RPOB_MAGMM
ID RPOB_MAGMM Reviewed; 1360 AA.
AC A0L5W6;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Mmc1_0840;
OS Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetococcus.
OX NCBI_TaxID=156889;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX PubMed=19465526; DOI=10.1128/aem.02874-08;
RA Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT coccus strain MC-1.";
RL Appl. Environ. Microbiol. 75:4835-4852(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; CP000471; ABK43359.1; -; Genomic_DNA.
DR RefSeq; WP_011712519.1; NC_008576.1.
DR AlphaFoldDB; A0L5W6; -.
DR SMR; A0L5W6; -.
DR STRING; 156889.Mmc1_0840; -.
DR PRIDE; A0L5W6; -.
DR EnsemblBacteria; ABK43359; ABK43359; Mmc1_0840.
DR KEGG; mgm:Mmc1_0840; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_5; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000002586; 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..1360
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300342"
SQ SEQUENCE 1360 AA; 152023 MW; 1D96DA5EF6F49F7E CRC64;
MALTFTEKKR LRKNFGRISS IIDIPNLISV QKESFVRFLQ TGTEFEKMKD TGLHGVFLSV
FPIHDYAGTV SLEYVSYALG EPKYDVDECL QRGMTFSAPL KVAFRLVIWD ENEETGTKTV
REIKEQDVYL GEIPLMTNTG TFIINGTERV IVSQMHRSPG VFFDHDRGKT HSSGKLLFSA
RVIPYRGSWL DFEFDPKDLL FARIDRRRKL PVTTLLRAMG MSSEQILERF YEIETFRKEG
VVWQKRMVPE RLMGNRLNYA IVHPESGEEI VKAKKRVTAR HIKKFEELGM DWLPVSQEEL
IGSFVARNMS DVMGEVVIEA GAEITEEMVQ YLEDGGIKEI DVLFIDGMSV GAYLRNTLAL
DKNSGQDEAL IDIYRMMRPG EPPTVDAAKA LFNNLFFNSD RYDLSTVGRL KMNSRLSLNT
ELHIRTLQHD DILGVVDILL KLKDGHGKVD DIDHLGNRRV RSVGELLENQ VRIGLVRMER
AIRERMSSAE ADQLVPHDVM NSKPFSAVIR EFFGSSQLSQ FMDQTNPLSE ITHKRRLSAL
GPGGMTRERA GFEVRDVHPT HYGRICPIET PEGPNIGLIN SLSTYARINE FGFIESPYRQ
VKEGTPIDQV DFLSAIDEEN YIIAQANAKL GDEASEEDAL IQCRHKLEFM VATPDRVNYQ
DVSPKQTVSV AASLIPFLEN DDANRALMGS NMQRQAVPLI KTDAPLVGTG IESVVARDSG
VTITARRTGV VDEVDAARIV VKADEEPGST EPGVDIYNLT KFSRSNQNTC INQVPLVKNG
ERVTAGDIIA DGPSTQIGEL ALGRNVLVAF MPWNGYNFED SILISERLVA EDVFTSIHID
EFEVMARDTK LGAEEITRDM PNVGEDALRN LDESGIIYVG AEVKPGDILV GKVTPKGETQ
LTPEEKLLRA IFGEKASDVR DTSLRLPPGV AGTVVDVRVF SRRGLEKDDR AKLIDQDEIA
LLRKDMAAER RIIERDADER IRNLMNGKPV RSAPGLQPGD HISQSWLDKS PSSHLRDVVL
DDDAITQQIE GIRHHVEKAA DRLKKRFESK VEKLERGDDL PPGVLKMVKV YIAVKRKLQP
GDKMAGRHGN KGVISKINPL EDMPYMANGT PVDIVLNPLG VPSRMNVGQI LETHLGWAAR
GMGFKIEEAL KQHRKGVADV LRRQFEEIYD NTRESAEIAA LSDDQLVDMA KNLQYGVPTA
TPVFDGAIES DISSWLNKAG LPTSGQIQLI DGRTGEPFDR HVTVGYIYML KLHHLVDDKI
HARSIGPYSL VTQQPLGGKA QFGGQRFGEM EVWALEAYGA AYTLQEMLTV KSDDVAGRTK
IYESIVKGDD TFEAGVPESF NVLVKELQAL ALDVTLQRDD
