RPOA_THETH
ID RPOA_THETH Reviewed; 315 AA.
AC Q9Z9H6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 127.
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 thermophilus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=274;
RN [1]
RP STRUCTURE BY NMR OF 247-315.
RX PubMed=10821859; DOI=10.1074/jbc.275.21.16057;
RA Wada T., Yamazaki T., Kyogoku Y.;
RT "The structure and the characteristic DNA binding property of the C-
RT terminal domain of the RNA polymerase alpha subunit from Thermus
RT thermophilus.";
RL J. Biol. Chem. 275:16057-16063(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=12000971; DOI=10.1038/nature752;
RA Vassylyev D.G., Sekine S., Laptenko O., Lee J., Vassylyeva M.N.,
RA Borukhov S., Yokoyama S.;
RT "Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 A
RT resolution.";
RL Nature 417:712-719(2002).
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}.
CC -!- CAUTION: The sequence shown here has been extracted from PDB entry
CC 1IW7. {ECO:0000305}.
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DR RefSeq; WP_011173698.1; NZ_AP019801.1.
DR PDB; 1DOQ; NMR; -; A=247-315.
DR PDB; 1IW7; X-ray; 2.60 A; A/B/K/L=1-315.
DR PDB; 1SMY; X-ray; 2.70 A; A/B/K/L=1-315.
DR PDB; 2BE5; X-ray; 2.40 A; A/B/K/L=1-315.
DR PDB; 2PPB; X-ray; 3.00 A; A/B/K/L=1-315.
DR PDB; 3EQL; X-ray; 2.70 A; A/B/K/L=1-315.
DR PDB; 4Q4Z; X-ray; 2.90 A; A/B=1-315.
DR PDB; 4Q5S; X-ray; 3.00 A; A/B=1-315.
DR PDBsum; 1DOQ; -.
DR PDBsum; 1IW7; -.
DR PDBsum; 1SMY; -.
DR PDBsum; 2BE5; -.
DR PDBsum; 2PPB; -.
DR PDBsum; 3EQL; -.
DR PDBsum; 4Q4Z; -.
DR PDBsum; 4Q5S; -.
DR AlphaFoldDB; Q9Z9H6; -.
DR BMRB; Q9Z9H6; -.
DR SMR; Q9Z9H6; -.
DR DIP; DIP-60256N; -.
DR IntAct; Q9Z9H6; 3.
DR DrugBank; DB08226; Myxopyronin B.
DR GeneID; 3169128; -.
DR EvolutionaryTrace; Q9Z9H6; -.
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..315
FT /note="DNA-directed RNA polymerase subunit alpha"
FT /id="PRO_0000175409"
FT REGION 1..229
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT REGION 247..315
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT TURN 4..6
FT /evidence="ECO:0007829|PDB:3EQL"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:3EQL"
FT STRAND 17..28
FT /evidence="ECO:0007829|PDB:3EQL"
FT HELIX 33..46
FT /evidence="ECO:0007829|PDB:3EQL"
FT STRAND 50..60
FT /evidence="ECO:0007829|PDB:3EQL"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:3EQL"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:3EQL"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:3EQL"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:3EQL"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:3EQL"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:3EQL"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:3EQL"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:3EQL"
FT STRAND 139..147
FT /evidence="ECO:0007829|PDB:3EQL"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:3EQL"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:3EQL"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:4Q5S"
FT STRAND 174..183
FT /evidence="ECO:0007829|PDB:3EQL"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:3EQL"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:3EQL"
FT HELIX 207..223
FT /evidence="ECO:0007829|PDB:3EQL"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:1DOQ"
FT HELIX 263..271
FT /evidence="ECO:0007829|PDB:1DOQ"
FT HELIX 277..282
FT /evidence="ECO:0007829|PDB:1DOQ"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:1DOQ"
FT HELIX 296..309
FT /evidence="ECO:0007829|PDB:1DOQ"
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
