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RPOB_LEIXX
ID   RPOB_LEIXX              Reviewed;        1165 AA.
AC   Q6ACX5;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=Lxx20640;
OS   Leifsonia xyli subsp. xyli (strain CTCB07).
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Leifsonia.
OX   NCBI_TaxID=281090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CTCB07;
RX   PubMed=15305603; DOI=10.1094/mpmi.2004.17.8.827;
RA   Monteiro-Vitorello C.B., Camargo L.E.A., Van Sluys M.A., Kitajima J.P.,
RA   Truffi D., do Amaral A.M., Harakava R., de Oliveira J.C.F., Wood D.,
RA   de Oliveira M.C., Miyaki C.Y., Takita M.A., da Silva A.C.R., Furlan L.R.,
RA   Carraro D.M., Camarotte G., Almeida N.F. Jr., Carrer H., Coutinho L.L.,
RA   El-Dorry H.A., Ferro M.I.T., Gagliardi P.R., Giglioti E., Goldman M.H.S.,
RA   Goldman G.H., Kimura E.T., Ferro E.S., Kuramae E.E., Lemos E.G.M.,
RA   Lemos M.V.F., Mauro S.M.Z., Machado M.A., Marino C.L., Menck C.F.,
RA   Nunes L.R., Oliveira R.C., Pereira G.G., Siqueira W., de Souza A.A.,
RA   Tsai S.M., Zanca A.S., Simpson A.J.G., Brumbley S.M., Setubal J.C.;
RT   "The genome sequence of the Gram-positive sugarcane pathogen Leifsonia xyli
RT   subsp. xyli.";
RL   Mol. Plant Microbe Interact. 17:827-836(2004).
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; AE016822; AAT89769.1; -; Genomic_DNA.
DR   RefSeq; WP_011186754.1; NC_006087.1.
DR   AlphaFoldDB; Q6ACX5; -.
DR   SMR; Q6ACX5; -.
DR   STRING; 281090.Lxx20640; -.
DR   EnsemblBacteria; AAT89769; AAT89769; Lxx20640.
DR   KEGG; lxx:Lxx20640; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_1_11; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   Proteomes; UP000001306; 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; -; 1.
DR   Gene3D; 2.40.50.150; -; 1.
DR   Gene3D; 3.90.1110.10; -; 1.
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; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..1165
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000224070"
SQ   SEQUENCE   1165 AA;  128136 MW;  DF7D01C018C37DFE CRC64;
     MAAARNATNN DKTLKNGRDV SRLSFAKITD TLTVPDLLAL QTESFDWLVG NDAWQARVAA
     AEAQGRQDLP AATGLEEIFE EISPIEDLGE TMQLSFTNPF LEEKKYSIDE CKEKGRTYAA
     PLYVEAEFMN HLTGEIKTQT VFMGDFPLMT ERGTFIINGT ERVVVSQLVR SPGVYFEAAA
     DKTSDKDIYS ARVIPSRGSW LEFEIDKRDQ VGVRIDRKRK QSVTVFLKAL GLTSEEILAE
     FAGFQSIELT LEKDAILTKE EALKDIYRKL RPGEQVAAEA ARALLDNFYF NPKRYDLAKV
     GRYKINRKLG LEAPLTDSVL TVQDIIATIK YLVSLHDGQT SFTGLRSGVE TDIRLDIDDI
     DHFGNRRIRA VGELIQNQVR TGLSRMERVV RERMTTQDIE AITPQTLINV RPVVAAIKEF
     FGTSQLSQFM DQNNPLAGLT HKRRLSALGP GGLSRERAGV EVRDVHPSHY GRMCPIETPE
     GPNIGLIGSL ASFARINSFG FIETPYRKVV DGLVTDQIDY LTASEEDDFV VAQANAPLDA
     RGHFVEERVL ARQKGGEVDL VPAEEIGYMD VSPRQMVSVG TSLIPFLEHD DANRALMGAN
     MQRQAVPLLR SESPVVGTGM EGYAAIDAGD VVIAEKSGIV SEVSADAVTV QADDGTVKTY
     YLRKFDRSNQ GTSYNHRVVV DEGDRIEAGE VVADGPATEN GELALGKNLL VAFMPWEGHN
     FEDAIILSQN LVKDDTLSSI HIEEYEVDAR DTKLGKEEIT RDLPNVSPDL LADLDERGII
     RIGAEVRPGD ILVGKVTPKG ETELSAEERL LRAIFNEKSR EVRDTSLKVP HGEEGTIIGV
     KVFDAQDGDD ELGSGVNQRV VVYIAQKRKI TAGDKLAGRH GNKGVISKIL PVEDMPFLAD
     GTPVDVILNP LGVPGRMNFG QVLEIHLGWI AKNGWEIKGK PKWAAELPET AFSAAPNTKV
     ATPVFDGAKE EEIAGLLDVT LPTRDGDRLI GSSGKTQLFD GRSGEPYPDP VSVGYMYILK
     LHHLVDDKIH ARSTGPYSMI TQQPLGGKAQ FGGQRFGEME VWALEAYGAA YALQELLTIK
     SDDILGRVKV YEAIVKGENI QEPGIPESFK VLIKEMQSLC LNVEVLSADG QAVSLRDADD
     EAFRAAEELG INISSRFESS SIDEI
 
 
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