ID   RPOB_MYCSM              Reviewed;        1169 AA.
AC   Q50388;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 99.
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};
OS   Mycolicibacterium smegmatis (Mycobacterium smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 14468 / DSM 43277 / NCIB 9953 / NCTC 10265 / W-113;
RX   PubMed=8540740; DOI=10.1128/aac.39.9.2164;
RA   Hetherington S.V., Watson A.S., Patrick C.C.;
RT   "Sequence and analysis of the rpoB gene of Mycobacterium smegmatis.";
RL   Antimicrob. Agents Chemother. 39:2164-2166(1995).
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   ---------------------------------------------------------------------------
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; U24494; AAA91426.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q50388; -.
DR   SMR; Q50388; -.
DR   STRING; 710686.Mycsm_00960; -.
DR   PRIDE; Q50388; -.
DR   eggNOG; COG0085; Bacteria.
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..1169
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047925"
SQ   SEQUENCE   1169 AA;  128942 MW;  517E5563599DE82E CRC64;
     MLEGCILAVS SQSKSNAITN NSVRGAPNGV SFAKLREPLE VRGLLDVQTD SFEWLVGSRR
     VRQAAIDRGE ENPVGGLEEV LAELSPIEDF SGSMSLSFSD PRFDEVKASV DECKDKDMTY
     AAPLFVTAEF INNNTGEIKS QTVFMGDFPM MTEKGTFIIN GTERVVVSQL VRSPGVYFDE
     TIDKSTEKTL HSVKVIPGRG AWLEFDVDKR DTVGVRIDRK RRQPVTVLLK ALGWTNEQIV
     ERFGFSEIMM GTLEKDTTSG TDEALLDIYR KLRPGEPPTK ESAQTLLENL FFKEKRYDLA
     RVGRYKVNKK LGLNAGKPIT SSTLTEEDVV ATIEYLVRLH EGQTSMTVPG GVEFAVESHD
     IDHFGNRRLR TVGELIQNQI RVRLSRMERV VRERMTTQDV EAITPQTLIN IRPVVAAIKE
     FFGTSQLSQF MDQNNPLSGL THKRRLSALG PGGLSRERAG LEVRDVHPSH YGRMCPIETP
     EGPNIGLIGS LSVYARVNPF GFIETPYRKV VEGVVTDQID YLTADEEDRH VVAQANSPTD
     ENGRFTEDRV MVRKKGGEVE FVSADQVDYM DVSPRQMVSV ATAMIPFLEH DDANRALMGA
     NMQRQAVPLV RSEAPLVGTG MELRAAIDAV TWSSHKTGVI EEVSADYITV MADDGTRQSY
     RLRKFARSNH GTCANQRPIV DAGQRVEAGQ VIADGPCTQN GEMALGKNLL VAIMPWEGHN
     YEDAIILSNR LVEEDVLTSI HIEEHEIDAR DTKLGAEEIT RVIPKLSDEV LADLDEPRIV
     RIGAEVRDGE ILVGKVTPKG ETELTPEERL LRAIFGEKAR EVRDTSLKVP HGESGKVIGI
     RVFSREDDDE LPVGVNELVR VYVAQKRKIS DGDKLARRHG NKGVIGKILP VEDMPFLPDG
     TPVDIILNTH GCRVVLNIGQ ILETHLGWGA KAGWNIDVLA GVPDWASKLP EELYSAPADS
     TVATPVFDGA QEGELAGLLG STLPNRDGEV MVNADGKATL FDGRSSGEPF PYPVTVGYMY
     ILKLHHLVDD KIHARSTGPY SMITQQPLGG KAQFGGQRFG EMECWAMQAY GAAYTLQELL
     TIKSDDTVGR VKVYEAIVKG ENIPEPGIPE SFKVLLKELQ SLCLNVEVLS SDGRAIEMRD
     GDDEDLERAA ANLGINLSRN ESASVEDLA