RPOB_NITWN
ID RPOB_NITWN Reviewed; 1380 AA.
AC Q3SSY0;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=Nwi_1350;
OS Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 /
OS NCIMB 11846 / Nb-255).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Nitrobacter.
OX NCBI_TaxID=323098;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255;
RX PubMed=16517654; DOI=10.1128/aem.72.3.2050-2063.2006;
RA Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L.,
RA Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J.,
RA Hickey W.J.;
RT "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium
RT Nitrobacter winogradskyi Nb-255.";
RL Appl. Environ. Microbiol. 72:2050-2063(2006).
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; CP000115; ABA04611.1; -; Genomic_DNA.
DR RefSeq; WP_011314629.1; NC_007406.1.
DR AlphaFoldDB; Q3SSY0; -.
DR SMR; Q3SSY0; -.
DR STRING; 323098.Nwi_1350; -.
DR PRIDE; Q3SSY0; -.
DR EnsemblBacteria; ABA04611; ABA04611; Nwi_1350.
DR KEGG; nwi:Nwi_1350; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_5; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000002531; 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..1380
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000224082"
SQ SEQUENCE 1380 AA; 154232 MW; E9002B52DB7B5139 CRC64;
MVQQTFTGRK RVRKFFGHIR EVAEMPNLIE VQKASYDQFL MVDEPEGGRL DEGLQAVFKS
VFPINDFSGA SQLEFVRYEF EAPKYDVDEC RQRGMTYAAP LKVTLRLIVF DIDEETGAKS
VKDIKEQDVY MGDIPLMTMN GTFVVNGTER VIVSQMHRSP GVFFDHDKGK THSSGKLLFA
ARVIPYRGSW LDIEFDAKDI VFARIDRRRK IPVTSLMFAL GLDGEEILST FYKKIIYKRA
KSGGGSDGWR VPYDPVRFRG YSTLNDLIDA DTGKVVLEAG KKLTVRAARQ LQEKGLKALR
MSDEELVGMY LAEDLVNPKT GEIYAEAGEE ITEKSLKALN EEGYKELPLL DIDHVNVGPY
IRNTLAADKN MTREDALFDI YRVMRPGEPP TLESAQNMFQ SLFFDAERYD LSAVGRVKMN
MRLDLDAPDT YRTLRKEDIL AVIKTLVDLR DGKGEIDDID HLGNRRVRSV GELMENQYRV
GLLRMERAIK ERMSSVDIDT VMPQDLINAK PAAAAVREFF GSSQLSQFMD QTNPLSEITH
KRRLSALGPG GLTRERAGFE VRDVHPTHYG RICPIETPEG PNIGLINSLA TFARVNKYGF
VETPYRKVKD GRVTDEVVYL SAMEEGRYHV AQANLPLDAR GRFTEDLVVC RHAGEVLPVT
PDKVDFMDVS PKQLVSVAAA LIPFLENDDA NRALMGSNMQ RQAVPLVRAE APFVGTGMEG
VVARDSGAAI AARRSGVIDQ IDATRVVIRA TEDLDPTKSG VDIYRLMKYQ RSNQSTCINQ
RPLVKVGDIV RKGDIIADGP STDLGELALG RNVLVAFMPW NGYNFEDSIL LSERIVKEDV
FTSIHIEEFE VMARDTKLGP EEITRDIPNV SEEALKSLDE AGIVYIGAEV RAGDILVGKI
TPKGESPMTP EEKLLRAIFG EKASDVRDTS LRVPPGVQGT IVEVRVFNRH GVDKDERALA
IEREEIERLA KDRDDEQAIL DRNVYGRLAD LLENRQGIAG PKGFKKDTKI TRAVLDEYPK
SQWWLFASPN DKLMAEIEAM RKQYDESKKG LEQRFLDKVE KLQRGDELPP GVMKMVKVFV
AVKRKIQPGD KMAGRHGNKG VVSKIVPIED MPFLEDGTHA DIVLNPLGVP SRMNVGQILE
THLGWACAGL GRRIGQAVDA YLASAKQETK PLKETLKKVY GDNETIKSLE DHELVELGRN
LRRGVPIATP VFDGAKEADI EQMLELAGMD KSGQSTVYDG RTGDPFDRKV TVGYIYMLKL
HHLVDDKIHA RSIGPYSLVT QQPLGGKAQF GGQRFGEMEV WALEAYGAAY TLQEMLTVKS
DDVAGRTKVY EAIVRGDDTF EAGIPESFNV LVKEMRSLGL NVDLHNSKIG DMMPTSEAAE