RPOA_THEAQ
ID RPOA_THEAQ Reviewed; 314 AA.
AC Q9KWU8;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
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;
OS Thermus aquaticus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=271;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND X-RAY CRYSTALLOGRAPHY (3.3
RP ANGSTROMS).
RX PubMed=10499798; DOI=10.1016/s0092-8674(00)81515-9;
RA Zhang G., Campbell E.A., Minakhin L., Richter C., Severinov K., Darst S.A.;
RT "Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A
RT resolution.";
RL Cell 98:811-824(1999).
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.
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; Y19222; CAB65464.2; -; Genomic_DNA.
DR PDB; 1HQM; X-ray; 3.30 A; A/B=1-314.
DR PDB; 1I6V; X-ray; 3.30 A; A/B=1-314.
DR PDB; 1L9U; X-ray; 4.00 A; A/B/J/K=1-314.
DR PDB; 1L9Z; X-ray; 6.50 A; A/B=1-314.
DR PDB; 1YNJ; X-ray; 3.20 A; A/B=1-314.
DR PDB; 1YNN; X-ray; 3.30 A; A/B=1-314.
DR PDB; 2GHO; X-ray; 5.00 A; A/B=1-314.
DR PDB; 4XLN; X-ray; 4.00 A; A/B/G/H=1-314.
DR PDB; 4XLP; X-ray; 4.00 A; A/B/G/H=1-314.
DR PDB; 4XLQ; X-ray; 4.60 A; A/B/G/H=1-314.
DR PDB; 4XLR; X-ray; 4.30 A; A/B/G/H=1-314.
DR PDB; 4XLS; X-ray; 4.01 A; A/B/G/H=1-314.
DR PDB; 5TJG; X-ray; 2.60 A; A/B=1-314.
DR PDBsum; 1HQM; -.
DR PDBsum; 1I6V; -.
DR PDBsum; 1L9U; -.
DR PDBsum; 1L9Z; -.
DR PDBsum; 1YNJ; -.
DR PDBsum; 1YNN; -.
DR PDBsum; 2GHO; -.
DR PDBsum; 4XLN; -.
DR PDBsum; 4XLP; -.
DR PDBsum; 4XLQ; -.
DR PDBsum; 4XLR; -.
DR PDBsum; 4XLS; -.
DR PDBsum; 5TJG; -.
DR AlphaFoldDB; Q9KWU8; -.
DR SMR; Q9KWU8; -.
DR EvolutionaryTrace; Q9KWU8; -.
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 Transcription; Transferase.
FT CHAIN 1..314
FT /note="DNA-directed RNA polymerase subunit alpha"
FT /id="PRO_0000175405"
FT REGION 1..229
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT REGION 246..314
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT STRAND 10..16
FT /evidence="ECO:0007829|PDB:5TJG"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:5TJG"
FT STRAND 20..28
FT /evidence="ECO:0007829|PDB:5TJG"
FT HELIX 32..47
FT /evidence="ECO:0007829|PDB:5TJG"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:5TJG"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:5TJG"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:5TJG"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:5TJG"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:5TJG"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:5TJG"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:5TJG"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:5TJG"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:5TJG"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:5TJG"
FT STRAND 138..147
FT /evidence="ECO:0007829|PDB:5TJG"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:5TJG"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:5TJG"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:1YNJ"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:5TJG"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:5TJG"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:5TJG"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:5TJG"
FT HELIX 207..222
FT /evidence="ECO:0007829|PDB:5TJG"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:5TJG"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:5TJG"
SQ SEQUENCE 314 AA; 34787 MW; F2D0AB716619A3F0 CRC64;
MLESKLKAPV FTATTQGDHY GEFVLEPLER GFGVTLGNPL RRILLSSIPG TAVTSVYIED
VLHEFSTIPG VKEDVVEIIL NLKELVVRFL DPKMASTTLI LRAEGPKEVR AGDFTPSADV
EIMNPDLHIA TLEEGGKLYM EVRVDRGVGY VPAERHGIKD RINAIPVDAI FSPVRRVAFQ
VEDTRLGQRT DLDKLTLRIW TDGSVTPLEA LNQAVAILKE HLNYFANPEA SLLPTPEVSK
GEKRESAEED LDLPLEELGL STRVLHSLKE EGIESVRALL ALNLKDLRNI PGIGERSLEE
IRQALAKKGF TLKE
