RPOB_MYCBP
ID RPOB_MYCBP Reviewed; 1178 AA.
AC A1KGE7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 90.
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=BCG_0716;
OS Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=410289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA Barrell B.G., Parkhill J., Cole S.T.;
RT "Genome plasticity of BCG and impact on vaccine efficacy.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAL70702.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM408590; CAL70702.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A1KGE7; -.
DR SMR; A1KGE7; -.
DR PRIDE; A1KGE7; -.
DR KEGG; mbb:BCG_0716; -.
DR HOGENOM; CLU_000524_4_1_11; -.
DR Proteomes; UP000001472; 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..1178
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300349"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1178 AA; 129865 MW; 3DA88DEC6A7DF661 CRC64;
MLEGCILADS RQSKTAASPS PSRPQSSSNN SVPGAPNRVS FAKLREPLEV PGLLDVQTDS
FEWLIGSPRW RESAAERGDV NPVGGLEEVL YELSPIEDFS GSMSLSFSDP RFDDVKAPVD
ECKDKDMTYA APLFVTAEFI NNNTGEIKSQ TVFMGDFPMM TEKGTFIING TERVVVSQLV
RSPGVYFDET IDKSTDKTLH SVKVIPSRGA WLEFDVDKRD TVGVRIDRKR RQPVTVLLKA
LGWTSEQIVE RFGFSEIMRS TLEKDNTVGT DEALLDIYRK LRPGEPPTKE SAQTLLENLF
FKEKRYDLAR VGRYKVNKKL GLHVGEPITS STLTEEDVVA TIEYLVRLHE GQTTMTVPGG
VEVPVETDDI DHFGNRRLRT VGELIQNQIR VGMSRMERVV RERMTTQDVE AITPQTLINI
RPVVAAIKEF FGTSQLSQFM DQNNPLSGLT HKRRLSALGP GGLSRERAGL EVRDVHPSHY
GRMCPIETPE GPNIGLIGSL SVYARVNPFG FIETPYRKVV DGVVSDEIVY LTADEEDRHV
VAQANSPIDA DGRFVEPRVL VRRKAGEVEY VPSSEVDYMD VSPRQMVSVA TAMIPFLEHD
DANRALMGAN MQRQAVPLVR SEAPLVGTGM ELRAAIDAGD VVVAEESGVI EEVSADYITV
MHDNGTRRTY RMRKFARSNH GTCANQCPIV DAGDRVEAGQ VIADGPCTDD GEMALGKNLL
VAIMPWEGHN YEDAIILSNR LVEEDVLTSI HIEEHEIDAR DTKLGAEEIT RDIPNISDEV
LADLDERGIV RIGAEVRDGD ILVGKVTPKG ETELTPEERL LRAIFGEKAR EVRDTSLKVP
HGESGKVIGI RVFSREDEDE LPAGVNELVR VYVAQKRKIS DGDKLAGRHG NKGVIGKILP
VEDMPFLADG TPVDIILNTH GVPRRMNIGQ ILETHLGWCA HSGWKVDAAK GVPDWAARLP
DELLEAQPNA IVSTPVFDGA QEAELQGLLS CTLPNRDGDV LVDADGKAML FDGRSGEPFP
YPVTVGYMYI MKLHHLVDDK IHARSTGPYS MITQQPLGGK AQFGGQRFGE MECWAMQAYG
AAYTLQELLT IKSDDTVGRV KVYEAIVKGE NIPEPGIPES FKVLLKELQS LCLNVEVLSS
DGAAIELREG EDEDLERAAA NLGINLSRNE SASVEDLA
