ID   RPOB_HYDCU              Reviewed;        1352 AA.
AC   Q31IY9;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=Tcr_0288;
OS   Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira
OS   crunogena).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Hydrogenovibrio.
OX   NCBI_TaxID=317025;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25203 / XCL-2;
RX   PubMed=17105352; DOI=10.1371/journal.pbio.0040383;
RA   Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., Blake R.A.,
RA   Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., Detter C., Do K.F.,
RA   Dobrinski K.P., Faza B.I., Fitzpatrick K.A., Freyermuth S.K., Harmer T.L.,
RA   Hauser L.J., Huegler M., Kerfeld C.A., Klotz M.G., Kong W.W., Land M.,
RA   Lapidus A., Larimer F.W., Longo D.L., Lucas S., Malfatti S.A., Massey S.E.,
RA   Martin D.D., McCuddin Z., Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H.,
RA   Paulsen I.T., Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P.,
RA   Tinkham L.E., Zeruth G.T.;
RT   "The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena
RT   XCL-2.";
RL   PLoS Biol. 4:1-17(2006).
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; CP000109; ABB40884.1; -; Genomic_DNA.
DR   RefSeq; WP_011369710.1; NC_007520.2.
DR   AlphaFoldDB; Q31IY9; -.
DR   SMR; Q31IY9; -.
DR   STRING; 317025.Tcr_0288; -.
DR   PRIDE; Q31IY9; -.
DR   EnsemblBacteria; ABB40884; ABB40884; Tcr_0288.
DR   KEGG; tcx:Tcr_0288; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_0_6; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
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; 2.
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..1352
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000237322"
SQ   SEQUENCE   1352 AA;  150208 MW;  E1570368298CDA53 CRC64;
     MTYSLTEKKR IRKDFATRSS ILEVPYLLSL QKESFKEFLQ KDKKPLERDP IGLHSAFSSV
     FPIHGVAGTA DLEYVSYTMG QPEFDVKECK QRGVTYSSPL RVKMRLVLFD KDAPAGKRPV
     KDVKEQEVYL GDVPLMTENG TFVINGTERV IVTQLHRSPG VIFDSDKGKS HSSGKVLFNA
     RIIPYRGSWL DFEFDHNDCV FVRIDRRRKL PVSIIFRAMG YSSEEILDTF FDHTHISYKK
     GAFVMQLVPS QLKGQTAAFD IADGDKVIIK AGKKITARNI KQLQEAKVDS VVVPEEYLLG
     KVLSSGITNE ETGELVARSN EVIASDLIET MKSIKDLSFR ILFIDDLENG SYISDTLNLD
     TTTSQLEAQI EIYRMMRPGE PPTKESSEAL FNSLFFDEAR YDLSSVGRMK LNRRLGRKDN
     EGSLVLENQD VVDVVKELLN IRNGLSTIDD IDTLGNRRIR AVGEMAENAF RVGLVRVERA
     VKERLNQAET DGLLPQDLIN AKPVSAAIKE FFGSSQLSQF MDQVNPLSEV THKRRVSALG
     PGGLTRERAG FEVRDVHPTH YGRVCPIETP EGPNIGLINT LAIYAKTNKY GFLETPYRKV
     IDGQVTEEVE YVSAIDEAQF VIAQASAAMD SDNKLLDELV TARHKNETIL ASSQDIDYMD
     VSPKQIVSVA ASLIPFLEHD DANRALMGSN MQRQAVPTLR ADKPLVGTGI EKTVAIDSGV
     TVIALRGGEI VSSDSARIVV RANQEEIAEG ETGVDIYNLI KYQRSNQNTC INQKPIVKAG
     DVVSRGDVLA DGPSTDLGEL AIGQNMRIAF MPWNGYNFED SILVSERVVQ EDRYTTIHIE
     ELTCLARDTK LGPEEVTSDI PNVGEAALSR LDESGIVYVG AEVKQGDILV GKVTPKGETQ
     LTPEEKLLRA IFGEKASDVK DTSLRVSKGV EGTVIDVQVF TREGVKKDAR ALAIQEDELQ
     KVRKDIDEQY KILEEDTIDR IQPMLIGQKL VDGTEITADF LASQDSSKWF GLNVADDALS
     SHLESLEKQL VAKKEELNGV FEEKKKKLTQ GDDLQPGVSK MVKVYVAVKR RIQPGDKMAG
     RHGNKGVISR ICPVEDMPYD ETGRPVDICL NPLGVPSRMN VGQILETHLG LAAEGLGAKI
     NAMLEQQADI KELKSFLHKI YNETQGQKVD FDSLTDAEII ELAGNLRKGV PMASPVFDGA
     SEDEIKALLR LADLPESGQM KLYDGISGEE FDRPVTVGYM YYLKLNHLVD DKMHARSTGP
     YSLVTQQPLG GKAQFGGQRF GEMEVWALEA YGAAFTLQEM LTVKSDDLNG RTRMYKNIVD
     GNEYMEPGIP ESFSVLRKEI RALGIDIELE QE