RPOB_MARMM
ID RPOB_MARMM Reviewed; 1357 AA.
AC Q0ANP3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=Mmar10_1802;
OS Maricaulis maris (strain MCS10).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Maricaulales; Maricaulaceae;
OC Maricaulis.
OX NCBI_TaxID=394221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCS10;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P.,
RA Stephens C., Richardson P.;
RT "Complete sequence of Maricaulis maris MCS10.";
RL Submitted (AUG-2006) 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; CP000449; ABI66094.1; -; Genomic_DNA.
DR RefSeq; WP_011643740.1; NC_008347.1.
DR AlphaFoldDB; Q0ANP3; -.
DR SMR; Q0ANP3; -.
DR STRING; 394221.Mmar10_1802; -.
DR PRIDE; Q0ANP3; -.
DR EnsemblBacteria; ABI66094; ABI66094; Mmar10_1802.
DR KEGG; mmr:Mmar10_1802; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_5; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000001964; 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..1357
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300343"
SQ SEQUENCE 1357 AA; 150306 MW; 83337DA3A02A0E06 CRC64;
MGLSFTGKKR IRKSFGRIPE TVAMPNLIEV QKSSYEHFLM KEVPAAERDD TGMQAVFKSV
FPVKDFAERA VLDFVSYEFE PPKFDVEECQ QRDMTFAAPL KVKMRLIVFD VDEETGARSV
KDIKEQDVYM GDIPLMTDKG TFVVNGTERV IVSQMHRSPG VFFDHDRGKT HASGKYLFAA
RIIPYRGSWL DFEFDAKDVV HMRLDRRRKL PATTLLYALG LDKEEILSTF YDTVTYKASK
KGWTVPYVKE RWRGVKPARD LVDAKTGDII APAGKKISAR AANKFADDGL AALLVSDEHL
LGGYLADDMV NLETGEIFAE AGDEMSEEIL ETLKDTGVKE LNLLDIDPAT GVGPYIRATL
AADKNDSREQ ALVDIYRVMR PGEPPTPETA EAMFQGLFFD SERYDLSAVG RVKMNMRLDL
DAPDDMRTLR KEDILAVLKT LVGLRDGRGE IDDIDNLGNR RVRSVGELME NQYRIGLLRM
ERAIKERMSS VDIETVMPHD LVNAKPAAAA VREFFGSSQL SQFMDQTNPL SEVTHKRRLS
ALGPGGLTRE RAGFEVRDVH PTHYGRICPI ETPEGPNIGL INSLSTFARV NKYGFIESPY
RKVENGKLTD QVDYLSAMQE SRYSIAQANA HVTESGELDN EFVNCRVAGD VTLVPREDVE
YIDVSPKQVV SVAAALIPFL ENDDANRALM GSNMQRQAVP LVKAEAPLVG TGMESIVARD
SGAAIAARRT GVIEQVDATR IVIRATEDLD AAKSGVDIYR LSKFQRSNQS TCINQRPIVR
VGDQVHAGDI IADGPSTDLG ELALGRNVVV AFMPWNGYNF EDSILISERI VRDDVFTSIH
LEEFEIAARD TKLGPEEITR DIPNVGEEAL RNLDEAGIVA VGAEVAAGDI LVGKVTPKGE
SPMTPEEKLL RAIFGEKASD VRDTSLRMPS GATGTVVEVR VFNRHGVDKD ERAISIEREE
IERLGKDRDD ELAILERNIY QRLGDLLLGK TAVSGPRGFA KGKVSQDALD ETPRSGWWRI
GLDDEKAMAE VEALQKQYDD SKARLDRRFE DKVDKLQRGD EMPPGVMKMV KVFVAVKRKL
QPGDKMAGRH GNKGVISKIN PIEDMPFLAN GEAVDIVLNP LGVPSRMNVG QILETHLGWA
CRGLGKQLGE AYDAYKRDGS TATLRSELDR VYEGDELPET DSDIAELGLN LSNGVPIATP
VFDGAREPDV AHWLTKAGFD PSGQSTLYDG QTGEPFRRKV TVGVKHLLKL HHLVDDKIHA
RSIGPYSLVT QQPLGGKAQF GGQRFGEMEV WALEAYGAAY TLQEMLTVKS DDVAGRTKVY
EAIVRGDDTF EAGVPESFNV LVKEMRSLGL NVELKNG
