Wang S., Zhao G., Zhang Y.;
RT "Genetic basis of virulence attenuation revealed by comparative genomic
RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL PLoS ONE 3:E2375-E2375(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; CP000611; ABQ72402.1; -; Genomic_DNA.
DR AlphaFoldDB; A5U052; -.
DR SMR; A5U052; -.
DR STRING; 419947.MRA_0676; -.
DR EnsemblBacteria; ABQ72402; ABQ72402; MRA_0676.
DR KEGG; mra:MRA_0676; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_11; -.
DR Proteomes; UP000001988; 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; Transcription;
KW Transferase.
FT CHAIN 1..1177
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300353"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1177 AA; 129752 MW; 6672916C1382DB2B CRC64;
MEGCILADSR QSKTAASPSP SRPQSSSNNS VPGAPNRVSF AKLREPLEVP GLLDVQTDSF
EWLIGSPRWR ESAAERGDVN PVGGLEEVLY ELSPIEDFSG SMSLSFSDPR FDDVKAPVDE
CKDKDMTYAA PLFVTAEFIN NNTGEIKSQT VFMGDFPMMT EKGTFIINGT ERVVVSQLVR
SPGVYFDETI DKSTDKTLHS VKVIPSRGAW LEFDVDKRDT VGVRIDRKRR QPVTVLLKAL
GWTSEQIVER FGFSEIMRST LEKDNTVGTD EALLDIYRKL RPGEPPTKES AQTLLENLFF
KEKRYDLARV GRYKVNKKLG LHVGEPITSS TLTEEDVVAT IEYLVRLHEG QTTMTVPGGV
EVPVETDDID HFGNRRLRTV GELIQNQIRV GMSRMERVVR ERMTTQDVEA ITPQTLINIR
PVVAAIKEFF GTSQLSQFMD QNNPLSGLTH KRRLSALGPG GLSRERAGLE VRDVHPSHYG
RMCPIETPEG PNIGLIGSLS VYARVNPFGF IETPYRKVVD GVVSDEIVYL TADEEDRHVV
AQANSPIDAD GRFVEPRVLV RRKAGEVEYV PSSEVDYMDV SPRQMVSVAT AMIPFLEHDD
ANRALMGANM QRQAVPLVRS EAPLVGTGME LRAAIDAGDV VVAEESGVIE EVSADYITVM
HDNGTRRTYR MRKFARSNHG TCANQCPIVD AGDRVEAGQV IADGPCTDDG EMALGKNLLV
AIMPWEGHNY EDAIILSNRL VEEDVLTSIH IEEHEIDARD TKLGAEEITR DIPNISDEVL
ADLDERGIVR IGAEVRDGDI LVGKVTPKGE TELTPEERLL RAIFGEKARE VRDTSLKVPH
GESGKVIGIR VFSREDEDEL PAGVNELVRV YVAQKRKISD GDKLAGRHGN KGVIGKILPV
EDMPFLADGT PVDIILNTHG VPRRMNIGQI LETHLGWCAH SGWKVDAAKG VPDWAARLPD
ELLEAQPNAI VSTPVFDGAQ EAELQGLLSC TLPNRDGDVL VDADGKAMLF DGRSGEPFPY
PVTVGYMYIM KLHHLVDDKI HARSTGPYSM ITQQPLGGKA QFGGQRFGEM ECWAMQAYGA
AYTLQELLTI KSDDTVGRVK VYEAIVKGEN IPEPGIPESF KVLLKELQSL CLNVEVLSSD
GAAIELREGE DEDLERAAAN LGINLSRNES ASVEDLA
