ID   RPOB_SYNR3              Reviewed;        1097 AA.
AC   A5GVF3;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 2.
DT   03-AUG-2022, entry version 77.
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=SynRCC307_1959;
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=316278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAK28862.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CT978603; CAK28862.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; A5GVF3; -.
DR   SMR; A5GVF3; -.
DR   STRING; 316278.SynRCC307_1959; -.
DR   PRIDE; A5GVF3; -.
DR   EnsemblBacteria; CAK28862; CAK28862; SynRCC307_1959.
DR   KEGG; syr:SynRCC307_1959; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_3_3; -.
DR   Proteomes; UP000001115; 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_0000329192"
FT   REGION          1073..1097
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1097 AA;  122582 MW;  6268AA2A1EC927C5 CRC64;
     MSSAIQVAKT ATYLPDLVEV QRGSFKWFLE KGLIEELESF SPITDYTGKL ELHFVGSEYR
     LKRPRHDVEE AKRRDATFAS QMYVTCRLVN KETGEIKEQE VFIGELPLMT ERGTFIINGA
     ERVIVNQIVR SPGVYFKDEQ DKNGRRTYNA SLIPNRGAWL KFETDKNDLL HVRVDKTRKI
     NAHVMMRAIG LSDNDVLDKL RHPEYYKKSI DAANEEGISS EDQALLELYK KLRPGEPPSV
     SGGQQLLHSR FFDPKRYDLG RVGRYKMNKK LRLTIPDAVR TLTPEDVLST LDYLINLELD
     VGGACLDDID HLGNRRVRSV GELLQNQVRV GLNRLERIIK ERMTVGETDS LTPAQLVNPK
     PLVAAIKEFF GSSQLSQFMD QTNPLAELTH KRRISALGPG VLTRERAGFA VRDIHPSHYG
     RICPIETPEG PNAGLIGSLA THARVNEYGF IETPFWKVTD GVVDKSGDPI YLSADLEDEC
     RVAPGDVATD ADGRITAELI PVRYRLDFET VPPNQVDYVQ LSPVQVISVA ASLIPFLEHD
     DANRALMGSN MQRQAVPLLR PERPLVGTGL ETQVARDSGM VPITRVNGEV VFVDSTQIIV
     RDDQGVDHYH LLQKYQRSNQ DTCLNQRPIV QQGDQVIAGQ VLANGSACEG GEIALGQNCL
     IAYMPWEGYN YEDAILVSER LVRDDLYTSV HIEKYEIEAR QTKLGPEEIT REIPNVAEES
     LGNLDEMGII RIGAFVESGD ILVGKVTPKG ESDQPPEEKL LRAIFGEKAR DVRDNSLRVP
     NTERGRVVDV RIYTREQGDE LPPGANMVVR VYVAQRRKIQ VGDKMAGRHG NKGIISRILP
     LEDMPYLPDG TPIDIVLNPL GVPSRMNVGQ VFECALMGWA ADNLDSRFKI VPFDEMHGAE
     KSRETVEGYL KEAAKQPGRE WVYDPENPGK IQLIDGRSGE PFDQPVTVGR AYILKLVHLV
     DDKIHARSTG PYSLVTQQPL GGKAQQGGQR LGEMEVWALE AYGAAYTLQE LLTVKSDDMQ
     GRNEALNAIV KGKPIPRPGT PESFKVLMRE LQSLGLDIAV YTDEGAEVDL MQDVNPRRST
     PSRPTYESLG VADYDED