ID   RPOB_CHLMU              Reviewed;        1252 AA.
AC   P56869;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 126.
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=TC_0589;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 385-754.
RC   STRAIN=MoPn;
RX   PubMed=2211507; DOI=10.1128/jb.172.10.5732-5741.1990;
RA   Engel J.N., Pollack J., Malik F., Ganem D.;
RT   "Cloning and characterization of RNA polymerase core subunits of Chlamydia
RT   trachomatis by using the polymerase chain reaction.";
RL   J. Bacteriol. 172:5732-5741(1990).
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; AE002160; AAF39421.1; -; Genomic_DNA.
DR   PIR; G81686; G81686.
DR   RefSeq; WP_010230915.1; NZ_CP027217.1.
DR   AlphaFoldDB; P56869; -.
DR   SMR; P56869; -.
DR   STRING; 243161.TC_0589; -.
DR   EnsemblBacteria; AAF39421; AAF39421; TC_0589.
DR   GeneID; 1245948; -.
DR   KEGG; cmu:TC_0589; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_1_0; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   Proteomes; UP000000800; 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; -; 2.
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..1252
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047879"
FT   CONFLICT        407
FT                   /note="C -> S (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        513..592
FT                   /note="NIGLITSLSSFAKINEFGFIETPYRVVRDGIVTDEIEYMTADVEEDCVIAQA
FT                   SAELDEYNMFKDSVCWARYKGEAFEADT -> KLTDQ (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        704..718
FT                   /note="CINQTPLCSVGDVVT -> M (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        747
FT                   /note="W -> Q (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1252 AA;  139965 MW;  81536837E31F4AD9 CRC64;
     MFKCPERVSI KKKEDILDLP NLVEVQIKSY KQFLQIGKLA EERENIGLEE VFREIFPIKS
     YNEATILEYL SYNLGVPKYS PEECIRRGIT YSVTLKVRFR LTDETGIKEE EVYMGTIPIM
     TDKGTFIING AERVVVSQVH RSPGINFEQE KHSKGNVLFS FRIIPYRGSW LEASFDINDL
     IYIHIDRKKR RRKILAMTFI RALGYSTDAD IIEEFFAVEE HSLRSEKDFV ALVGKVLADN
     VVDADSSLVY GKAGEKLSTA MLKRILDAGV QSLKIAVGAD ENHPIIKMLA KDPTDSYEAA
     LKDFYRRLRP GEPATLANAR STIMRLFFDS KRYNLGRVGR YKLNKKLGFP LDDETLSQVT
     LRKEDVIGAL KYLIRLRMGD EKTSIDDIDH LANRRVRSVG ELIQNHCRSG LARMEKIVRE
     RMNLFDFSSD TLTPGKIISA KGLVSVLKDF FSRSQLSQFM DQTNPVAELT HKRRLSALGP
     GGLNRERAGF EVRDVHSSHY GRICPIETPE GPNIGLITSL SSFAKINEFG FIETPYRVVR
     DGIVTDEIEY MTADVEEDCV IAQASAELDE YNMFKDSVCW ARYKGEAFEA DTSTVTHMDV
     SPKQLVSVVT GLIPFLEHDD ANRALMGSNM QRQAVPLLKT EAAIVGTGLE GRAAKDSGAI
     VVAQEDGVVE YVDSYEIVVA KKNNPTLKDT YPLKKFLRSN SGTCINQTPL CSVGDVVTHG
     DVLADGPATD KGELALGKNV LVAFMPWYGY NFEDAIIISE KLIKQDAYTS IYIEEFELTA
     RDTKLGKEEI TRDIPNVSEE VLANLGEDGI VRIGAEVKPG DILVGKITPK SETELAPEER
     LLRAIFGEKA ADVKDASLTV PPGTEGVVMD VKVFSRKDRL SKSDDELVEE AVHLKDLQKE
     YKSQLAQLKM EHREKLGALL LNEKAPAAII HRRSADILVQ EGAVFDQETI ELLERESLVD
     LLMAPCDMYD VLKDILSNYE TAVQRLEVNY KTEAEHIKEG DADLDHGVIR QVKVYVASKR
     KLQVGDKMAG RHGNKGVVSK IVPEADMPFL ANGETVQMIL NPLGVPSRMN LGQVLETHLG
     YAAKTAGIYV KTPVFEGFPE SRIWDMMIEQ GLPEDGKSYL FDGKTGERFD SKVVVGYIYM
     LKLSHLIADK IHARSIGPYS LVTQQPLGGK AQMGGQRFGE MEVWALEAYG VAHMLQEILT
     VKSDDVSGRT RIYESIVKGE NLLRSGTPES FNVLIKEMQG LGLDVRPMVV DA