RPOB_SYNWW
ID RPOB_SYNWW Reviewed; 1107 AA.
AC Q0AUH2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Swol_2341;
OS Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophomonas.
OX NCBI_TaxID=335541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2245B / Goettingen;
RX PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT metabolism and biohydrogen production.";
RL Environ. Microbiol. 12:2289-2301(2010).
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; CP000448; ABI69632.1; -; Genomic_DNA.
DR RefSeq; WP_011641716.1; NC_008346.1.
DR AlphaFoldDB; Q0AUH2; -.
DR SMR; Q0AUH2; -.
DR STRING; 335541.Swol_2341; -.
DR PRIDE; Q0AUH2; -.
DR EnsemblBacteria; ABI69632; ABI69632; Swol_2341.
DR KEGG; swo:Swol_2341; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000001968; 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; -; 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; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1107
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300421"
FT REGION 1062..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1076
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1107 AA; 124193 MW; 4F11BCC411890521 CRC64;
MAHLEQFGRV SRLSYSRIKE PVELPNLIQI QKNSYDWFLE HGLREALQEV FPISDFTGNL
ELGFLDYSMG EPKYSINECK ERDVSYQAPL KLKVRLTDKE NGEIKESEVY MGDLPLMTEK
GTFIINGAER VVVSQLVKSP GVYFNERMDV AGHPLFGATI IPNRGAWFEL EMDSAGLVYT
RIDKTRKIPV TVLLRALGYE SNEVILDMYD GDETIARTLE KDTSTNKKEA LIEFYRRLRP
GELATEDAAE QLLKNLFFDP RRYDMAAVGR YKVNKKLGLN IPPENRHLTL EDITATIGYL
LKLIKGEGKT DVIDHLGNRR LRSIGELLQN QFRTGLVRME RVVRERMSIH DVETLTPQVL
INIRPITAAV KEFFGSSQLS QFMDQTNPLA ELTHKRRLSA LGPGGLTRER AGFQVRDVHH
SHYGRICPIE TPEGPNIGLI GYLATFGQVN DFGFIETPYR KVDKKLGRVL NEIVYLSADE
EDEYYVAQAN APLDENGYFI EEKVEARYFE EILEIPKNRV DYMDVSPKQV FSVATALIPF
LENDDANRAL MGANMQRQAV PLVKTEAPIV GTGLEHKAAR DSGAVVIAKK AGTVKKASAS
RISIEKDDGT IDNYELLKFM RSNQGTCYNQ RPIVKVGERV EANEVIADGP STEQGELALG
RNVMVAFMPW EGYNYEDAIL ISEKLVKDDV FTSIHIEEYE CEARDTKLGS EEITRDIPNV
SEDMLKNLDD QGVIRVGAEV RPDDILVGKV TPKGETELTP EERLLRAIFG EKAREVRDSS
LRVPHGEAGK VVAVKRFSRE KGDELPPGVN QLVRVYIAQK RKISEGDKMA GRHGNKGVIS
RILPEEDMPF LEDGTPVEIV LNPLGVPSRM NIGQILECHM GWAARALGLN IATPVFDGAN
EEDIFTKLRE ASLLESGKTI LFDGRTGEKF KHEITVGYVY MLKLAHLVDD KIHARSIGPY
SLVTQQPLGG KAQFGGQRFG EMEVWALEAY GSSYTLQEIL TVKSDDVAGR LKTYESIVKG
ENIPEPGVPE GFKVLIKELQ SLALDVRILA GDDHEILIKD NDNEGNEKEK ARELGLDLPD
NPVGRMLEIT QPIENAEQDV ELKSSPK
