RPOA_THET8
ID RPOA_THET8 Reviewed; 315 AA.
AC Q5SHR6;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=DNA-directed RNA polymerase subunit alpha;
DE Short=RNAP subunit alpha;
DE EC=2.7.7.6;
DE AltName: Full=RNA polymerase subunit alpha;
DE AltName: Full=Transcriptase subunit alpha;
GN Name=rpoA; OrderedLocusNames=TTHA1664;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9880810; DOI=10.1093/oxfordjournals.jbchem.a022251;
RA Wada T., Yamazaki T., Kuramitsu S., Kyogoku Y.;
RT "Cloning of the RNA polymerase alpha subunit gene from Thermus thermophilus
RT HB8 and characterization of the protein.";
RL J. Biochem. 125:143-150(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) 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 -!- 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;
CC -!- SUBUNIT: Homodimer. The RNAP catalytic core consists of 2 alpha, 1
CC beta, 1 beta' and 1 omega subunit. When a sigma factor is associated
CC with the core the holoenzyme is formed, which can initiate
CC transcription (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q5SHR6; Q8RQE8: rpoC; NbExp=4; IntAct=EBI-2106870, EBI-2106930;
CC Q5SHR6; Q53W63: TTHB099; NbExp=2; IntAct=EBI-2106870, EBI-16208148;
CC -!- DOMAIN: The N-terminal domain is essential for RNAP assembly and basal
CC transcription, whereas the C-terminal domain is involved in interaction
CC with transcriptional regulators and with upstream promoter elements.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC {ECO:0000305}.
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DR EMBL; AB024328; BAA75549.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD71487.1; -; Genomic_DNA.
DR RefSeq; WP_011173698.1; NC_006461.1.
DR RefSeq; YP_144930.1; NC_006461.1.
DR PDB; 1ZYR; X-ray; 3.00 A; A/B/K/L=1-315.
DR PDB; 2A68; X-ray; 2.50 A; A/B/K/L=1-315.
DR PDB; 2A69; X-ray; 2.50 A; A/B/K/L=1-315.
DR PDB; 2A6E; X-ray; 2.80 A; A/B/K/L=1-315.
DR PDB; 2A6H; X-ray; 2.40 A; A/B/K/L=1-315.
DR PDB; 2BE5; X-ray; 2.40 A; A/B/K/L=1-315.
DR PDB; 2CW0; X-ray; 3.30 A; A/B/K/L=1-315.
DR PDB; 2O5I; X-ray; 2.50 A; A/B/K/L=1-315.
DR PDB; 2O5J; X-ray; 3.00 A; A/B/K/L=1-315.
DR PDB; 3AOH; X-ray; 4.10 A; A/B/F/G/K/L=1-315.
DR PDB; 3AOI; X-ray; 4.30 A; A/B/F/G/K/L=1-315.
DR PDB; 3DXJ; X-ray; 3.00 A; A/B/K/L=1-315.
DR PDB; 3WOD; X-ray; 3.60 A; A/B=1-315.
DR PDB; 4G7H; X-ray; 2.90 A; A/B/K/L=1-315.
DR PDB; 4G7O; X-ray; 2.99 A; A/B/K/L=1-315.
DR PDB; 4G7Z; X-ray; 3.82 A; A/B/K/L=1-315.
DR PDB; 4GZY; X-ray; 3.51 A; A/B=1-315.
DR PDB; 4GZZ; X-ray; 4.29 A; A/B=1-315.
DR PDB; 4MQ9; X-ray; 3.35 A; A/B=1-314.
DR PDB; 4OIN; X-ray; 2.80 A; A/B=1-315.
DR PDB; 4OIO; X-ray; 3.10 A; A/B=1-315.
DR PDB; 4OIP; X-ray; 3.40 A; A/B=1-315.
DR PDB; 4OIQ; X-ray; 3.62 A; A/B=1-315.
DR PDB; 4OIR; X-ray; 3.10 A; A/B=1-305.
DR PDB; 4WQS; X-ray; 4.31 A; A/B/K/L=1-315.
DR PDB; 4WQT; X-ray; 4.40 A; A/B/F/G/K/L=1-315.
DR PDB; 5D4C; X-ray; 3.28 A; A/B/K/L=1-315.
DR PDB; 5D4D; X-ray; 3.00 A; A/B/K/L=1-315.
DR PDB; 5D4E; X-ray; 3.08 A; A/B/K/L=1-315.
DR PDB; 5E17; X-ray; 3.20 A; A/B=1-315.
DR PDB; 5E18; X-ray; 3.30 A; A/B=1-315.
DR PDB; 5I2D; X-ray; 4.41 A; A/B/L/M=1-315.
DR PDB; 5TMC; X-ray; 2.71 A; A/B=1-315.
DR PDB; 5TMF; X-ray; 3.00 A; A/B=1-315.
DR PDB; 5VO8; X-ray; 3.30 A; A/B=1-315.
DR PDB; 5X21; X-ray; 3.32 A; A/B=1-315.
DR PDB; 5X22; X-ray; 3.35 A; A/B/K/L=1-315.
DR PDB; 5XJ0; X-ray; 4.00 A; A/B=1-315.
DR PDB; 6ASG; X-ray; 3.80 A; A/B=1-315.
DR PDB; 6KQD; X-ray; 3.30 A; A/B/K/L=1-315.
DR PDB; 6KQE; X-ray; 3.30 A; A/B=1-315.
DR PDB; 6KQF; X-ray; 2.45 A; A/B=1-315.
DR PDB; 6KQG; X-ray; 2.78 A; A/B=1-315.
DR PDB; 6KQH; X-ray; 3.18 A; A/B=1-315.
DR PDB; 6KQL; X-ray; 2.89 A; A/B=1-315.
DR PDB; 6KQM; X-ray; 3.20 A; A/B=1-315.
DR PDB; 6KQN; X-ray; 3.49 A; A/B=1-315.
DR PDB; 6L74; X-ray; 3.12 A; A/B=1-315.
DR PDB; 6LTS; X-ray; 3.45 A; A/B=1-315.
DR PDB; 6M6A; EM; 5.00 A; A/B=1-315.
DR PDB; 6M6B; EM; 4.10 A; A/B=1-315.
DR PDB; 6M6C; EM; 3.10 A; A/B=1-315.
DR PDB; 6OVR; X-ray; 2.84 A; A/B=1-315.
DR PDB; 6OVY; X-ray; 3.00 A; A/B=1-315.
DR PDB; 6OW3; X-ray; 2.77 A; A/B=1-315.
DR PDB; 6OY6; X-ray; 3.10 A; A/B=1-315.
DR PDB; 6OY7; X-ray; 3.04 A; A/B=1-315.
DR PDB; 6P70; X-ray; 3.05 A; A/B=1-315.
DR PDB; 6P71; X-ray; 2.92 A; A/B=1-315.
DR PDB; 6WOX; X-ray; 3.14 A; A/B=1-315.
DR PDB; 6WOY; X-ray; 3.00 A; A/B=1-315.
DR PDB; 7EH0; X-ray; 2.81 A; A/B=1-315.
DR PDB; 7EH1; X-ray; 2.90 A; A/B=1-315.
DR PDB; 7EH2; X-ray; 3.34 A; A/B/K/L=1-315.
DR PDB; 7MLB; X-ray; 3.60 A; A/B=1-315.
DR PDB; 7MLI; X-ray; 3.60 A; A/B=1-315.
DR PDB; 7MLJ; X-ray; 3.75 A; A/B=1-315.
DR PDB; 7RDQ; EM; 3.00 A; A/B=1-315.
DR PDBsum; 1ZYR; -.
DR PDBsum; 2A68; -.
DR PDBsum; 2A69; -.
DR PDBsum; 2A6E; -.
DR PDBsum; 2A6H; -.
DR PDBsum; 2BE5; -.
DR PDBsum; 2CW0; -.
DR PDBsum; 2O5I; -.
DR PDBsum; 2O5J; -.
DR PDBsum; 3AOH; -.
DR PDBsum; 3AOI; -.
DR PDBsum; 3DXJ; -.
DR PDBsum; 3WOD; -.
DR PDBsum; 4G7H; -.
DR PDBsum; 4G7O; -.
DR PDBsum; 4G7Z; -.
DR PDBsum; 4GZY; -.
DR PDBsum; 4GZZ; -.
DR PDBsum; 4MQ9; -.
DR PDBsum; 4OIN; -.
DR PDBsum; 4OIO; -.
DR PDBsum; 4OIP; -.
DR PDBsum; 4OIQ; -.
DR PDBsum; 4OIR; -.
DR PDBsum; 4WQS; -.
DR PDBsum; 4WQT; -.
DR PDBsum; 5D4C; -.
DR PDBsum; 5D4D; -.
DR PDBsum; 5D4E; -.
DR PDBsum; 5E17; -.
DR PDBsum; 5E18; -.
DR PDBsum; 5I2D; -.
DR PDBsum; 5TMC; -.
DR PDBsum; 5TMF; -.
DR PDBsum; 5VO8; -.
DR PDBsum; 5X21; -.
DR PDBsum; 5X22; -.
DR PDBsum; 5XJ0; -.
DR PDBsum; 6ASG; -.
DR PDBsum; 6KQD; -.
DR PDBsum; 6KQE; -.
DR PDBsum; 6KQF; -.
DR PDBsum; 6KQG; -.
DR PDBsum; 6KQH; -.
DR PDBsum; 6KQL; -.
DR PDBsum; 6KQM; -.
DR PDBsum; 6KQN; -.
DR PDBsum; 6L74; -.
DR PDBsum; 6LTS; -.
DR PDBsum; 6M6A; -.
DR PDBsum; 6M6B; -.
DR PDBsum; 6M6C; -.
DR PDBsum; 6OVR; -.
DR PDBsum; 6OVY; -.
DR PDBsum; 6OW3; -.
DR PDBsum; 6OY6; -.
DR PDBsum; 6OY7; -.
DR PDBsum; 6P70; -.
DR PDBsum; 6P71; -.
DR PDBsum; 6WOX; -.
DR PDBsum; 6WOY; -.
DR PDBsum; 7EH0; -.
DR PDBsum; 7EH1; -.
DR PDBsum; 7EH2; -.
DR PDBsum; 7MLB; -.
DR PDBsum; 7MLI; -.
DR PDBsum; 7MLJ; -.
DR PDBsum; 7RDQ; -.
DR AlphaFoldDB; Q5SHR6; -.
DR BMRB; Q5SHR6; -.
DR SMR; Q5SHR6; -.
DR DIP; DIP-47009N; -.
DR IntAct; Q5SHR6; 6.
DR STRING; 300852.55773046; -.
DR DrugBank; DB08266; Methyl [(1E,5R)-5-{3-[(2E,4E)-2,5-dimethyl-2,4-octadienoyl]-2,4-dioxo-3,4-dihydro-2H-pyran-6-yl}hexylidene]carbamate.
DR EnsemblBacteria; BAD71487; BAD71487; BAD71487.
DR GeneID; 3169128; -.
DR KEGG; ttj:TTHA1664; -.
DR PATRIC; fig|300852.9.peg.1634; -.
DR eggNOG; COG0202; Bacteria.
DR HOGENOM; CLU_053084_0_1_0; -.
DR OMA; LMKFRNF; -.
DR PhylomeDB; Q5SHR6; -.
DR BRENDA; 2.7.7.6; 2305.
DR EvolutionaryTrace; Q5SHR6; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 2.170.120.12; -; 1.
DR Gene3D; 3.30.1360.10; -; 1.
DR HAMAP; MF_00059; RNApol_bact_RpoA; 1.
DR InterPro; IPR011262; DNA-dir_RNA_pol_insert.
DR InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3.
DR InterPro; IPR011773; DNA-dir_RpoA.
DR InterPro; IPR036603; RBP11-like.
DR InterPro; IPR011260; RNAP_asu_C.
DR InterPro; IPR036643; RNApol_insert_sf.
DR PANTHER; PTHR32108; PTHR32108; 1.
DR Pfam; PF01000; RNA_pol_A_bac; 1.
DR Pfam; PF03118; RNA_pol_A_CTD; 1.
DR Pfam; PF01193; RNA_pol_L; 1.
DR SMART; SM00662; RPOLD; 1.
DR SUPFAM; SSF55257; SSF55257; 1.
DR SUPFAM; SSF56553; SSF56553; 1.
DR TIGRFAMs; TIGR02027; rpoA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Nucleotidyltransferase;
KW Reference proteome; Transcription; Transferase.
FT CHAIN 1..315
FT /note="DNA-directed RNA polymerase subunit alpha"
FT /id="PRO_0000175408"
FT REGION 1..229
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT /evidence="ECO:0000250"
FT REGION 247..315
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000250"
FT TURN 4..6
FT /evidence="ECO:0007829|PDB:2A6H"
FT STRAND 10..16
FT /evidence="ECO:0007829|PDB:2A6H"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:2A6H"
FT STRAND 20..28
FT /evidence="ECO:0007829|PDB:2A6H"
FT HELIX 33..46
FT /evidence="ECO:0007829|PDB:2A6H"
FT STRAND 49..60
FT /evidence="ECO:0007829|PDB:2A6H"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6KQF"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:2A6H"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:2A6H"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:2A6H"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1ZYR"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:2CW0"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:2A6H"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:2A6H"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2A6H"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:2A6H"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:2A6H"
FT STRAND 137..151
FT /evidence="ECO:0007829|PDB:2A6H"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:2A6H"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:5TMC"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:5TMF"
FT STRAND 174..183
FT /evidence="ECO:0007829|PDB:2A6H"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:4G7H"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:2A6H"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:2A6H"
FT HELIX 207..223
FT /evidence="ECO:0007829|PDB:2A6H"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:6WOY"
SQ SEQUENCE 315 AA; 35013 MW; F79D93B57526A1CB CRC64;
MLDSKLKAPV FTVRTQGREY GEFVLEPLER GFGVTLGNPL RRILLSSIPG TAVTSVYIED
VLHEFSTIPG VKEDVVEIIL NLKELVVRFL NPSLQTVTLL LKAEGPKEVK ARDFLPVADV
EIMNPDLHIA TLEEGGRLNM EVRVDRGVGY VPAEKHGIKD RINAIPVDAV FSPVRRVAFQ
VEDTRLGQRT DLDKLTLRIW TDGSVTPLEA LNQAVEILRE HLTYFSNPQA AAVAAPEEAK
EPEAPPEQEE ELDLPLEELG LSTRVLHSLK EEGIESVRAL LALNLKDLKN IPGIGERSLE
EIKEALEKKG FTLKE
