ID   RPOB_XYLFA              Reviewed;        1388 AA.
AC   Q9PA86;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=XF_2633;
OS   Xylella fastidiosa (strain 9a5c).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=160492;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9a5c;
RX   PubMed=10910347; DOI=10.1038/35018003;
RA   Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M.,
RA   Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S.,
RA   Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S.,
RA   Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H.,
RA   Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M.,
RA   Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H.,
RA   Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S.,
RA   Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H.,
RA   Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D.,
RA   Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E.,
RA   Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F.,
RA   Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N.,
RA   Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F.,
RA   Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y.,
RA   Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O.,
RA   Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A.,
RA   de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R.,
RA   Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B.,
RA   Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G.,
RA   Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M.,
RA   da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z.,
RA   Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D.,
RA   Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S.,
RA   Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.;
RT   "The genome sequence of the plant pathogen Xylella fastidiosa.";
RL   Nature 406:151-159(2000).
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; AE003849; AAF85430.1; -; Genomic_DNA.
DR   PIR; E82533; E82533.
DR   AlphaFoldDB; Q9PA86; -.
DR   SMR; Q9PA86; -.
DR   STRING; 160492.XF_2633; -.
DR   PRIDE; Q9PA86; -.
DR   EnsemblBacteria; AAF85430; AAF85430; XF_2633.
DR   KEGG; xfa:XF_2633; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_0_6; -.
DR   OMA; FMTWEGY; -.
DR   Proteomes; UP000000812; 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; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..1388
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000048000"
SQ   SEQUENCE   1388 AA;  154782 MW;  2CB30F50C4A2D372 CRC64;
     MKDLMTSYSF TEKKRIRKDF GKHRSILKVP FLLAIQVDSY RAFLQGDVES SQRKDIGLHA
     ALKSVFPIVS YSGNAALEYV GYKLGEPMFD ERECRQRGMS YGAPLRVTVR LVIYDRESST
     KAVKYIKEQE VYLGEIPLMT ENGTFIVNGT ERVIVSQLHR SPGVFFDHDR GKTHSSGKLL
     YSARIIPCRG SWLDFEFDPK DALFTRIDRR RKLPVSILLR ALGYSNEEIL GEFFEINTFH
     INPDKGVQLE LVPERLRGEI LSFNLTDGGG VIVEAGKRIT ARHVKQLEAS GISALAVPDE
     YLIGRILSHD VIDATTGELL ASANSEVNED RIVAFRKAGI DSVGTLWVND 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 TSGDVLADGP STDIGELALG QNMLIAFMPW
     NGYNFEDSIL LSERVVEEDR YTTIHIEELT CIARDTKLGS EEISADIPNV SEQALNRLDE
     SGVVYIGAEV RAGDILVGKV TPKGESQLTP EEKLLRAIFG EKASDVKDSS LRVPPGMDGT
     VIDVQVFTRD GIEKDKRAHQ IEEYEIKRVK KDFDDQFRIL EGAIYARLRS QIVGKVVNSG
     VDIKKGEVIT GAYLDGLKKS DWFALRMKDE VAVEAIDRAQ KQIQAYQKEF DQRFSDKRSK
     ITQGDDLAPG VLKMVKVFLA VKRCIQPGDK MAGRHGNKGV VSNVVPVEDM PFMEDGTPVD
     IVLNPLGVPS RMNIGQILEV HLGWAAKGLG HRIQRMLEAN AAIADLRKFL NEIYNHDKSV
     VGERVDLSQF SDDELLNMAK NLTDGVPMAS PVFDGASEQE IKRMLDLAEL PTGGQTQLYD
     GHTGEPFDRK TTVGYMHYLK LNHLVDDKMH ARSTGPYSLV TQQPLGGKAQ FGGQRFGEME
     VWALEAYGAA YTLQEMLTVK SDDVQGRNQM YKNIVDGDHQ MVAGMPESFN VLVKEIRSLA
     INIELEDN