ID   RPOB_PARUW              Reviewed;        1254 AA.
AC   Q6MDM1;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=pc0604;
OS   Protochlamydia amoebophila (strain UWE25).
OC   Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae;
OC   Candidatus Protochlamydia.
OX   NCBI_TaxID=264201;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UWE25;
RX   PubMed=15073324; DOI=10.1126/science.1096330;
RA   Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA   Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA   Mewes H.-W., Wagner M.;
RT   "Illuminating the evolutionary history of chlamydiae.";
RL   Science 304:728-730(2004).
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; BX908798; CAF23328.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6MDM1; -.
DR   SMR; Q6MDM1; -.
DR   STRING; 264201.pc0604; -.
DR   PRIDE; Q6MDM1; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_1_0; -.
DR   OMA; FMTWEGY; -.
DR   Proteomes; UP000000529; 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; 2.40.270.10; -; 2.
DR   Gene3D; 2.40.50.150; -; 1.
DR   HAMAP; MF_01321; RNApol_bact_RpoB; 1.
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; 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; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..1254
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000224087"
SQ   SEQUENCE   1254 AA;  140972 MW;  8D3331B7243755E6 CRC64;
     MLQRPPHRES FNDKEEIIDL PNLIEIQIKS YNQFLQADKF PDERENIGLQ EVFTEIFPIK
     SYDEKTILEF LSYNLGVPKY NPEECIRRGI TYNVTLKVKF RLTDETGIKE EEVYMGTIPV
     MTDKGTFIVN GAERVVVSQL HRSPGICFEQ ERHSRGNVIY SFRIIPYRGS WLEGAFDTND
     LIHIYIDRKK RRRKILATTF IRALGYSSNS DIIEEFFTTR KYKIKNEKEF AKLVGKILAQ
     DVVDEESGLV FGKASEKLTT AMLKRIVDAG IDVIRIAEDA DETSPVIKML AKDPTDSYES
     ALKDFYRKIR PGEPATLSNA RSAIMRLFFD PKRYNLGRVG RYKLNSKLGC EINDEKLQTV
     TLDKEDVIGA LKYLIMLKSG SEEASIDDID HLGNRRVRSV GELIQNQCRI GLARMEKIIR
     ERMNLFDFSS DTLTPGKIVS AKGLSGVLKD FFGRSQLSQF MDQTNPIAEL THKRRLSSLG
     PGGLNRDRAG FEVRDVHTSH YGRICPIETP EGPNIGLISS LSSFAKINEF GFIETPYRIV
     REGVVTDEIE YMTADQEEQC VIAQASAPLD EYHMFAEPIC WARYKGEQFE TDTKNVTHMD
     VSPKQLVSIV TGLIPFLEHD DANRALMGSN MQRQGVPLLK PTAPIVGTGL EARAARDSGA
     VLIAHEDGVV DYVDGLKIVI SPDDNRLEKR TYLLKKFIRS NAGTCINQRP LCHVGDKIKA
     GDVIADGPAT DKGEVALGRN VLVAFMPWFG YNYEDAIIIS EKLLREDYYT SLYIEEFELT
     ARDTKLGKEE ITRDIPNVSE ETLRNLNDDG IIRIGAEVKP GDTLVGKITP KSETELAPEE
     RLLRAIFGDK ASDVKDASLI APPGTEGVVM DVKVFSRRDR LSKTDDELVE EASKLKDIQR
     EYKSNQAQLR TEKHERVGAL LLNETAPGNI VHRRTAEIIV DEGDLITQDL IEALEKESVE
     DLLMPENDIY TTLRQILHDY EIALQTVETQ YKTQLEFMRK GDTDLDPGVI RQVKVYVASK
     RKLQVGDKMA GRHGNKGVVS KIVPEADMPF LSTGQTIEII LNPLGVPSRM NMGQLFETHL
     GIAAKHTGIT VKSPVFEGFP EEKIWEMMKK AGLPEDGKFF LYDGCSGERF DNSVVVGYIY
     MLKLSHLVAD KIHARAVGPY SLVTQQPLGG KAQMGGQRFG EMEVWAAEAY GAAHLLQEML
     TVKSDDVAGR TRIYESIVKG ENLLKSGTPE SFNVLIKEMQ GLGLNVYTEA VDDS