RPOB_PSEMY
ID RPOB_PSEMY Reviewed; 1357 AA.
AC A4XZ97;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=Pmen_3916;
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ymp;
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., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-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; CP000680; ABP86663.1; -; Genomic_DNA.
DR RefSeq; WP_012019783.1; NC_009439.1.
DR AlphaFoldDB; A4XZ97; -.
DR SMR; A4XZ97; -.
DR STRING; 399739.Pmen_3916; -.
DR PRIDE; A4XZ97; -.
DR EnsemblBacteria; ABP86663; ABP86663; Pmen_3916.
DR KEGG; pmy:Pmen_3916; -.
DR PATRIC; fig|399739.8.peg.3969; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_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..1357
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000051974"
SQ SEQUENCE 1357 AA; 150752 MW; C0E1F6376A329A1F CRC64;
MAYSYTEKKR IRKDFSKLPD VMDVPYLLAI QLDSYREFLQ QGVSKEQFRD IGLHAAFKSV
FPIISYSGNA ALEYVGYRLG EPAFDVKECV LRGVTFAVPL RVKVRLIIFD KESSNKAIKD
IKEQEVYMGE IPLMTENGTF VINGTERVIV SQLHRSPGVF FDHDRGKTHS SGKLLYSARI
IPYRGSWLDF EFDPKDAVFV RIDRRRKLPA SVLLRALGYS TEEVLDAFYD TNVFHVKNES
LSLELVPQRL RGEVAVLDIK DASGKVIVEQ GRRITARHIN QLDKAGIKEL EVPLDYVIGR
TTAKAIVHPA TGEIIAECNT ELTADLLAKM AKANVVRFET LYTNDIDCGP FISDTLKIDS
TTNQLEALVE IYRMMRPGEP PTKDAAETLF NNLFFSAERY DLSAVGRMKF NRRIGRTEIE
GSGVLSKEDI VAVLKTLVDI RNGKGIVDDI DHLGNRRVRC VGEMAENQFR VGLVRVERAV
KERLSMAESE GLMPQDLINA KPVAAAVKEF FGSSQLSQFM DQNNPLSEIT HKRRVSALGP
GGLTRERAGF EVRDVHPTHY GRVCPIETPE GPNIGLINSL AAYARTNQYG FLESPYRVVK
EGKVTDEIVF LSAIEEADHV IAQASATLND KGELVDELVA VRHLNEFTVK APEDVTLMDV
SPKQVVSVAA SLIPFLEHDD ANRALMGSNM QRQAVPTLRA DKPLVGTGME RNVARDSGVC
VVARRGGVID SVDASRIVVR VNDDEVETGE AGVDIYNLTK YTRSNQNTCI NQRPLVSKGD
QVARGDIMAD GPSTDMGELA LGQNMRVAFM PWNGFNFEDS ICLSERVVQE DRFTTIHIQE
LTCVARDTKL GPEEISSDIP NVGEAALNKL DEAGIVYVGA EVGPGDILVG KVTPKGETQL
TPEEKLLRAI FGEKASDVKD TSLRVPTGTK GTVIDVQVFT RDGVERDSRA LAIEKQQLDE
IRKDLNEEFR IVEGATFERL RSALVGAIAE GGAGLKKGTA ITDEFLDGLE RGQWFKLRMA
DDALNEQLEK AQAYISDRRQ MLDDKFEDKK RKLQQGDDLA PGVLKIVKVY LAIRRRIQPG
DKMAGRHGNK GVVSVIMPVE DMPHDANGTP VDIVLNPLGV PSRMNVGQIL ETHLGLAAKG
LGEKINRMLE EQRKVAELRK FLAEIYNEIG GRQENLDEFS DNEILELAKN LKGGVPMATA
VFDGAKETEI KAMLKLADLP ESGQMRLFDG RTGNQFERPT TVGYMYMLKL NHLVDDKMHA
RSTGSYSLVT QQPLGGKAQF GGQRFGEMEV WALEAYGAAY TLQEMLTVKS DDVNGRTKMY
KNIVDGDHRM EPGMPESFNV LIKEIRSLGI DIDLETE
