RPOB_MYCA1
ID RPOB_MYCA1 Reviewed; 1175 AA.
AC A0QL49;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 81.
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=MAV_4503;
OS Mycobacterium avium (strain 104).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=243243;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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=ABK68123.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000479; ABK68123.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A0QL49; -.
DR SMR; A0QL49; -.
DR PRIDE; A0QL49; -.
DR EnsemblBacteria; ABK68123; ABK68123; MAV_4503.
DR KEGG; mav:MAV_4503; -.
DR HOGENOM; CLU_000524_4_3_11; -.
DR Proteomes; UP000001574; 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..1175
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300348"
FT REGION 12..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1175 AA; 129760 MW; 5CC4B998E35D2919 CRC64;
MLEGCILADF RQSKTDRPQS SSNGSSSLNG SVPGAPNRVS FAKLREPLEV PGLLDVQIDS
FEWLIGAPRW REAAIARGDA EPKGGLEEVL DELSPIEDFS GSMSLSFSDP RFDEVKAPVD
ECKDKDMTYA APLFVTAEFI NNNTGEIKSQ TVFMGDFPMM TEKGTFIING TERVVVSQLV
RSPGVYFDET IDKSTEKTLH SVKVIPSRGA WLEFDVDKRD TVGVRIDRKR RQPVTVLLKA
LGWTNEQITE RFGFSEIMMS TLEKDNTAGT DEALLDIYRK LRPGEPPTKE SAQTLLENLF
FKEKRYDLAR VGRYKVNKKL GLHAGEPITS STLTEEDVVA TIEYLVRLHE GQPTMTVPGG
IEVPVETDDI DHFGNRRLRT VGELIQNQIR VGMSRMERVV RERMTTQDVE AITPQTLINI
RPVVAAIKEF FGTSQLSQFM DQNNPLSGLT HKRRLSALGP GGLSRERAGL EVRDVHPSHY
GRMCPIETPE GPNIGLIGSL SVYARVNPFG FIETPYRKVV DGVVTDEIHY LTADEEDRHV
VAQANSPIDD KGRFAEARVL VRRKAGEVEY VPSSEVDYMD VSPRQMVSVA TAMIPFLEHD
DANRALMGAN MQRQAVPLVR SEAPLVGTGM ELRAAIDAGD VVVAEKSGVI EEVSADYITV
MADDGTRHTY RMRKFERSNH GTCANQSPIV DAGDRVEAGQ VIADGPCTEN GEMALGKNLL
VAIMPWEGHN YEDAIILSNR LVEEDVLTSI HIEEHEIDAR DTKLGAEEIT RDIPNVSDEV
LADLDERGIV RIGAEVRDGD ILVGKVTPKG ETELTPEERL LRAIFGEKAR EVRDTSLKVP
HGESGKVIGI RVFSREDDDE LPAGVNELVR VYVAQKRKIS DGDKLAGRHG NKGVIGKILP
QEDMPFLPDG TPVDIILNTH GVPRRMNIGQ ILETHLGWVA KSGWNIDGNP EWAVNLPEEL
RHAQPNQIVS TPVFDGAKEE ELAGMLSCTL PNRDGEVMVD GDGKAVLFDG RSGEPFPYPV
TVGYMYIMKL HHLVDDKIHA RSTGPYSMIT QQPLGGKAQF GGQRFGEMEC WAMQAYGAAY
TLQELLTIKS DDTVGRVKVY EAIVKGENIP EPGIPESFKV LLKELQSLCL NVEVLSSDGA
AIELREGEDE DLERAAANLG INLSRNESAS VEDLA
