RPOB_MARMS
ID RPOB_MARMS Reviewed; 1366 AA.
AC A6W399;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=Mmwyl1_4283;
OS Marinomonas sp. (strain MWYL1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=400668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWYL1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA Richardson P.;
RT "Complete sequence of Marinomonas sp. MWYL1.";
RL Submitted (JUN-2007) 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: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC and 1 omega subunit. When a sigma factor is associated with the core
CC the holoenzyme is formed, which can initiate transcription.
CC {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; CP000749; ABR73178.1; -; Genomic_DNA.
DR RefSeq; WP_012071943.1; NC_009654.1.
DR AlphaFoldDB; A6W399; -.
DR SMR; A6W399; -.
DR STRING; 400668.Mmwyl1_4283; -.
DR PRIDE; A6W399; -.
DR EnsemblBacteria; ABR73178; ABR73178; Mmwyl1_4283.
DR KEGG; mmw:Mmwyl1_4283; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_6; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
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; 2.
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..1366
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000086373"
SQ SEQUENCE 1366 AA; 151756 MW; 0250FCDBDFAA05D8 CRC64;
MAYSYTEKKR IRKDFGKLPP VLDVPYLLAI QLESYRNFLQ EGKSLAERGE LGLHGAFKSV
FPMVSFSGNA ALEYVDYRLG KPVFDVKECQ LRGVTYAAPL RVRVRLIIYD KESSNKAIKD
IREQEVYMGE IPLMTDNGTF VINGTERVIV SQLHRSPGVF FDHDRGKTHS SGKLLHSARI
IPYRGSWLDF EFDPKDCVFV RIDRRRKLPA TILLRALGYG TEQILDTFFD STRFYLKRDG
FEMDLVANRL RGETALFNIA DANGELIVEE GRRITAKHIR VMEKSGLERL SVPLEYMLGK
VTAKNLVHPA TGELIAEANT ELSVDLLEAL VSSGITEVDT LYTNDLDNGP FISDTLRIDP
TSNQLEALVE IYRMMRPGEP PTKESAEGLF QGLFFSEDRY DLSGVGRMKF NRRLGREEDT
GAGVLDNDDI VAVLKTLLDI RNGNGMVDDI DHLGNRRVRS VGEMAENQFR VGLVRVERAV
KERLSMAEAD GLMPQDLLNA KPVAAAIKEF FGSSQLSQFM DQNNPLSEVT HKRRVSALGP
GGLTRERAGF EVRDVHATHY GRVCPIETPE GPNIGLINSL STYARTNSYG FLETPYRKIV
DGKQTDETVY VSAIDEAKYV IAQASANVDA EGRLVDELVQ VRHMHETTLI PKEKVNLMDV
SPRQVVSVAA SLIPFLEHDD ANRALMGSNM QRQAVPTLKA DKPVVGTGME KNVAKDSGVC
IVANRGGVIE SVDASRIVVR VNSEETIAGE AGVDIYNLTK YVRSNQNTCI NQRTLVMKGE
RIASGDIMAD GPSVDMGELA LGQNMRIAFM PWNGFNFEDS ILVSERVVEE DRFTSIHIQE
LTCVARDTKL GPEEITADIP NVGEGALSKL DQSGIVYIGA EVEPGDILVG KVTPKGETQL
TPEEKLLRAI FGEKASDVKD TSQRVKTGTR GTVIDVQVFT RDGIEKDDRA KFIEKSQLDQ
VRKDLNEEFR IVEKATFERL AEALIGQQAE GGPGLARNAI ITEEYLANLD HPEWFKIRVA
NEDASEQLEK AQAALIERRK ELDAKFEDKK RKLQTGDDLA PGVLKIVKVY VAIKRRIQPG
DKMAGRHGNK GVISKIMPVE DMPYDENGDP VDIVLNPLGV PSRMNVGQVL ETHLGAASKG
LGRKINEMLV VEREKAEAVA ELRSFLGEIY NGYEGDLRCA RTEDLDSFTD EEILTLASNL
TGGVPMASGA FDGAKESEIK RMLRLAGINE SGQVKLFNGR TGDAFERPVT VGYMYMLKLN
HLVDDKMHAR STGSYSLVTQ QPLGGKAQFG GQRFGEMEVW ALEAYGAAYT LQEMLTVKSD
DVNGRTKMYK NIVDGDHRME PGMPESFNVL VKEIRSLGID IELENE
