RPOB_MYCGE
ID RPOB_MYCGE Reviewed; 1390 AA.
AC P47583; Q49439; Q49441;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=MG341;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 533-644 AND 945-1067.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL J. Bacteriol. 175:7918-7930(1993).
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}.
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; L43967; AAC71566.1; -; Genomic_DNA.
DR EMBL; U01737; AAD10547.1; -; Genomic_DNA.
DR EMBL; U01735; AAD10545.1; -; Genomic_DNA.
DR PIR; G64237; G64237.
DR RefSeq; WP_009885798.1; NZ_AAGX01000006.1.
DR AlphaFoldDB; P47583; -.
DR SMR; P47583; -.
DR STRING; 243273.MG_341; -.
DR EnsemblBacteria; AAC71566; AAC71566; MG_341.
DR KEGG; mge:MG_341; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_14; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR BioCyc; MGEN243273:G1GJ2-428-MON; -.
DR Proteomes; UP000000807; 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; -; 2.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 2.
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..1390
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047919"
FT CONFLICT 1062
FT /note="H -> L (in Ref. 2; AAD10545)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1390 AA; 156331 MW; 4D1888A07680912C CRC64;
MSQKSNFFQK RYSPTATRRY YGKIETNFIQ PNLADIQIKS YQKFLDHDLE KLIASYFPIK
SPNDRYTINF RGLHRTEPER DEAQSRAQSK TYEVGIYADL ELVDNDKGTV KKARKSKKNI
ASNTNGVFLA SMPLITHDGV FIINGIEKFV ISQITRSPGI YMLTKSQLKL SNSRKRVQEG
YVCEVLPANG SVMLIYISNK KKIEDAFVQI LLRDAVREGA KIFPITTLLK AFGLNNREIL
KIFKNNEFIK RSLEAEIYNA KDFLSNVDPE IKNLLKEFRD GKTDLRRKGI ASDQKLRSLV
NEYVTLEKQY NALKQTSPND SSLTALELEM ENKMDSVITE RAAKHIVNEL SISLRDIENT
EECHEVSFHA LLCARFFRNK RYNLSNAGRY KVSRKLRLTE RIYQKTLACD LFLKDGKLLL
KKGTLLLKEE IDKIKQAAKN NEISFVNKMQ LTTDGKAVDL AKESLFYETI DVYITNDNLS
VSVPVIGIHN ENDLNKAMTL SDFIASISYV INLPYGIGKY DDIDHLGNKR VKLINELITA
KLESGFTRME RFLKEKLTIA DGVNRGQQIN EEGQVIEQGE KKELTIKSLI NSKPIQIVIK
DFFNTHQLTQ FLDHQNPLSE LSNKRRISAM GPGGISREDP NLDIRDVHYS QYGRICPIET
PEGMNIGLIM SLASFAKIDE NGFLMAPYRK IKAGVITDEV EYLTALREDE HIIAEISSLV
NISNDNKILD KEIIGRYRSM QGLYDPLKID YIDVAPHQVV SIGSSLIPFL ENDDSARALM
GTNMQRQAYP LIKPYAPAVG TGQEHKIASD SGLTMSSPCS GVVSYVDNSK IIITSDSSKK
ETVNLVKFER SNQNTCYNHK PIVEIGQRVN KDEIIVDGPA VNKSELALGQ NVLVAFTTWN
GYNYEDAIVI SERLVKEDIL TSLTINEYVA QCLSTKNGDE QITRDIPNVS DANKRYLDEN
GIIMVGAEVK EGDVLVGKVS PKGQVEVSPE EKLFKAIFPE SVQNVRDSSL KVSHGGDGIV
SAVKRFSIAN GDELNDGVIE MIKVYVVQKR KIQIGDKLAG RHGNKGVISK VVPIEDMPHL
EDGTPVDILL NPLGVPSRMN IGQIFETHLG YAAHKLAVRS LISSCFDQNK AKEFAIEINQ
PQARVERLIK GLKNQINDRN IKSEKEALEK LDNSDISLVL KEIGMSFDDL IYKIATPIFQ
GVNFLDLQDV MQEAGLDPQK NQGKFKLIDG RSGMPFERPI SLGIMYMMKL NHMVDDKIHA
RAVGPYSKIT QQPLGGKSQN GGQRFGEMEV WALEAYGAAY NLQELLTIKS DDVQGRNRAY
AAIVKGAAFP EPGIPESFKL LTKELQGLAL SVSFIYDDNT QQDSNNVSIL QSDGEQDEFF
NDFEFDTEGY
