RPOB_PROMT
ID RPOB_PROMT Reviewed; 1095 AA.
AC Q46J22;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=PMN2A_1016;
OS Prochlorococcus marinus (strain NATL2A).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59920;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL2A;
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; CP000095; AAZ58506.1; -; Genomic_DNA.
DR RefSeq; WP_011295361.1; NC_007335.2.
DR AlphaFoldDB; Q46J22; -.
DR SMR; Q46J22; -.
DR STRING; 59920.PMN2A_1016; -.
DR EnsemblBacteria; AAZ58506; AAZ58506; PMN2A_1016.
DR KEGG; pmn:PMN2A_1016; -.
DR HOGENOM; CLU_000524_4_1_3; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR PhylomeDB; Q46J22; -.
DR Proteomes; UP000002535; 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..1095
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000224091"
FT REGION 1069..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1095 AA; 122610 MW; 5E5F3B5071A0F395 CRC64;
MSRSAIQVAK AATYLPDLVE VQRSSFKWFL DKGLIEELDN FSPITDYTGK LELHFIGAEY
KLKRPRHDVE EAKRRDATFA SQMYVTCRLV NKETGEIKEQ EVFIGELPLM TERGTFIING
AERVIVNQIV RSPGVYFKDE QDKNGRRTYN ASVIPNRGAW LKFETDKNDL LHVRVDKTRK
INAHVLMRAM GLSDNDVIDK LRHPEFYKKS IDAANEEGIS SEDQALLELY KKLRPGEPPS
VSGGQQLLQT RFFDPKRYDL GRVGRYKINK KLRLTIPDNL RTLTNEDVLS TLDYLINLEL
DVGGATLDDI DHLGNRRVRS VGELLQNQVR VGLNRLERII KERMTVGETD SLTPAQLVNP
KPLVAAIKEF FGSSQLSQFM DQTNPLAELT HKRRISALGP GGLTRERAGF AVRDIHPSHY
GRLCPIETPE GPNAGLINSL ATHARVNEYG FIETPFWKVE NGRLIKEGDP IYLSADLEDE
CRVAPGDVAT NEEGKIMAEL VPVRYRQDFE TVSPEQVDYV QLSPVQVISV AASLIPFLEH
DDANRALMGS NMQRQAVPLL RPERPLVGTG LETQVARDSG MVPISKVNGK VTYVDANAIV
VTDDEGNDHT HYLQKYQRSN QDTCLNHRPI VFNGDPVIVG QVLADGSACE GGEIALGQNV
LIAYMPWEGY NYEDAILVSE RLVKDDLYTS VHIEKYEIEA RQTKLGPEEI TREIPNVSEE
NLGNLDEMGI IRIGAYVESG DILVGKVTPK GESDQPPEEK LLRAIFGEKA RDVRDNSLRV
PSTERGRVVD VRIYTREQGD ELPPGANMVV RVYVAQRRKI QVGDKMAGRH GNKGIISRIL
PREDMPYLPD GTPVDICLNP LGVPSRMNVG QVFELLMGWA ASNLDCRVKI VPFDEMYGPE
MSNQTVQAYL KKAAKQPGKS WVYNPKDPGK LLLKDGRTGE PFDQPVAVGY AHFLKLVHLV
DDKIHARSTG PYSLVTQQPL GGKAQQGGQR LGEMEVWALE AYGAAYTLQE LLTVKSDDMQ
GRNEALNSIV KGKPIPRPGT PESFKVLMRE LQSLGLDIGV YTDDGKEVDL MQDVNPRRST
PSRPTYESLG KEYEE
