ID   RPOB_NEORS              Reviewed;        1363 AA.
AC   Q93MK8;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 79.
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};
OS   Neorickettsia risticii (Ehrlichia risticii).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Neorickettsia.
OX   NCBI_TaxID=950;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC VR-986 / Illinois;
RX   PubMed=12710612; DOI=10.1099/ijs.0.02411-0;
RA   Taillardat-Bisch A.V., Raoult D., Drancourt M.;
RT   "RNA polymerase beta-subunit-based phylogeny of Ehrlichia spp., Anaplasma
RT   spp., Neorickettsia spp. and Wolbachia pipientis.";
RL   Int. J. Syst. Evol. Microbiol. 53:455-458(2003).
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; AF401089; AAK83925.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q93MK8; -.
DR   SMR; Q93MK8; -.
DR   PRIDE; Q93MK8; -.
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; -; 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; 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..1363
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047896"
SQ   SEQUENCE   1363 AA;  152512 MW;  9B217508CFB9BCA3 CRC64;
     MSEFHRLYFD ELLFDFPDLV KVQKDSYASF VGGGDAVSSI NDIFASVFPV NDGYGRASLE
     FVSCRMGEPK HDEYGCVERG ITYSAPLRAI LRLVVFGDET SGEGGEGVST EPAVKDVREQ
     EIYMGDIPIM SKNGTFIING VERVVVSQMH RAPGVFFDND KARSISGKLN YIARIIPYRG
     SWLDFEFDAK DVLYFRIDKK RKLPVTLLLR ALGLSNKDIF AQFCEVSECR LTKDGKWTVC
     FVPERFKGVR LQYDLINAET GELVLAKGNR ISIVLARNLY AKGLRYCYMD LEVMKDMYLA
     DDLVSAKGEV LLPHGTRLTK EHVAKLEFLD VDSIKLVELK GNYIFSTVLQ YDCSYEEAML
     SIYRVIRPGE IPSIESAEKL FESLFFSPER YDLLNVGRIR LNAKFNLSHD ESLTVLTKED
     IFCTVRELAL LQREVGDVDD IDHLGNSALG LRRVRSVGEF MDNQFRIGLV RMAKVIVENM
     ATADFDTVMP CEMINSKILG AVIREFFMSS ALSQFMDQTN PLSEITHKRR ISALGPGGLN
     RGRAGFEVRD VHTTHYGRIC ATETPEGATI GLINSLAIYA KINKYGFIET PYRYVRDGRV
     TDEVTYLSAI DEIKANICQA SVRVDEEGYI LDDLVYCRRN YENVFIPRSE VQFADVSAKQ
     IVSVAASLIP FLENDDANRA LMGSNMQRQA VPLIVPEAPL VGTGMEGYVA RGSGAVIVAK
     RAGIVQYIDA RNIVVASESK DDFWIDSYTL CKFRKSNHNT CIHQRCVVYQ GQRVKKGDIL
     ADGPAIQQGE LALGRNLVVA FLSWRGYNFE DSVVISSNVV RDDLFTSVHL EGFECVVRDT
     RLGPEEITRD VSGVAEEFLH CLDEFGIACV GANVEAGDVL VGKVTPKSSS PVTPEEKLLR
     AIFGEKAIDV KDSSLYLPPG VSGCVVDVKV LQRRGIEKVG RALLIEKQAI DAEKARRDHE
     LAVLTNYIYS LLKEMLVGKV ALNTLAPISK GDLITGEALE KIDRESWWKL SVDEISSIKL
     LRQRFVDRFD EINKTYEENF EKIRGDDDLA QGVLMVVKVF VAVKHTLQPG DKMSGRHGNK
     GVISRIVPAE DMPYLADGTP VDIILNPLGV PSRMNVGQIL ETHLGWAAYN LGKKISKLLD
     EGNYSEVKSL ILEIYKNDRK MMARLKRMTD TEIVEYSRSL RRGVPVAASV FEGPKTDEIE
     RLLVLAGKDP SGQEVLYDGV TGEKFDRKVT VGCKYMLKLH HLVNDKIHAR SIGSYSLITQ
     QPLGGKSHFG GQRFGEMECW ALQAYGATFA LQEMLTIKSD DVVGRVNVYD SIVRGDNDFY
     YGVPESFNVM MNELRALCLN VEFCSDLERK EDFSDLPLAV SGR