ID   RPOB_MYCS5              Reviewed;        1202 AA.
AC   Q4A5S7;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 2.
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=MS53_0485;
OS   Mycoplasmopsis synoviae (strain 53) (Mycoplasma synoviae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=262723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=53;
RX   PubMed=16077101; DOI=10.1128/jb.187.16.5568-5577.2005;
RA   Vasconcelos A.T.R., Ferreira H.B., Bizarro C.V., Bonatto S.L.,
RA   Carvalho M.O., Pinto P.M., Almeida D.F., Almeida L.G.P., Almeida R.,
RA   Alves-Junior L., Assuncao E.N., Azevedo V.A.C., Bogo M.R., Brigido M.M.,
RA   Brocchi M., Burity H.A., Camargo A.A., Camargo S.S., Carepo M.S.,
RA   Carraro D.M., de Mattos Cascardo J.C., Castro L.A., Cavalcanti G.,
RA   Chemale G., Collevatti R.G., Cunha C.W., Dallagiovanna B., Dambros B.P.,
RA   Dellagostin O.A., Falcao C., Fantinatti-Garboggini F., Felipe M.S.S.,
RA   Fiorentin L., Franco G.R., Freitas N.S.A., Frias D., Grangeiro T.B.,
RA   Grisard E.C., Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A.,
RA   Laurino J.P., Lima L.F.A., Lopes M.I., Loreto E.L.S., Madeira H.M.F.,
RA   Manfio G.P., Maranhao A.Q., Martinkovics C.T., Medeiros S.R.B.,
RA   Moreira M.A.M., Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C.,
RA   Paixao R.F.C., Pedrosa F.O., Pena S.D.J., Pereira M., Pereira-Ferrari L.,
RA   Piffer I., Pinto L.S., Potrich D.P., Salim A.C.M., Santos F.R., Schmitt R.,
RA   Schneider M.P.C., Schrank A., Schrank I.S., Schuck A.F., Seuanez H.N.,
RA   Silva D.W., Silva R., Silva S.C., Soares C.M.A., Souza K.R.L., Souza R.C.,
RA   Staats C.C., Steffens M.B.R., Teixeira S.M.R., Urmenyi T.P.,
RA   Vainstein M.H., Zuccherato L.W., Simpson A.J.G., Zaha A.;
RT   "Swine and poultry pathogens: the complete genome sequences of two strains
RT   of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae.";
RL   J. Bacteriol. 187:5568-5577(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; AE017245; AAZ43894.2; -; Genomic_DNA.
DR   RefSeq; WP_041352028.1; NC_007294.1.
DR   AlphaFoldDB; Q4A5S7; -.
DR   SMR; Q4A5S7; -.
DR   STRING; 262723.MS53_0485; -.
DR   PRIDE; Q4A5S7; -.
DR   EnsemblBacteria; AAZ43894; AAZ43894; MS53_0485.
DR   KEGG; msy:MS53_0485; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_1_14; -.
DR   OMA; FMTWEGY; -.
DR   Proteomes; UP000000549; 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; -; 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   PROSITE; PS01166; RNA_POL_BETA; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..1202
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000224080"
SQ   SEQUENCE   1202 AA;  135228 MW;  CE444DE9E4BE9DC8 CRC64;
     MQKDKKNYKL RKFGPITERR DYSITKHSLP VGDILATSKK SYQDFINKKI EELLNEIYPI
     EASNKEASLE YEKKSVKFEL PFKKAEHENL QIKTCKAKKT NFSMKVYITL KKVVSQTGVV
     KKEKILLGEI PYITSSGSFI INGSEKVIVS QLIRSPGAYF GVSVRNKQSE DLFNKLEILP
     RIGSWIEVSH KVTSANLDAI KIKIDKNKNI NIVTFLASFG LLADDIRYLF GKNEVLEETI
     RKNKTIDITE FSRQEIMDLC QEKIFRIIRK GDRISEESKR SLLSGMLFDK KRYNLSKTGR
     YMLNNKLSLV ERITNTYLAQ KVVSHLGNTF DVGTYVTYEI AKEIQESFEA KAKDNKSNLH
     LEKIPNINPD DVYYKINKDN KSLNKRINIA RIKIWPTKRA MDANETPSEV IGNDPKATEE
     HLLLSDIIAA ISYYLNLTVG IGQDDDPDSL MNKRIVSVGE LLEGELRIAL LKLEKATRER
     MGAKEPDKIT AKNVTNNKLI TNQMKTFFNT SKLAQFMDQI NPLAEISNKR RVTSLGPGGL
     NRDTAQFEVR DVHSTHYGRI CPIETPEGPN IGLILNYAIY STVNELGFLQ TPYYKVNDGV
     VDYNDVRYLT SYEEIGYAFA QSSVHVNDKN EIIDEQITIK KDYNYIIGSP KDIDFLEVSS
     KQIVSVAAAA IPFLENNDAN RALMGSNMQR QAVPLIEAEA PLVATGIEAD IAKFSSYNIV
     ANNDGEVIYV DGTKIQVRTA KKIDTYNLKN FEKSNQGTII QQKPIVKVGD HVKEGDLLVD
     GSSFKDGEMA LGKNLLVGFT TWNGYNFEDA IIINERLVKD DVLTSIYIEE QTIQFRISKS
     SEDIMTRDIP NVSKYSMRNL DEFGIIKVGS EVVAGDVLVG RISPKGEENP SQEEKLLNAI
     FNQRPQNYKD TSLKVKNGHN GTVIHVEVLS RENGDILEDG LDSIIKVYIA QKRKIKVGDK
     MAGRHGNKGV ISIILPEEDM PHLEDGTPLD IMLNPQGVPS RMNIGQVLEM HLGMAAKKLG
     TKFVTPSFDG IKKETIEDLL QEANLDKSGK QVVIDPITGE KFDNPISVGV IYMLKLNHMV
     DDKMHARSVG PYSLITQQPL GGKSQNGGQR FGEMETWALE SYGASNILQE ILTYKSDDIY
     SRNLVYKALV NDSAIPNPGM PESFNVLSNE LKGLLMKLGI TETESNSDEL IQHFDHLGVE
     HE