RPOB_SYNE7
ID RPOB_SYNE7 Reviewed; 1100 AA.
AC Q31N17;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=Synpcc7942_1522;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) 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; CP000100; ABB57552.1; -; Genomic_DNA.
DR RefSeq; WP_011378064.1; NC_007604.1.
DR AlphaFoldDB; Q31N17; -.
DR SMR; Q31N17; -.
DR STRING; 1140.Synpcc7942_1522; -.
DR PRIDE; Q31N17; -.
DR EnsemblBacteria; ABB57552; ABB57552; Synpcc7942_1522.
DR KEGG; syf:Synpcc7942_1522; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_3; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1522-MON; -.
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; Transcription;
KW Transferase.
FT CHAIN 1..1100
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000237320"
FT REGION 1064..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1100 AA; 123277 MW; 76D74FF497D62E34 CRC64;
MAEQTQLAPA AFHLPDLVAI QRNSFRWFLE EGLIEELESF SPITDYTGKL ELHFLGKQYK
LKRPKYDVDE AKRRDGTYSV QMYVPTRLIN KETGEIKEQE VFIGDLPLMT DRGTFIINGA
ERVIVNQIVR SPGVYYKSER DKNGRLTHNA SLIPNRGAWL KFETDKNGLV WVRIDKTRKL
SAQVLLKALG LSDNEIYDKL RHPEYYQKTI DKEGQFSEDE ALMELYRKLR PGEPPTVSGG
QQLLESRFFD PKRYDLGRVG RYKLNKKLGL NVADTVRTLT SEDILAAIDY LINLELDLGG
CEVDDIDHLG NRRVRSVGEL LQNQVRVGLN RLERIIRERM TVSDSDSLSP ASLVNPKPLV
AAIKEFFGSS QLSQFMDQTN PLAELTHKRR LSALGPGGLT RERAGFAVRD IHPSHYGRIC
PIETPEGPNA GLIGSLATHA RVNDYGFIET PFWRVEEGRV RKDLAPVYMT ADQEDDLRVA
PGDVATDDAG YILGTTIPVR YRQDFTTTTP ERVDYVALSP VQIISVATSL IPFLEHDDAN
RALMGSNMQR QAVPLLRPER PLVGTGLEPQ AARDSGMVIT SPVDGTISYV DATHIEVTAD
TGEKYGYALQ KYQRSNQDTC LNQRPIVFEG DRVQRGQVIA DGSATEKGEL ALGQNILVAY
MPWEGYNYED AILISERLVY DDVYTSIHIE KFEIEARQTK LGPEEITREI PNVGEDALRQ
LDENGIIRVG AWVESGDILV GKVTPKGESD QPPEEKLLRA IFGEKARDVR DNSLRVPNGE
KGRVVDVRLF TREQGDELPP GANMVVRVYV AQKRKIQVGD KMAGRHGNKG IISRILPCED
MPYLPDGTPL DIVLNPLGVP SRMNVGQVFE CMLGWAGQLL DARFKVTPFD EMYGAEASRL
TVNAKLSEAR EQTGQPWVFS DDEPGKIQVY DGRTGEPFDR PVTVGRAYML KLVHLVDDKI
HARSTGPYSL VTQQPLGGKA QQGGQRFGEM EVWALEAYGA AYILQELLTV KSDDMQGRNE
ALNAIVKGKA IPRPGTPESF KVLMRELQSL CLDIAVYKAS TEDYEEDKEV DLMADVNQRR
TPSRPTYESM SVGDIDDDDD
