RPO2_THEAC
ID RPO2_THEAC Reviewed; 1195 AA.
AC Q03587;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo2 {ECO:0000305};
DE EC=2.7.7.6 {ECO:0000250|UniProtKB:P11513};
DE AltName: Full=DNA-directed RNA polymerase subunit B;
GN Name=rpo2 {ECO:0000305}; Synonyms=rpoB {ECO:0000303|PubMed:1408839};
GN OrderedLocusNames=Ta0390;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=1408839; DOI=10.1093/nar/20.19.5226;
RA Klenk H.-P., Renner O., Schwass V., Zillig W.;
RT "Nucleotide sequence of the genes encoding the subunits H, B, A' and A'' of
RT the DNA-dependent RNA polymerase and the initiator tRNA from Thermoplasma
RT acidophilum.";
RL Nucleic Acids Res. 20:5226-5226(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
CC -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC transcription of DNA into RNA using the four ribonucleoside
CC triphosphates as substrates. This subunit is involved in DNA promoter
CC recognition. {ECO:0000250|UniProtKB:B8YB55}.
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:0000250|UniProtKB:P11513};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:B8YB55};
CC Note=Binds 1 Zn(2+) per subunit. {ECO:0000250|UniProtKB:B8YB55};
CC -!- SUBUNIT: Part of the RNA polymerase complex.
CC {ECO:0000250|UniProtKB:B8YB55}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B8YB55}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000305}.
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DR EMBL; X68198; CAA48280.1; -; Genomic_DNA.
DR EMBL; AL445064; CAC11534.1; -; Genomic_DNA.
DR PIR; S26722; S26722.
DR RefSeq; WP_010900819.1; NC_002578.1.
DR AlphaFoldDB; Q03587; -.
DR SMR; Q03587; -.
DR STRING; 273075.Ta0390; -.
DR EnsemblBacteria; CAC11534; CAC11534; CAC11534.
DR GeneID; 1456006; -.
DR KEGG; tac:Ta0390; -.
DR eggNOG; arCOG01762; Archaea.
DR HOGENOM; CLU_000524_5_0_2; -.
DR OMA; RDLHGTH; -.
DR OrthoDB; 198at2157; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 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; 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; IPR007646; RNA_pol_Rpb2_4.
DR InterPro; IPR007647; RNA_pol_Rpb2_5.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR InterPro; IPR019969; RNAP_Rpo2.
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; PF04566; RNA_pol_Rpb2_4; 1.
DR Pfam; PF04567; RNA_pol_Rpb2_5; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR TIGRFAMs; TIGR03670; rpoB_arch; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA-binding; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1195
FT /note="DNA-directed RNA polymerase subunit Rpo2"
FT /id="PRO_0000048098"
FT REGION 894..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:B8YB55"
FT BINDING 1140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:B8YB55"
FT BINDING 1155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:B8YB55"
FT BINDING 1158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1195 AA; 134690 MW; 7C1A575F218CF43E CRC64;
MKEIVDAYFK KYGIVNHQLD SMNSFYATPD NPNSVMQQIV DETKVSDDAD PGYFVLDPAK
TGGHDIRIYY GRVRENGHYV GEQTIFIGKP EIKEASGASN QITPNEARLR DLNYLAPVTL
KLRIVEDGIE KGSEIIKVGD LPVMVRSKIC TLSEENLDQY IEKNNGPIGL SRREKLQYVG
EDPDDPGGYF IIGGSERVIV SLEDLAPNKI MVEWEDRYES KVEVSKVFSQ RGGFRALTSM
EKGTDGTINV SIPSVAGTVP LVILMKALGL ERDVDVHDAI ASVPEMEPII YSNIEDSKNP
KVLPPNGVNT TEDAISYLEK RFAAGQAKEF RDKKISQMLD HSLLPHLGDS PSDRIRKAIY
LGRMARSLLE LSLGIRKEDD KDHLANKRIK LAGDLMDELF RSAFQSVMKD LKYQLEKTYN
RKRGIKIRPA VRQDLLTQRV LHAMSTGNWI GGRTGVSQLL DRVSNLSTIS HLRRIISPLT
RTQPHFEARD LHPTQWGRIC PNETPEGQNC GLVKNAALLI NVTQGIDPDS VMEILKGMDV
REVLEESPKK GRVYLNGDFI GYHDDPRYLV SRIREERRSG RMSDEVNVRY DDNTNEVIVN
SDRGRLRRPL LILKDGKTVL DRTMIERLKH GEISFEDLVK QGAIEWLDAE EEEDTYVAVY
AYDIPEKCPH CNSYLYRSMV DWVNPGESEI TLECGFCHQR FNVPSKLSKE NTHLEIDPAM
ILGVVASIIP YPEHNSSPRI TIASAMAKQS LGFAQSNVRI RPDTRGHLLH YPQVPLVRTR
VMDYIHYDRR PAGQNFVVAV LSYEGYNIQD ALVINKAAIE RGLGRSTFFR TYSAEERRYP
GGQEDKFEIP THDIIGARAE EYYKNLDDSG IIFPEAYVEG SDVLIGKTSP PRFLEEGEER
LGPQRRRESS VTMRPNESGY VDNVFLTVSE SNSRVVKIKV RSERIPELGD KFASRHGQKG
VVGLVVPQED MPFTEDGIIP DLIFNPHSIP SRMTVGHILE MIGGKIASRT GRFIDGTIFS
GEPEKSLRDA LVKYGFRKSS TEVMYDGITG RRFKADIFVG VIYYQKLHHM VAGKFHARSR
GPVQILTRQP TEGRSRQGGL RFGEMERDTL IAHGAAMVIK DRLLDQSDGT VLYVCGNPSC
GHIAIYDRRK GTLRCPVCGN TGNIYPIETS YAFKLMRDEL ISLGVVMRLM LGDMK
