RPOB_AZOVD
ID RPOB_AZOVD Reviewed; 1358 AA.
AC C1DKK5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=Avin_06170;
OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=322710;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ / ATCC BAA-1303;
RX PubMed=19429624; DOI=10.1128/jb.00504-09;
RA Setubal J.C., Dos Santos P., Goldman B.S., Ertesvaag H., Espin G.,
RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA Dean D.R., Dixon R., Wood D.;
RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT to support diverse anaerobic metabolic processes.";
RL J. Bacteriol. 191:4534-4545(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; CP001157; ACO76868.1; -; Genomic_DNA.
DR RefSeq; WP_012699296.1; NC_012560.1.
DR AlphaFoldDB; C1DKK5; -.
DR SMR; C1DKK5; -.
DR STRING; 322710.Avin_06170; -.
DR EnsemblBacteria; ACO76868; ACO76868; Avin_06170.
DR KEGG; avn:Avin_06170; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_6; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000002424; 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; Transcription;
KW Transferase.
FT CHAIN 1..1358
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000214470"
SQ SEQUENCE 1358 AA; 150932 MW; C0B36D4C870C4F1C CRC64;
MAYSYTEKKR IRKDFSKLPD VMDVPYLLAI QLDSYREFLQ AGVSKDKLRD VGLHAAFKSV
FPIISYSGNA ALEYVGYRLG EPAFDVKECV LRGVTFAVPL RVKVRLIIFD KESSNKAIKD
IKEQEVYMGE IPLMTENGTF IVNGTERVIV SQLHRSPGVF FDHDRGKTHS SGKLLYSARI
IPYRGSWLDF EFDPKDAVFV RIDRRRKLPA SVLLRALGYS TEEVLDIFYD TNVFHVTEQG
LSLELVPQRL RGEIAVFDIK DASGKVIVEQ GRRITARHIN QLEKAGIKEL DVPLEYVLGR
TSAKVIVHPS TGEIIAECNS ELTQDLLVKI AKAQVVRIET LYTNDIDCGP FISDTLKIDS
TTNQLEALVE IYRMMRPGEP PTKDAAETLF NNLFFSAERY DLSAVGRMKF NRRIGREEIE
GAGVLSREDI VDVLKTLVDI RNGKGIVDDI DHLGNRRVRC VGEMAENQFR VGLVRVERAV
KERLSMAESE GLMPQDLINA KPVAAAVKEF FGSSQLSQFM DQNNPLSEIT HKRRVSALGP
GGLTRERAGF EVRDVHPTHY GRVCPIETPE GPNIGLINSL AAYARTNQYG FLESPYRVVK
EGQVTDEIVF LSAIEEADHV IAQASATLDE NGRLIDELVA VRHLNEFTVK APEDVTLMDV
SPRQVVSVAA SLIPFLEHDD ANRALMGSNM QRQAVPTLRA DKPLVGTGME RNVARDSGVC
VVARRGGVID SVDASRIVVR VNNDEVETGE AGVDIYNLTK YTRSNQNTCI NQRPLVSKGD
QVARGDIMAD GPSTDMGELA LGQNMRVAFM PWNGFNFEDS ICLSERVVQE DRFTTIHIQE
LTCVARDTKL GPEEITADIP NVGEAALNKL DEAGIVYVGA EVMAGDILVG KVTPKGETQL
TPEEKLLRAI FGEKASDVKD TSLRVPTGTK GTVIDVQVFT RDGVERDSRA LAIERMQLDE
IRKDLNEEFR IVEGATFERL RAALVGAVCE GGAGLKKGTE IDDGILDGLE RGQWFKLRMA
DDALNEQLEK AQAYLADRRQ LLDDKFEDKK RKLQQGDDLA PGVLKIVKVY LAIKRRIQPG
DKMAGRHGNK GVVSVIMPVE DMPYDANGTP VDIVLNPLGV PSRMNVGQIL ETHLGLAAKG
LGEKINRMLE EQRKVAELRQ FLGEVYNEIG GRQKEDLDSL SDSEILDLAS NLRGGVPMAT
PVFDGARETE IKAMLKLADL PESGQMRLFD GRTGNQFERP TTVGYMYMLK LNHLVDDKMH
ARSTGSYSLV TQQPLGGKAQ FGGQRFGEME VWALEAYGAA YTLQEMLTVK SDDVNGRTKM
YKNIVDGDHR MEAGMPESFN VLIKEIRSLG IDIELETE