ID   RPOB_SPICI              Reviewed;        1302 AA.
AC   P47767;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 91.
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   Spiroplasma citri.
OC   Bacteria; Tenericutes; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC   Spiroplasma.
OX   NCBI_TaxID=2133;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=R8A2HP;
RX   PubMed=8675039; DOI=10.1016/0378-1119(96)00071-6;
RA   Laigret F., Gaurivaud P., Bove J.;
RT   "The unique organization of the rpoB region of Spiroplasma citri: a
RT   restriction and modification system gene is adjacent to rpoB.";
RL   Gene 171:95-98(1996).
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; U25815; AAC44217.1; -; Genomic_DNA.
DR   PIR; T43230; T43230.
DR   AlphaFoldDB; P47767; -.
DR   SMR; P47767; -.
DR   STRING; 2133.SCITRI_0093; -.
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..1302
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047957"
SQ   SEQUENCE   1302 AA;  146534 MW;  8D971C23EB9FEB2F CRC64;
     MALKEKEFGH YAKRIDYTKV SGNLDLPNLI EIQTETYDWF KKTGISEVFR EVFPIVGHEG
     NIVLEMLDWE FREPRRTISQ AKDESKIFEA PIYSNLKLTI NSKDVEVEKA IVKGEPELIK
     AWIEERVGHM ITILKKTTDV IYYDIHSGDE IATCTVTIKE RLDDKLIVDI TIEKEGEVFF
     GDFPLMTGKG TFIVNGSEKV VVSQLVRSPG AYYKIDLNRK NGENVYYVDL IPSRGTWLEF
     ESDHKKIKVG KEEKFENVFY VKIDKSRKVS VANFLTALGI IKEDALDIFG DNKLVKSTYE
     LDPYTGDILY DQSIAVQEIY KKIRSGETAT PDGATKYLYG LLFDKRKYDL TKAGRFKLIQ
     KLSVENRIYN KILAEDIKDV NGKVVFTEGT LMDKEAINKL KGILKAGACL QEVKFSDEII
     CSNKIQKIKV YVDNEVRSRV ANIIGIDPNA TDEYVTVPDV LATFSYLLNL TDGIGEVDDI
     DHLGNRRVRT IGELLQNQFR IGLLRIEKNV KEKMSTSNLF KMKPSNIINN KPLSAIIGEF
     FNLSQLSQFM DQTNPLAELT NKRRLTALGP GGLSRERAGL EVRDVHYSHY GRICPIETPE
     GPNIGLINNL ATYAKINSYG FIETPYRRVI GCKVTMENDY LTADEEKNYV VAQANIRLSD
     KGEILDEQVV ARFQGENIIA GRNDVDYVDV SPKQIVSIAT SCIPFLENDD ANRALMGANM
     QRQAIPLIAP NSPYVGTGVE YAAARDSGLA IVSQYDGIVD FVDATRIVLK TKEGLKNYNL
     DTFVRSNQGT SLTHVPLVRQ GQKVEKGQVL ADGPSIDKGE LALGQNVVVA FTTWNGYNYE
     DAIIVSERLV SEDVFTSIHI EEYTIERRQT KQGPEEITRE IPNISENARK FLDDDGLVII
     GTEVKPGDIL VGKVTPKGQT QLSPEDKLLQ AIFGEKSKNV KDNSLRVPNG GEGIIQAIKR
     FPREKYEVSA DVLEVIKIYI VQKRKIQEGD KMAGRHGNKG VISKILPLED MPHMEDGTPV
     DIMLNPLGVP SRMNIGQVLE IHLGMAAKKL GQKISTPVFD GMINEELIEI MDKAGMKNFG
     KEVLIDGRTG EKFDNPVSVG VMYMLKLSHM VDDKLHARNV GPYSLITQQP LGGKAQNGGQ
     RFGEMEVWAL EAYGAAHTLR EILTIKSDDI KGRTRAYESI VKDKKIPEPG IPESFNVLTR
     EIQGLGFNIH MIDEKGNIKN IKSYDEADYV DEDLLTDCDE FEDEFDIDNF ILSTNREPQK
     KEHLEDFVKV EDSFDLVDNL DDNELDDIDN EIDEINDQDE LS