RPOB_PROM2
ID RPOB_PROM2 Reviewed; 1097 AA.
AC A8G6Y6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=P9215_17541;
OS Prochlorococcus marinus (strain MIT 9215).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=93060;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9215;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(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; CP000825; ABV51367.1; -; Genomic_DNA.
DR RefSeq; WP_012008384.1; NC_009840.1.
DR AlphaFoldDB; A8G6Y6; -.
DR SMR; A8G6Y6; -.
DR STRING; 93060.P9215_17541; -.
DR EnsemblBacteria; ABV51367; ABV51367; P9215_17541.
DR KEGG; pmh:P9215_17541; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_3; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000002014; 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..1097
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000067551"
FT REGION 1072..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1089
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1097 AA; 122996 MW; C21BD9F44E58E6E4 CRC64;
MSSSALQVAK TATYLPDLVE VQRASFKWFL EQGLIEELQN FSPISDYTGK LELHFIGEEY
RLKRPRHDVE EAKRRDATFA SQMYVTCRLI NKETGEIKEQ EVFIGELPLM TERGTFIING
AERVIVNQIV RSPGVYFKDE LDKNGRRTYN ASVIPNRGAW LKFETDKNNL LYVRVDKTRK
INAHVLMRAM GLSDNDVVDK LRHPEFYQSS IESANDEGIN SEDQALLELY KKLRPGEPPS
VSGGQQLLHS RFFDPKRYDL GRVGRYKINK KLRLTVPDDV RTLTHEDVLS TIDYLINLEL
DIGGASLDDI DHLGNRRVRS VGELLQNQVR VGLNRLERII KERMTVGETD SLTPAQLVNP
KPLVAAIKEF FGSSQLSQFM DQTNPLAELT HKRRISALGP GGLTRERAGF AVRDIHPSHY
GRLCPIETPE GPNAGLINSL ATHARVNEYG FIETPFWEVN NGKVDKEGNP VYLSADLEDE
CRVAPGDVAT DKEGNIIANL IPVRYRQDFE KVPPHQVDYV QLSPVQVISV ATSLIPFLEH
DDANRALMGS NMQRQAVPLL RPERPLVGTG LESQVARDSG MVPITKVNGI VSYVDANEIV
VKDDHGNEHF HYLQKYQRSN QDTCLNQRPI VKIGDRVISG QVLADGSACE GGEIALGQNV
LIAYMPWEGY NYEDAILVSE RMVTDDLYTS VHIEKYEIEA RQTKLGPEEI TREIPNISEE
SLNNLDEMGI IRIGAFVESG DILVGKVTPK GESDQPPEEK LLRAIFGEKA RDVRDNSLRV
PKTEKGRVLD VRIYTREQGD ELPPGANMVV RVYVAQRRKI QVGDKMAGRH GNKGIISRIL
PREDMPYLPD GTPVDIVLNP LGVPSRMNVG QVFELLMGWA ASNLNCRVKV VPFDEMYGAE
KSHQTVQAFL EEASKQPGKA WVYNPDDPGK LLLKDGRTGE PFDQPVAVGY SHFLKLVHLV
DDKIHARSTG PYSLVTQQPL GGKAQQGGQR LGEMEVWALE AYGAAYTLQE LLTVKSDDMQ
GRNEALNAIV KGKPIPRPGT PESFKVLMRE LQSLGLDIGV YTDEGKEVDL MQDINPRRNT
PSRPTYESLG TSEYEED
