RPOB_MYCUA
ID RPOB_MYCUA Reviewed; 1176 AA.
AC A0PM24;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=MUL_0746;
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=362242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Agy99;
RX PubMed=17210928; DOI=10.1101/gr.5942807;
RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT "Reductive evolution and niche adaptation inferred from the genome of
RT Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL Genome Res. 17:192-200(2007).
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; CP000325; ABL03393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0PM24; -.
DR SMR; A0PM24; -.
DR STRING; 362242.MUL_0746; -.
DR PRIDE; A0PM24; -.
DR EnsemblBacteria; ABL03393; ABL03393; MUL_0746.
DR KEGG; mul:MUL_0746; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_11; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000000765; 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..1176
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300354"
FT REGION 13..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1176 AA; 129489 MW; A5EA2B775D61A03F CRC64;
MLEGRILADF RQTDASLHQG RPQSSSNSSV PGAPNRVSFA KLREPLEVPG LLDVQTDSFE
WLIGSQRWRE SAAQRGDATP VGGLEEVLYE LSPIEDFSGS MSLSFSDPRF DEVKAPVDEC
KDKDMTYAAP LFVTAEFINN NTGEIKSQTV FMGGFPMMTE KGTFIINGTE RVVVSQLVRS
PGVYFDETID KSTDKLLHSV KVIPSRGAWL EFDVDKRDTV GVRIDRKRRQ PVTVLLKALG
WSNEQIHERF GFSEIMMGTL EKDNTAGTDE ALLDIYRKLR PGEPPTKESA QTLLENLFFK
EKRYDLARVG RYKVNKKLGL NAGQPITSST LTEEDVVATI EYLVRLHEGQ TAMTAPGGVE
VPVETDDIDH FGNRRLRTVG ELIQNQIRVG MSRMERVVRE RMTTQDVEAI TPQTLINIRP
VVAAIKEFFG TSQLSQFMDQ NNPLSGLTHK RRLSALGPGG LSRERAGLEV RDVHPSHYGR
MCPIETPEGP NIGLIGSLSV YARVNPFGFI ETPYRKVVDG VVSDEIHYLT ADEEDRHVVA
QANSPIDAQG RFVEPRVLVR RKAGEVEYVP SSEVDYMDVS PRQMVSVATA MIPFLEHDDA
NRALMGANMQ RQAVPLVRSE APLVGTGMEL RAAIDAGDVV VADKAGVIEE VSADYITVMA
DDGTRHTYRM RKFARSNHGT CANQSPIVDA GERVEAGQVI ADGPCTQNGE MALGKNLLVA
IMPWEGHNYE DAIILSNRLV EEDVLTSIHI EEHEIDARDT KLGAEEITRD IPNVSDEVLA
DLDERGIVRI GAEVRDGDIL VGKVTPKGET ELTPEERLLR AIFGEKAREV RDTSLKVPHG
ESGKVIGIRV FSREDDDELP AGVNELVRVY VAQKRKISDG DKLAGRHGNK GVIGKILPAE
DMPFLPDGTP VDIILNTHGV PRRMNIGQIL ETHLGWVAKS GWNIDVANGV PEWAGKLPEN
LLSAQPDSIV STPVFDGAQE AELQGLLSAT LPNRDGEVLV DGDGKAKLFD GRSGEPFPYP
VTVGYMYIMK LHHLVDDKIH ARSTGPYSMI TQQPLGGKAQ FGGQRFGEME CWAMQAYGAA
YTLQELLTIK SDDTVGRVKV YEAIVKGENI PEPGIPESFK VLLKELQSLC LNVEVLSSDG
AAIELREGED EDLERAAANL GINLSRNESA SVEDLA