RPOB_SPHAL
ID RPOB_SPHAL Reviewed; 1392 AA.
AC Q1GT23;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=Sala_1486;
OS Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
OS (Sphingomonas alaskensis).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=317655;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13593 / LMG 18877 / RB2256;
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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; CP000356; ABF53199.1; -; Genomic_DNA.
DR RefSeq; WP_011541779.1; NC_008048.1.
DR AlphaFoldDB; Q1GT23; -.
DR SMR; Q1GT23; -.
DR STRING; 317655.Sala_1486; -.
DR EnsemblBacteria; ABF53199; ABF53199; Sala_1486.
DR KEGG; sal:Sala_1486; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_5; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000006578; 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; 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; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1392
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300407"
FT REGION 1372..1392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1392
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1392 AA; 154115 MW; 2279106F2569F0B4 CRC64;
MATKAKSVGQ ALEATATKRI RKLFGNIHEA VEMPNLIEVQ RESYEQFLRS DPSIGYVSGL
EKTLRSVFPI RDFAGTAELD FVHYELEAPK YDVEECRQRG ITYAAPMKVT LRLIVFEVDS
ETDTRSVLDI KEQDVYMGDM PLMTENGTFF VNGTERVIVS QMHRSPGVLF DHDRGKTHSS
GKFLFAARVI PYRGSWLDFE FDAKDIVNVR IDRKRKLPVT SLLYALGMTG EEILNHFYDR
LVFERAENGW KVPFMVENWR GSKPAFDVVD AKTGEVVFAA GHKISPRLAN KAAKDGLDTL
LIPTEEIFGR YSAYDLINES TGEIYIEAGD EVSAENLEKL DAAGIDKLVL LDIDHNNTGP
WIRNTLKADK AEDRDQALSD IYRVMRPGEP PTRETAEALF AGLFFDPERY DLSAVGRVKL
NMRLGLDAED TVTTLRSEDI LAVVKELVNL KDGKGEIDDI DNLGNRRVRS VGELLENQYR
VGLLRMERAV KERMSSVDVS TVMPNDLINA KPAVAAVREF FGSSQLSQFM DQTNPLSEVT
HKRRVSALGP GGLTRERAGF EVRDVHPTHY GRICPIETPE GPNIGLINSL ATFARVNKYG
FIETPYRRVV DGKVTNEVVY LSAMEESKHT VAQANADLNP DGSFIDELIS AREAGEFLMA
PREQITLMDV SPKQLVSVAA SLIPFLENDD ANRALMGSNM QRQAVPLLRA EAPVVGTGME
ETVARDSGAA IAARRGGVID QVDATRIVIR ATDMVEPGKS GVDIYRLQKF QRSNQNTCIN
QRPLVKVGDV VRAGDIIADG PSTELGELAL GKNVLVAFMP WNGYNYEDSI LISERIVKDD
VFTSIHIEEF EVTARDTRLG PEDITRDIPN VGEEALRNLD EAGIVYIGAE VGPGDILAGK
ITPKGESPMT PEEKLLRAIF GEKASDVRDT SLRLPPGVSG TVVEVRVFNR HGIDKDERAI
AIEREEIERL KQDADDERAI LNRATFSSLK DLLVGQATSA VPKGLKKGDI VTEEMLVGLD
RADWWKLAVV DDKAQTALEA IKAQYDDAIK RINAKYEDRV EKLQRGDELA PGVLKMVKVF
VAVKRKLQPG DKMAGRHGNK GVISRILPVE DMPFLEDGTP VDIVLNPLGV PSRMNVGQIL
ETHLGWASRG LGQQVTRALE EWRDANPDAT GGEMPEAVRE KLEHVYGAEY VEDIRSRDAE
GIIELASNLK VGVPFATPVF DGAKEADVSN MLTLAGLDES GQSDLYDGRT GDKFDRKVTV
GYIYMLKLHH LVDDKIHARS IGPYSLVTQQ PLGGKAQFGG QRFGEMEVWA LQAYGAAYTL
QEMLTVKSDD VIGRTKVYEA IVKGDDTFEA GIPESFNVLV KEMRSLGLNV ELSSYAEEDP
DEGPEALPEA AE
