RPOB_DESHD
ID RPOB_DESHD Reviewed; 1115 AA.
AC B8G1V8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=Dhaf_0414;
OS Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=272564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10664 / DCB-2;
RX PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA Tiedje J.M.;
RT "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT anaerobe capable of dehalogenation and metal reduction.";
RL BMC Microbiol. 12:21-21(2012).
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; CP001336; ACL18481.1; -; Genomic_DNA.
DR RefSeq; WP_015942749.1; NC_011830.1.
DR AlphaFoldDB; B8G1V8; -.
DR SMR; B8G1V8; -.
DR PRIDE; B8G1V8; -.
DR EnsemblBacteria; ACL18481; ACL18481; Dhaf_0414.
DR KEGG; dhd:Dhaf_0414; -.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000007726; 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; Transcription;
KW Transferase.
FT CHAIN 1..1115
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000165803"
FT REGION 1084..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1115
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1115 AA; 125202 MW; A72B1CDAD8EA7CD4 CRC64;
MFYPVKVGTR ERWSYSRIRE VLDMPNLIEI QQNSYQWFLD EGLREMFRDI SPIQDFTGNL
VLEFIDYSLG EPKYEVEECK ERDVTYAAPL RVKVRLINKE TGEVKEQEVF MGDFPLMTTK
GTFIINGAER VIVSQLVRSP GVYYSESIDP SGKKVFGATV IPNRGAWLEF ETDVNDNIFV
RVDRTRKLPA TVLIRALGYA TNGQIAELFD DNEHIRITLE RDNTESAEEA LVEIYKRLRP
GEPPTVDSAR SLLEALFFDP KRYDLAKVGR YKLNKKLKLS VPTDVHHLTK EDIVASLRQM
LTLMSGEGHK DDIDHLGNRR LRSVGELLQN QFRIGLSRME RVVRERMTIQ DVDVITPQVL
INIRPVVAAI KEFFGSSQLS QFMDQTNPLA ELTHKRRLSA LGPGGLSRER AGFEVRDVHH
SHYGRMCPIE TPEGPNIGLI GSLSTYGRIN PYGFIEAPYR KVNNGQVTDQ IDYLTADEEE
KFVVAQANAP LTDDGHFIEE KIDGRHGPDF VLVAPERIDY MDVSPKQMVS IATALIPFLE
HDDANRALMG ANMQRQAVPL LRTDAPYVGT GMEYKAAKDS GVCVLASKDG TVERATAEDI
IIRHDDGTLE KHKLLKYLRS NQGTCINQRP IVMKNERVEA GQIIADGPST DHGELALGRN
VLIAFMTWEG YNYEDAILIS EKLVKEDYYT SIHIEEYEAD ARDTKLGPEE ITRDIPNVGE
DVLKDLDERG IIRIGAEVST GDILVGKVTP KGETELTAEE RLLRAIFGEK AREVRDTSLR
VPHGEAGKIV DVKVFTRENG DELAPGVNEL VRVYIAQKRK ISVGDKMAGR HGNKGVISRI
MKQEDMPFLP DGTPVEIVLN PLGVPSRMNI GQVMETHLGW AAKALGLRLA TPVFDGAQEE
DVFATLRKAG LPETGKTVLY DGRTGDPFDN KITVGYMYFL KLHHLVDDKI HARSTGPYSL
VTQQPLGGKA QFGGQRFGEM EVWALEAYGA AYTLQEILTV KSDDVVGRVK TYEAIVKGEN
IPEPGVPESF KVLIKELQSL GLDVRVLSEN DEEIEIREID EDVTETAKEL GIDLHEDLPA
PVIHEAGEGE DDEYFEEDEE AVDDEPMTFD DDDME
