RPOB_PROM9
ID RPOB_PROM9 Reviewed; 1097 AA.
AC Q318Q7;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-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};
GN OrderedLocusNames=PMT9312_1578;
OS Prochlorococcus marinus (strain MIT 9312).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9312;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000111; ABB50638.1; -; Genomic_DNA.
DR RefSeq; WP_011377120.1; NC_007577.1.
DR AlphaFoldDB; Q318Q7; -.
DR SMR; Q318Q7; -.
DR STRING; 74546.PMT9312_1578; -.
DR EnsemblBacteria; ABB50638; ABB50638; PMT9312_1578.
DR KEGG; pmi:PMT9312_1578; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_3; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000002715; 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_0000237310"
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; 122905 MW; 691F9137F99EE3C6 CRC64;
MSSSALQVAK TGTYLPDLVE VQRASFKWFL EKGLIEELQN FSPISDYTGK LELHFIGEEY
RLKRPRHDVE EAKRRDATFA SQMYVTCRLI NKETGEIKEQ EVFIGELPLM TERGTFIING
AERVIVNQIV RSPGVYFKDE QDKNGRRTYN ASVIPNRGAW LKFETDKNNL LYVRVDKTRK
INAHVLMRAM GLSDNDVVDK LRHPEFYQNS IESANDEGIN SEDQALLELY KKLRPGEPPS
VSGGQQLLFS RFFDPKRYDL GRVGRYKINK KLRLTVPDDV RTLTHEDVLS TIDYLINLEL
DIGGASLDDI DHLGNRRVRS VGELLQNQVR VGLNRLERII KERMTVGETD SLTPAQLVNP
KPLVAAIKEF FGSSQLSQFM DQTNPLAELT HKRRISALGP GGLTRERAGF AVRDIHPSHY
GRLCPIETPE GPNAGLINSL ATHARVNEYG FIETPFWKVN NGKVNKDGDP IYLSADLEDE
CRVAPGDVAT DKDGNILANL IPVRYRQDFE KVPPEQVDYV QLSPVQVISV ATSLIPFLEH
DDANRALMGS NMQRQAVPLL RPERPLVGTG LESQVARDSG MVPITKVNGT VSYVDANEIV
VKGEDGNEHF HYLQKYQRSN QDTCLNQRPI VNIGDQVISG QVLADGSACE GGEIALGQNV
LIAYMPWEGY NYEDAILVSE RMVTDDLYTS VHIEKYEIEA RQTKLGPEEI TREIPNISED
SLNNLDEMGI IRIGAFVESG DILVGKVTPK GESDQPPEEK LLRAIFGEKA RDVRDNSLRV
PKTEKGRVLD VRIYTREQGD ELPPGANMVV RVYVAQRRKI QVGDKMAGRH GNKGIISRIL
PREDMPYLPD GTPVDIVLNP LGVPSRMNVG QVFELLMGWA ASNLNCRVKV VPFDEMYGAE
KSHQTVQAFL EEASKQPGKA WIYNPEDPGK LLLKDGRTGE PFDQPVAVGY SHFLKLVHLV
DDKIHARSTG PYSLVTQQPL GGKAQQGGQR LGEMEVWALE AYGAAYTLQE LLTVKSDDMQ
GRNEALNAIV KGKPIPRPGT PESFKVLMRE LQSLGLDIGV YTDEGKEVDL MQDINPRRNT
PSRPTYESLG TSEYEED
