ID   RPOB_CHLTA              Reviewed;        1252 AA.
AC   Q3KM47;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=CTA_0337;
OS   Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=315277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-571B / DSM 19440 / HAR-13;
RX   PubMed=16177312; DOI=10.1128/iai.73.10.6407-6418.2005;
RA   Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT   "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT   genitotropic strains.";
RL   Infect. Immun. 73:6407-6418(2005).
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; CP000051; AAX50575.1; -; Genomic_DNA.
DR   RefSeq; WP_011324678.1; NC_007429.1.
DR   AlphaFoldDB; Q3KM47; -.
DR   SMR; Q3KM47; -.
DR   EnsemblBacteria; AAX50575; AAX50575; CTA_0337.
DR   KEGG; cta:CTA_0337; -.
DR   HOGENOM; CLU_000524_4_1_0; -.
DR   OMA; FMTWEGY; -.
DR   Proteomes; UP000002532; 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; -; 3.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 2.
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_0000224043"
SQ   SEQUENCE   1252 AA;  140158 MW;  4B91FD4F509464FC CRC64;
     MFKCPERVSI KKKEDILDLP NLVEVQIKSY KQFLQIGKLA EERENIGLEE VFREIFPIKS
     YNEATILEYL SYNLGVPKYS PEECIRRGIT YSVTLKVRFR LTDETGIKEE EVYMGTIPIM
     TDKGTFIING AERVVVSQVH RSPGINFEQE KHSKGNVLFS FRIIPYRGSW LEAVFDINDL
     IYIHIDRKKR RRKILAMTFI RALGYSTDAD IIEEFFSVEE RSLRLEKDFV ALVGKVLADN
     VVDADSSLVY GKAGEKLSTA MLKRILDAGV QSLKIAVGAD ENHPIIKMLT KDPTDSYEAA
     LKDFYRRLRP GEPATLVNAR STIMRLFFDA KRYNLGRVGR YKLNKKLGFP LDDETLSQVT
     LRKEDVIGAL KYLIRLRMGD EKTSIDDIDH LANRRVRSVG ELIQNHCRSG LARMEKIVRE
     RMNLFDFSSD TLTPGKIISA KGLVSVLKDF FSRSQLSQFM DQTNPVAELT HKRRLSALGP
     GGLNRERAGF EVRDVHASHY GRICPIETPE GPNIGLITSL SSFAKINEFG FIETPYRVVR
     DGIVTDEIEY MTADVEEECV IAQASAELDE YNMFKTPVCW ARYKGEAFEA DTSTVTHMDV
     SPKQLVSVVT GLIPFLEHDD ANRALMGSNM QRQAVPLLKT EAAIVGTGLE GRAAKDSGAI
     IVAQEDGVVE YVDSYEIVVA KKNNPTLKDR YQLKKFLRSN SGTCINQTPL CSVGDVVTHG
     DVLADGPATD KGELALGKNV LVAFMPWYGY NFEDAIIISE RLIKQDAYTS IYIEEFELTA
     RDTKLGKEEI TRDIPNVSEE VLANLGEDGI VRIGAEVKPG DILVGKITPK SETELAPEER
     LLRAIFGEKA ADVKDASLTV PPGTEGVVMD VKVFSRKDRL SKSDDELVEE AVHLKDLQKE
     YKSQLAQLKV EHREKLGALL LNEKAPAAII HRRSADILVQ EGAIFDQETI ELLERESLVD
     LLMAPCDMYD VLKDILSSYE 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