RPOB_CHLFF
ID RPOB_CHLFF Reviewed; 1252 AA.
AC Q255E6;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, 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=CF0320;
OS Chlamydia felis (strain Fe/C-56) (Chlamydophila felis).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=264202;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fe/C-56;
RX PubMed=16766509; DOI=10.1093/dnares/dsi027;
RA Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H.,
RA Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., Fukushi H.,
RA Hattori M., Kuhara S., Shirai M.;
RT "Genome sequence of the cat pathogen, Chlamydophila felis.";
RL DNA Res. 13:15-23(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; AP006861; BAE81092.1; -; Genomic_DNA.
DR RefSeq; WP_011457872.1; NC_007899.1.
DR AlphaFoldDB; Q255E6; -.
DR SMR; Q255E6; -.
DR STRING; 264202.CF0320; -.
DR PRIDE; Q255E6; -.
DR KEGG; cfe:CF0320; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_0; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000001260; 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_0000300297"
SQ SEQUENCE 1252 AA; 140346 MW; 8ECCF64157D73154 CRC64;
MFKCPERVSV KKKEDILDLP NLIEIQIKSY KQFLQIGKLA EERDNVGLEE VFREIFPIKS
YNEATILEYL SYNLGVPKYS PEECIRRGIT YSVTLKVRFR LTDETGIKEE EVYMGTIPIM
TDKGTFIING AERVVVSQVH RSPGINFEQE KHSKGNILFS FRIIPYRGSW LEAIFDINDL
IYIHIDRKKR RRKILAMTFI RALGYSSDAD IIEEFFQIEE CSLKSEKDFS VLVGKILADN
VLDEASSLVY GKAGEKLSTA MLKRMLDADI STLKIALEAD ENHPIIKMLA KDPTDSYEAA
LKDFYRRLRP GEPATLANAR STIMRLFFDP KRYNLGRVGR YKLNRKLGFP MDEESLSQVT
LRKEDVIGAL KYLIRLKMGD EKASIDDIDH LANRRVRSVG ELIQNQCRSG LARMEKIVRE
RMNLFDFSSD TLIPGKIISA KGLTSVLKDF FGRSQLSQFM DQTNPVAELT HKRRLSALGP
GGLNRERAGF EVRDVHASHY GRICPIETPE GPNIGLITSL SSFAKINEFG FIETPYRIVR
DGVVTDEIEY MTADVEEECV IAQASANLDE YNMFTDPVCW ARYRGEAFEA DTSTVTHMDV
SPKQLVSIVT GLIPFLEHDD ANRALMGSNM QRQAVPLLKT EAPIVGTGLE ARAAKDSGAI
VVAEEDGVVE YVDGYKVVVA AKHNPTLKRT YEFKKFLRSN SGTCINQRPL CSVGDIVVKG
DVIADGPATD QGELALGKNI LVAFMPWYGY NFEDAVIISE KLIKQDAYTS IYIEEFELTA
RDTKLGKEEI TRDIPNVSEE VLANLGEDGI IRIGAEVKPG DILVGKITPK SETELAPEER
LLRAIFGEKA ADVKDASLTV PPGTEGVVMD VKVFSRKDRL SKSDDELVEE AVHLKDLQKG
YKNQISVLKT EYREKLGALL LNEKAPASII HRRTADILVQ EGTVFDQETI ELLEQESLVD
LLMPPCDMYD VLKNLLSDYE TSLQRLEVNY KTEVEHIREG DADLDHGVIR QVKVYVASKR
KLQVGDKMAG RHGNKGVVSK IVPEADMPYL ANGETIQMIL NPLGVPSRMN LGQVLETHLG
YAAKTAGIHV KTPVFEGFPE SRIWDMMIEQ GLPADGKSYL YDGKTGERFD NTVVIGYIYM
LKLSHLIADK IHARSIGPYS LVTQQPLGGK AQMGGQRFGE MEVWALEAYG VAHMLQEILT
VKSDDVSGRT RIYESIVKGE NLLKSGTPES FNVLIKEMQG LGLDVRPMVV DA
