RPOB_SYNS3
ID RPOB_SYNS3 Reviewed; 1097 AA.
AC Q0I7L7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=sync_2358;
OS Synechococcus sp. (strain CC9311).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=64471;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9311;
RX PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA Paulsen I.T.;
RT "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT coastal environment.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
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; CP000435; ABI46057.1; -; Genomic_DNA.
DR RefSeq; WP_011620265.1; NC_008319.1.
DR AlphaFoldDB; Q0I7L7; -.
DR SMR; Q0I7L7; -.
DR STRING; 64471.sync_2358; -.
DR EnsemblBacteria; ABI46057; ABI46057; sync_2358.
DR KEGG; syg:sync_2358; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_3; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000001961; 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_0000300418"
FT REGION 1073..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1097 AA; 122688 MW; 4424EC41B67D838F CRC64;
MSSSAIQVAK TVTYLPDLVE VQRASFKWFL DKGLIEELES FSPITDYTGK LELHFVGSEY
RLKRPRHDVE EAKRRDATFA SQMYVTCRLV NKETGEIKEQ EVFIGELPLM TERGTFIING
AERVIVNQIV RSPGVYFKDE QDKNGRRTYN ASVIPNRGAW LKFETDKNDL LHVRVDKTRK
INAHVLMRAM GLSDNDVVDK 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 FIETPFWRVE NGVVQKSGDP IYLSADLEDE
CRVAPGDVAT DADGQILAEL IPVRYRQDFE KVPPEQVDYV QLSPVQVISV ATSLIPFLEH
DDANRALMGS NMQRQAVPLL RPERPLVGTG LETQVARDSG MVPISRVNGT VTFVDATAIV
VRDEEGYDHT HFLQKYQRSN QDTCLNQRPI VRQGDPVIIG QVLADGSACE GGEIALGQNV
LIAYMPWEGY NYEDAILVSE RLVNDDLYTS VHIEKYEIEA RQTKLGPEEI TREIPNVAEE
SLGNLDEMGI IRIGAFVESG DILVGKVTPK GESDQPPEEK LLRAIFGEKA RDVRDNSLRV
PSTERGRVVD VRIYTREQGD ELPPGANMVV RVYVAQRRKI QVGDKMAGRH GNKGIISRIL
PREDMPYLPD GTPVDICLNP LGVPSRMNVG QVFELLMGWA AANLDCRVKI VPFDEMYGPE
KSQQTVQAYL KEAASQPGKD WIYNPEDPGK LLLRDGRTGE PFDQPVAVGY SHFLKLVHLV
DDKIHARSTG PYSLVTQQPL GGKAQQGGQR LGEMEVWALE AYGAAYTLQE LLTVKSDDMQ
GRNEALNAIV KGKPIPRPGT PESFKVLMRE LQSLGLDIAV FTDEGKEVDL MQDVNPRRST
PSRPTYESLG VADYDED
