ID   RPOB_XYLFT              Reviewed;        1388 AA.
AC   Q87A32;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=PD_2001;
OS   Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=183190;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Temecula1 / ATCC 700964;
RX   PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA   Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA   Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA   Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA   Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA   Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA   Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA   Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA   Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA   Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA   Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA   Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA   Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT   "Comparative analyses of the complete genome sequences of Pierce's disease
RT   and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL   J. Bacteriol. 185:1018-1026(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; AE009442; AAO29830.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q87A32; -.
DR   SMR; Q87A32; -.
DR   EnsemblBacteria; AAO29830; AAO29830; PD_2001.
DR   KEGG; xft:PD_2001; -.
DR   HOGENOM; CLU_000524_4_0_6; -.
DR   OMA; FMTWEGY; -.
DR   Proteomes; UP000002516; 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; 2.40.270.10; -; 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; 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..1388
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000048001"
SQ   SEQUENCE   1388 AA;  154885 MW;  5D57D6C02EA55425 CRC64;
     MKDLMTSYSF TEKKRIRKDF GKHRSILKVP FLLAIQVDSY RAFLQGDVES SQRKDIGLHG
     ALKSVFPIVS YSGNAALEYV GYKLGEPMFD ERECRQRGMS YGAPLRVTVR LVIYDRESST
     KAVKYIKEQE VYLGEIPLMT ENGTFIVNGT ERVIVSQLHR SPGVFFDHDR GKTHSSGKLL
     YSARIIPCRG SWLDFEFDPK DALFTRIDRR RKLPVSILLR ALGYSNEEIL GEFFEINTFH
     INPDEGVQLE LVPERLRGEI LSFNLTDGGS VIVEAGKRIT ARHVKQLEAS GISALAVPDE
     YLIGRILSHD VIDATTGELL ASANSEVNED RIIAFRKAGI ESVGTLWVND LDRGAYLSNT
     LRIDPTRTQL EAQVEIYRMM RPGEPPTKEA AQNLFHNLFF TFDRYDLSMV GRMKFNRRVG
     RKEVAGEPVL YDKKYFSDRN DEESRRLVSK LGETSDILDV IKGLCEIRNG RGVVDDIDHL
     GNRRVRSVGE MAENVFRVGL VRVERAVKER LSMAESEGLT PQELINAKPV AAAIKEFFGS
     SQLSQFMDQN NPLSEVTHKR RLSALGPGGL TRERAGFEVR DVHLSHYGCL CTIETPEGPN
     IGLINSLAVF ARTNQYGFLE TPYRKVVEGR VTDEVEYLSA IEENQYVIAQ ANTLTDDNGQ
     LTESFVPCRF QGESLLKPPS YVHYMDVSPM QTVSVAAALV PFLEHDDANR ALMGANMQRQ
     AVPTLRAQKP LVGTGIERTV ARDSGVTVNA RRGGVIDQVD AGRIVVKVNE SEIIGATDAG
     VDIYGLIKYT RSNQNTCINQ RPLVNVGDIV ASGDVLADGP STDIGELALG QNMLIAFMPW
     NGYNFEDSIL LSERVVEEDR YTTIHIEELT CIARDTKLGS EEISADIPNV SEQALNRLDE
     SGVVYIGAEV RAGDILVGKV TPKGESQLTP EEKLLRAIFG EKASDVKDSS LRVPPGMDGT
     VIDVQVFTRD GIEKDKRAHQ IEEYEIKRVK KDFDDQFRIL EGAIYARLRS QIVGKVVNSG
     VDIKKGEVIT DPYLDGLKKS DWFALRMKDE VAVEAIDRAQ KQIQAYQKEF DQRFSDKRSK
     ITQGDDLAPG VLKMVKVFLA VKRCIQCGDK MAGRHGNKGV ISNVVPVEDM PFMEDGTPVD
     IVLNPLGVPS RMNIGQILEV HLGWAAKGLG HRIQRMLEAN AAIADLRKFL NEIYNHDKSL
     VGERVDLSQF SDDELLNMAK NLTDGVPMAS PVFDGASEQE IKRMLDLAEL PAGGQTQLYD
     GHTGEPFDRK TTVGYMHYLK LNHLVDDKMH ARSTGPYSLV TQQPLGGKAQ FGGQRFGEME
     VWALEAYGAA YTLQEMLTVK SDDVQGRNQM YKNIVDGDHQ MVAGMPESFN VLVKEIRSLA
     INIELEDN