RPOB_JANMA
ID RPOB_JANMA Reviewed; 1368 AA.
AC A6T3L3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 74.
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=mma_3420;
OS Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=375286;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marseille;
RX PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA Drancourt M.;
RT "Genome analysis of Minibacterium massiliensis highlights the convergent
RT evolution of water-living bacteria.";
RL PLoS Genet. 3:1454-1463(2007).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABR88926.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000269; ABR88926.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041296708.1; NC_009659.1.
DR AlphaFoldDB; A6T3L3; -.
DR SMR; A6T3L3; -.
DR STRING; 375286.mma_3420; -.
DR PRIDE; A6T3L3; -.
DR EnsemblBacteria; ABR88926; ABR88926; mma_3420.
DR KEGG; mms:mma_3420; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_4; -.
DR OrthoDB; 9601at2; -.
DR BioCyc; JSP375286:MMA_RS17680-MON; -.
DR Proteomes; UP000006388; 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..1368
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000329180"
SQ SEQUENCE 1368 AA; 152387 MW; 55451590EC232C0E CRC64;
MHYSFTEKKR IRKSFAKRAN VHNVPFLLAT QLESYHGFLQ EDKIPSQRKN EGLQSAFTSI
FPIVSHNGFA RLEFLSYVLG DPPFNIKECQ QRGLTYASPL RAKVRLVILD KESPTKPVVK
EMKEQEVYMG ELPLMTSTGS FVINGTERVI VSQLHRSPGV FFEHDRGKTH SSGKLLFSAR
IIPYRGSWLD YEFDPKDILF FRVDRRRKMP VTILLKAIGM TPEQILENFF VFDDFALHAD
GAEMAFVAER LRGEVARFDI TDKAGKVLVA KDKRINSKHV RDVEAAGIKN ISVPEDYLLG
RILAKNIVDK ETGEVIANAN DELTEDLLAR LREGKVTHIQ TLYTNDLDQG GYISQTLRMD
DTTDQMAAKV AIYRMMRPGE PPTEDSVEAL FNGLFYNADR YDLSAVGRMK FNRRIGRDEL
TGDMTLSNDD VLAVIKILVE LRNGRGEVDD IDHLGNRRVR CVGELAENQF RAGLVRVERA
VKERLGQAEA DNLMPHDLIN SKPISAAIRE FFGSSQLSQF MDQTNPLSEI THKRRVSALG
PGGLTRERAG FEVRDVHPTH YGRVCPIETP EGPNIGLINS LALYARLNEY GFLETPYRKV
EGSKITDQID YLSAIEEGRY IIAQANATID KSGALSDELV SAREAGETIL VSPERVQYMD
VAPGQVVSVA ASLIPFLEHD DANRALMGAN MQRQAVPCLR PEKAFVGTGI ERTVAVDSGT
TVQALRGGIV DYIDAGRVVI RVNDDEAQAG EVGVDIYNLI KYTRSNQNTN INQRPIVQVG
DRVAKHDVIA DGASTDLGEL ALGQNMLVAF MPWNGYNFED SILISEKVVA DDRYTSIHIE
ELSVVARDTK LGAEEITRDI SNLAENQLAR LDESGIVYIG AEVTAGDTLV GKVTPKGETQ
LTPEEKLLRA IFGEKASDVK DTSLRVPSGM VGTVIDVQVF TREGIPRDKR AQQIIDDELQ
RYRLDLNDQL RIVEGDAFQR LEKMLIGKVV NGGPKKIAKG AKITKEYLDD LDKYHWFDIR
PADDTSANAL EAIKESIAEK RHQFDLAFEE KRKKLTQGDE LPPGVQKMVK VYLAVKRRLQ
PGDKMAGRHG NKGVVSRILP IEDMPHMADG TPADVVLNPL GVPSRMNVGQ VLEVHLGWAA
KGLGLRIGEM LNAQVQIAEL RKFLAAIYNE SGKTEDLDSF SDAEILELAG NLKNGVPFAT
PVFDGADEGE TRRMLDLAYP DHIAKQLGMT ASKNQVTMYD GRTGEAFERT VTVGYMHYLK
LHHLVDDKMH ARSTGPYSLV TQQPLGGKAQ FGGQRFGEME VWALEAYGAS YVLQEMLTVK
SDDVNGRTKV YENLVKGDHV IDAGMPESFN VLVKEIRSLG IDIDLERD
