RPOB_PROM3
ID RPOB_PROM3 Reviewed; 1097 AA.
AC A2C6S8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-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=P9303_04361;
OS Prochlorococcus marinus (strain MIT 9303).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9303;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000554; ABM77188.1; -; Genomic_DNA.
DR AlphaFoldDB; A2C6S8; -.
DR SMR; A2C6S8; -.
DR STRING; 59922.P9303_04361; -.
DR EnsemblBacteria; ABM77188; ABM77188; P9303_04361.
DR KEGG; pmf:P9303_04361; -.
DR HOGENOM; CLU_000524_4_1_3; -.
DR OMA; FMTWEGY; -.
DR BioCyc; PMAR59922:G1G80-405-MON; -.
DR Proteomes; UP000002274; 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_0000300371"
FT REGION 1072..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1097 AA; 122574 MW; DD1F56193BE62CD6 CRC64;
MSSSAIQVAK TATYLPDLVE VQRASFKWFL DEGLIEELDS FSPITDYTGK LELHFVGNEY
RLKRPRHDVE EAKRRDATFA SQMYVTCRLV NKETGEIKEQ EVFIGELPLM TERGTFIING
AERVIVNQIV RSPGVYFKDE QDKNGRRTYN ASVIPNRGAW LKFETDKNDL LHVRVDKTRK
INAHVLMRAM GLSDNDVIDK LRHPEYYKKS IEAANEEGIS SEDQALLELY KKLRPGEPPS
VSGGQQLLQT RFFDPKRYDL GRVGRYKINK KLRLTIPDTV RTLTHEDVLS TLDYLINLEL
DVGGASLDDI DHLGNRRVRS VGELLQNQVR VGLNRLERII KERMTVGETD SLTPAQLVNP
KPLVAAVKEF FGSSQLSQFM DQTNPLAELT HKRRISALGP GGLTRERAGF AVRDIHPSHY
GRLCPIETPE GPNAGLINSL ATHARVNQYG FIETPFWKVE NGRLIKEGDP IYLSADLEDE
CRVAPGDVAT DADGQILAEL IPVRYRQDFE KVPPEQVDYV QLSPVQVISV ATSLIPFLEH
DDANRALMGS NMQRQAVPLL RPERPLVGTG LETQVARDSG MVPISRVNGM VTFVDATAII
VRDEDGVDHT HYLQKYQRSN QDTCLNQRPI VCQGDPVIVG QVLADGSACE GGEIALGQNV
LVAYMPWEGY NYEDAILVSE RLVKDDLYTS VHIEKYEIEA RQTKLGPEEI TREIPNVAEE
SLGNLDEMGI IRIGAFVESG DILVGKVTPK GESDQPPEEK LLRAIFGEKA RDVRDNSLRV
PSTERGRVVD VRIYTREQGD ELPPGANMVA RVYVAQRRKI QVGDKMAGRH GNKGIISRIL
PREDMPFLPD GTPVDIVLNP LGVPSRMNVG QVFECLMGWA AANLDCRVKV VPFDEMYGAE
KSQQTVEAYL KEAAKQPGKE WVYNPENPGK LQLIDGRSGE PFDQPVTVGY AQILKLVHLV
DDKIHARSTG PYSLVTQQPL GGKAQQGGQR LGEMEVWALE AYGAAYTLQE LLTVKSDDMQ
GRNEALNAIV KGKPIPRPGT PESFKVLMRE LQSLGLDIAV YTDEGKEVDL MQDVNPRRST
PSRPTYESLG VADYDED