ID   RPOB_PETMO              Reviewed;        1187 AA.
AC   A9BF33;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Pmob_0355;
OS   Petrotoga mobilis (strain DSM 10674 / SJ95).
OC   Bacteria; Thermotogae; Petrotogales; Petrotogaceae; Petrotoga.
OX   NCBI_TaxID=403833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10674 / SJ95;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Noll K., Richardson P.;
RT   "Complete sequence of Petroga mobilis SJ95.";
RL   Submitted (NOV-2007) 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}.
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DR   EMBL; CP000879; ABX31097.1; -; Genomic_DNA.
DR   RefSeq; WP_012208204.1; NC_010003.1.
DR   AlphaFoldDB; A9BF33; -.
DR   SMR; A9BF33; -.
DR   STRING; 403833.Pmob_0355; -.
DR   PRIDE; A9BF33; -.
DR   EnsemblBacteria; ABX31097; ABX31097; Pmob_0355.
DR   KEGG; pmo:Pmob_0355; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_3_0; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   Proteomes; UP000000789; 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   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; 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; 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..1187
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000329185"
SQ   SEQUENCE   1187 AA;  134956 MW;  A48214DDE5AC86A8 CRC64;
     MNTVVREVGR RERKFFGKVP EKTEIYEDLV KIQKDSFRDF LDKKIMESIK RYMPIKIPVK
     ASGKKNKEFL IDFVDVKFED SSFSENECRD KGLTYAGKAY LKVRITDSAT GEMIEKDDIF
     LCNIPYMTER GIFIVNGAER VIVNQLVRSP GVYFIKEEET DTSKEMFIAH FLPIKGAWLE
     ILYNPNPGKE VLQVRIDRKR KFNFFLFLRA LGYENDLDIL RLFPKEIDLD DEVELSNYNN
     CTVLSDLSFQ ELDDMDPPRK STYGMKLYEV LELLKKYEIK SVTVAHLVAE ITLEKMKKRY
     EKEERLTSLE AYKEIFSKLK PTEIPRAQKA KEEIEDMYFN PEKFDFSQIG RQKIQVKLRK
     AYIDYLREVE KKDISEDMED KIKYPIKTFA VDKLDIILSA RYLLHVKENI EGLDTRDHLG
     NKRVRSVGEL MQIEFERAFS KMIQHAPEKL AGVQSINKIS PQSLINSRSI MTAFHQFFAS
     SQLSQFLDQV NPLAELTHKR RLSAIGPGGL KREHAKFEVR DVHHSHYGRM CPIETPEGAN
     IGLITSMAIL AKVDEYGFLK TPYYRVKHAK VDLNNIVYLS ADEEELYRIA PASAEIGEDG
     SLVEEYIEAR YLGKVSLFHK DEIEYISVTP KQIASVSAAL IPFLEHDDAN RALMGSNMQR
     QAVPLLRPQA PFVGTGVEWL AARDSGYLIM AKHKGIVDYV DGRKIVITRL DEENNVLKDS
     NDEPLKDEYT LLKYVRSNQD MCINQVPIVN VGDVVTKGQA IADGPSMDMG ELALGRNIFI
     GFLPWEGYNF EDAIVVSQEL LENDAFTSIH IEVFETKAMD TQLGPEEITA DIPNVKKELL
     RNLDEEGIVK IGSYVSSGDI LVGKVTPRGE SDTTPEEKLI KSVFGDKGRD IKDSSLTVPH
     GIEGRVIDVQ IFDRKDIPSL EIGVNKYVKV FIATKKTLQV GDKLAGRHGN KGVISTILNK
     EDMPFLPDGT PLQMLLSPLG VPSRMNIGQV LELHLGWLSM LTNDYYATPI FDGATESEIM
     DELSKVREEH ELYLGDDPDQ PNGKIVLRDG RTGEPFDFPV AVGSMYMLKL SHIAKDKIHA
     RSTGPYSLIH QQPLGGKAHF GGQRFGEMEV WALEAHGAAH TLNEMLTYKS DDIKGRNEVY
     KAILKGENLP EPGIPESFKV LTKELQGLML DIKLYDEDGN ELDVDRL