RPOB_SYNP6
ID RPOB_SYNP6 Reviewed; 1100 AA.
AC Q5MZ23;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=syc2507_d;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(2007).
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; AP008231; BAD80697.1; -; Genomic_DNA.
DR RefSeq; WP_011244817.1; NC_006576.1.
DR AlphaFoldDB; Q5MZ23; -.
DR SMR; Q5MZ23; -.
DR STRING; 269084.syc2507_d; -.
DR EnsemblBacteria; BAD80697; BAD80697; syc2507_d.
DR KEGG; syc:syc2507_d; -.
DR eggNOG; COG0085; Bacteria.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000001175; 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; Transcription;
KW Transferase.
FT CHAIN 1..1100
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000224114"
FT REGION 1064..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1100 AA; 123265 MW; A10EDE6FB7C3BCF3 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
RALMSSNMQR QAVPLLRPER PLVGTGLEPQ AARDSGMVIT SPVDGTISYV DATHIEVTAD
TGEKYGYALQ KYQRSNQDTC LNQRPIVFEG DRGQRGQVIA 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
