RPOB_TRIEI
ID RPOB_TRIEI Reviewed; 1102 AA.
AC Q110H1;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=Tery_2939;
OS Trichodesmium erythraeum (strain IMS101).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC Microcoleaceae; Trichodesmium.
OX NCBI_TaxID=203124;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMS101;
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 Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Richardson P.;
RT "Complete sequence of Trichodesmium erythraeum IMS101.";
RL Submitted (JUN-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: In cyanobacteria the RNAP catalytic core is composed of 2
CC alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When a sigma
CC factor is associated with the core the holoenzyme is formed, which can
CC initiate transcription. {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; CP000393; ABG52103.1; -; Genomic_DNA.
DR RefSeq; WP_011612461.1; NC_008312.1.
DR AlphaFoldDB; Q110H1; -.
DR SMR; Q110H1; -.
DR STRING; 203124.Tery_2939; -.
DR EnsemblBacteria; ABG52103; ABG52103; Tery_2939.
DR KEGG; ter:Tery_2939; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_3; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
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; 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..1102
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300422"
FT REGION 1081..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1102 AA; 123704 MW; FC2840613374821A CRC64;
MTYQKLNVNT YSNLQIFNMP DLIEIQRASF RWFLEYGLIE ELDSYSPITD YTGKLELHFI
AKNYKLKQPK YSVEESKRRD SSYAVQMYVP TRLINKETGE IKEQEVFIGD LPLMTDRGTF
IINGAERVIV NQIVRSPGVY YKSETDKSGR RTYNASLIPN RGAWLKFETD KNDLVWVRID
KTRKLSAQVL LKALGLGDSE IFDSLRHPDY FQKTIEKEGQ YGEEEALLEL YRKLRPGEPP
TIAGGEQLLH SRFFDQKRYD LGQVGRYKLN NKLRLNLPNT VRVLTKEDIL ASIDYLINLE
YDIGQTDDID HLGNRRVRSV GELLQNQIRV GLNRLERIIR ERMTVSESET LTPTSLVNPK
PLVAAIKEFF GSSQLSQFMD QTNPLAELTH KRRISALGPG GLTRERAGFA VRDIHPSHYG
RICPIETPEG PNAGLIGSLA NHAKVNSYGF IETPYYPVEN GRVLRDRTPI YMTADAEDDL
RVAPGDIMTD AEGKILGDVV PVRYRQDFTT TNPQQVDYVA VSPVQVVSVA TSLIPFLEHD
DANRALMGSN MQRQAVPLLN PDRPLVGTGL EPQAARDSGM VVVTRTDGEV SYVDSTKISV
IDKEGNQADY PLCKYQRSNQ DTCLNQRPLV FEGDQVVAGQ VLADGSSTEG AELALGQNVL
VAYMPWEGYN YEDAILISER LVYDDVYTSI HIEKFEIEAR QTKLGPEEIT REIPNVGEDG
LRNLDEQGII RVGAWVQSGD ILVGKVTPKG ESDQPPEEKL LRAIFGEKAR DVRDNSLRVP
NGEKGRIVDV RVFTREKGDE LPPGANMVVR VYVAQKRKIQ VGDKVAGRHG NKGIISRILP
IEDMPYLPDG TPIDVVLNPL GVPSRMNVGQ IFECLLGWAG EILSVRFKCV PFDEMHGPEK
SRETVHLMLK LARDNSGKDW VFDEKHPGKI WVFDGRTGER FDRPVTVGIA YMLKLVHLVD
DKIHARSTGP YSLVTQQPLG GKAQQGGQRF GEMEVWALEA FGAAYTLQEL LTVKSDDMQG
RNEALNAIVK GKAIPRPGTP ESFKVLMREL QSLCLDIAAH KVETVDDGTT QDVEVDLMAD
LPGKRTPSRP IYESLSTEGN QD
