ID   RPOB_SYNPW              Reviewed;        1097 AA.
AC   A5GNH3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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};
GN   OrderedLocusNames=SynWH7803_2062;
OS   Synechococcus sp. (strain WH7803).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32051;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH7803;
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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: In cyanobacteria the RNAP catalytic core is composed of 2
CC       alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When a sigma
CC       factor is associated with the core the holoenzyme is formed, which can
CC       initiate transcription. {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; CT971583; CAK24488.1; -; Genomic_DNA.
DR   RefSeq; WP_011933953.1; NC_009481.1.
DR   AlphaFoldDB; A5GNH3; -.
DR   SMR; A5GNH3; -.
DR   STRING; 32051.SynWH7803_2062; -.
DR   EnsemblBacteria; CAK24488; CAK24488; SynWH7803_2062.
DR   KEGG; syx:SynWH7803_2062; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_1_3; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   Proteomes; UP000001566; 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..1097
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000300419"
FT   REGION          1072..1097
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1097 AA;  122582 MW;  A8F6D7A744EF0656 CRC64;
     MSSSAIQVAK TATYLPDLVE VQRASFKWFL EKGLIEELES FSPITDYTGK LELHFVGSEY
     RLKRPRHDVE EAKRRDATFA SQMYVTCRLV NKETGEIKEQ EVFIGELPLM TERGTFIING
     AERVIVNQIV RSPGVYFKDE QDKNGRRTYN ASVIPNRGAW LKFETDKNDL LHVRVDKTRK
     INAHVLMRAM GLSDNDVIDK LRHPEYYKKS IEAANDEGIS SEDQALLELY KKLRPGEPPS
     VSGGQQLLQT RFFDPKRYDL GRVGRYKINK KLRLTIPDSV RTLTHEDVLS TLDYLINLEL
     DVGGASLDDI DHLGNRRVRS VGELLQNQVR VGLNRLERII KERMTVGETD SLTPAQLVNP
     KPLVAAIKEF FGSSQLSQFM DQTNPLAELT HKRRISALGP GGLTRERAGF AVRDIHPSHY
     GRLCPIETPE GPNAGLINSL ATHARVNEYG FIETPFWKVE NGRVLKQGDP IYLSADLEDE
     CRVAPGDVAT DSDGAILADL IPVRYRQDFE KVPPEQVDYV QLSPVQVISV ATSLIPFLEH
     DDANRALMGS NMQRQAVPLL RPERPLVGTG LETQVARDSG MVPISRVNGT VTFVDATAIV
     VRDEEGVDHS HYLQKYQRSN QDTCLNQRPI VRQGDPVIVG QVLADGSACE GGEIALGQNV
     LIAYMPWEGY NYEDAILVSE RLVNDDLYTS VHIEKYEIEA RQTKLGPEEI TREIPNVAEE
     SLGNLDEMGI IRIGAFVESG DILVGKVTPK GESDQPPEEK LLRAIFGEKA RDVRDNSLRV
     PSTERGRVVD VRIYTREQGD ELPPGANMVV RVYVAQRRKI QVGDKMAGRH GNKGIISRIL
     PREDMPYLPD GTPVDIVLNP LGVPSRMNVG QVFELLMGWA AANLDCRVKV VPFDEMYGAE
     KSQQTVETFL KEAAKQPGKE WIYNPDDPGK LQLIDGRSGE PFDQPVAVGY SHFLKLVHLV
     DDKIHARSTG PYSLVTQQPL GGKAQQGGQR LGEMEVWALE AYGAAYTLQE LLTVKSDDMQ
     GRNEALNAIV KGKPIPRPGT PESFKVLMRE LQSLGLDIAV FTDEGKEVDL MQDVNPRRST
     PSRPTYESLG VADYDED