RPOB_DESDA
ID RPOB_DESDA Reviewed; 1378 AA.
AC B8J1A8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=Ddes_1636;
OS Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=525146;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27774 / DSM 6949 / MB;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Hazen T.C.;
RT "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT ATCC 27774.";
RL Submitted (JAN-2009) 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; CP001358; ACL49535.1; -; Genomic_DNA.
DR RefSeq; WP_012625259.1; NC_011883.1.
DR AlphaFoldDB; B8J1A8; -.
DR SMR; B8J1A8; -.
DR STRING; 525146.Ddes_1636; -.
DR PRIDE; B8J1A8; -.
DR EnsemblBacteria; ACL49535; ACL49535; Ddes_1636.
DR KEGG; dds:Ddes_1636; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_7; -.
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; -; 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; 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..1378
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000165802"
FT REGION 1359..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1378 AA; 154130 MW; A3FDEE225DA6F385 CRC64;
MGQLTKQFGK IKISLPIPHL LNLQIDSYEK FLQEGVPEAE RRPDEGLEGV FHTVFPIEDF
NKTASLEFVS YEIGEPKYDQ AECISKGLTY EAPMRIKVRL VVYDADEASG NRTIRDIKEQ
DIYFGTLPLM TEKGTFIING TERVIVNQLQ RSPGIIFEHD GGKTHTSRKV LYSCRVIPMR
GSWLDFDFDH KDILYVRIDR RRKMPATILF KAMGMSKEQI LDYFYTQETY RLEERNTIFW
EVRKELYRKD NAYADIVDSE GNVIVKAGKP ITKRSWRLIC EAGIEAIEMR PDTLDGMFLA
GDVADPKTGE LLAEAADEIT PGLLDRMRDA GINRVSVLHT KGNDTSSSIR DTLMLDRIPD
QLKAQEEIYR RLRPSSPPTA EIAASFFDNL FRNPDYYDLS PVGRYKLNQR LSLDEPSDLR
TLTDNDILTA IKVLVHLKDS HGPADDIDHL GNRRVRLVGE LVENQYRIGL VRMERAIKER
MSLQEISTLM PHDLINPKPV AAVLKEFFGT SQLSQFMDQT NSLSEVTHKR RLSALGPGGL
TRERAGFEVR DVHTSHYGRI CPIETPEGPN IGLIVSLTTF AKVNDYGFIE TPYHVVREGR
VTDEVLHLDA SREGDQVVAQ ANALLDEQGN LVDEFVTVRV KGEVEMRHRD EVTLMDISPS
QMVSISAALI PFLEHDDANR ALMGSNMQRQ AVPLLRSEKP LVGTGMEVDV ARDSGACIVA
PADGKIEYVD ADRIVVAYEG DVYKKQGGVR AYDLLKYHKS NQNSCFGQKP SCHPGQIVKK
GQILADGPGI DDGELALGKN LVVAFMPWCG YNYEDSILIS ERTVKEDVFT SIHIEEFEVV
ARDTKLGPEE ITRDIPNVSE DMLRNLDESG IIRIGAAVKP DDILVGKITP KGETQLTPEE
KLLRAIFGEK ARDVKNTSLK VPPGVEGTII DVKVFNRRSG EKDDRTLAIE GHDTAVLDQK
EADHMRALTD RTRALLIPHV VGKQVAASLP GKKKGEVLVE AGAALTEEML ASLPVKKLSG
LFKSKEVNDA VAEILKPYDQ QVDYLHAIYD SKREKVTEGD DLPPGVIKMV KVHIAIKRKL
SVGDKMAGRH GNKGVVSCIL PEEDMPFFAD GRPVDIVLNP LGVPSRMNIG QIMETHLGWG
AKELGRQLAE LLDSGAAMQV LRDEVKSIFS SDDINALVDE MDDEEFKASV SKLRNGIVTK
TPVFDGATEE EIWSWMERAG LANDGKTTLY DGRTGEAFKN RVTTGVMYML KLHHLVDEKI
HARSTGPYSL VTQQPLGGKA QFGGQRLGEM EVWALEAYGA AYLLQEFLTV KSDDVTGRVK
MYEKIVKGDN FLEAGLPESF NVLVKELMSL GLNVTLHQEE GKKKPKRTGY MREREDEA
