ID RPOA_ECOLI Reviewed; 329 AA. AC P0A7Z4; P00574; Q2M6W0; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 23-JAN-2007, entry version 26. DE DNA-directed RNA polymerase alpha chain (EC 2.7.7.6) (RNAP alpha DE subunit) (Transcriptase alpha chain) (RNA polymerase alpha subunit). GN Name=rpoA; Synonyms=pez, phs, sez; OrderedLocusNames=b3295, JW3257; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=77162615; PubMed=323055; DOI=10.1016/0014-5793(77)80131-2; RA Ovchinnikov Y.A., Lipkin V.M., Modyanov N.N., Chertov O.Y., RA Smirnov Y.V.; RT "Primary structure of alpha-subunit of DNA-dependent RNA polymerase RT from Escherichia coli."; RL FEBS Lett. 76:108-111(1977). RN [2] RP PROTEIN SEQUENCE. RA Modyanov N.N., Lipkin V.M., Smirnov Y.V., Shuvaeva T.M., RA Kocherginskaya S.A.; RT "The primary structure of alpha-subunit of DNA-dependent RNA RT polymerase from E. coli. V. The cyanogen bromide peptides."; RL Bioorg. Khim. 4:437-449(1978). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=84272255; PubMed=6379605; RA Meek D.W., Hayward R.S.; RT "Nucleotide sequence of the rpoA-rplQ DNA of Escherichia coli: a RT second regulatory binding site for protein S4?"; RL Nucleic Acids Res. 12:5813-5821(1984). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX MEDLINE=85242076; PubMed=2989779; RA Bedwell D.M., Davis G.R., Gosink M., Post L.E., Nomura M., Kestler H., RA Zengel J.M., Lindahl L.; RT "Nucleotide sequence of the alpha ribosomal protein operon of RT Escherichia coli."; RL Nucleic Acids Res. 13:3891-3903(1985). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (MUTANTS RPOA101 AND RPOA112). RX MEDLINE=91045051; PubMed=2235479; RA Igarashi K., Fujita N., Ishihama A.; RT "Sequence analysis of two temperature-sensitive mutations in the alpha RT subunit gene (rpoA) of Escherichia coli RNA polymerase."; RL Nucleic Acids Res. 18:5945-5948(1990). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-159. RX MEDLINE=80049646; PubMed=387752; RA Post L.E., Nomura M.; RT "Nucleotide sequence of the intercistronic region preceding the gene RT for RNA polymerase subunit alpha in Escherichia coli."; RL J. Biol. Chem. 254:10604-10606(1979). RN [9] RP PROTEIN SEQUENCE OF 1-19. RC STRAIN=K12 / EMG2; RX MEDLINE=97443975; PubMed=9298646; RA Link A.J., Robison K., Church G.M.; RT "Comparing the predicted and observed properties of proteins encoded RT in the genome of Escherichia coli K-12."; RL Electrophoresis 18:1259-1313(1997). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12. RC STRAIN=K12; RX MEDLINE=85267249; PubMed=3894886; DOI=10.1007/BF00330268; RA Schnier J., Isono S., Cumberlidge A.G., Isono K.; RT "Unstable mutations caused by regional tandem multiplications in the RT gene for ribosomal protein S4 show thermosensitivity in Escherichia RT coli."; RL Mol. Gen. Genet. 199:265-270(1985). RN [11] RP STRUCTURE BY NMR OF 233-349. RX MEDLINE=96095212; PubMed=7491496; RA Jeon Y.H., Negishi T., Shirakawa M., Yamazaki T., Fujita N., RA Ishihama A., Kyogoku Y.; RT "Solution structure of the activator contact domain of the RNA RT polymerase alpha subunit."; RL Science 270:1495-1497(1995). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-235. RX MEDLINE=98322352; PubMed=9657722; DOI=10.1126/science.281.5374.262; RA Zhang G., Darst S.A.; RT "Structure of the Escherichia coli RNA polymerase alpha subunit amino- RT terminal domain."; RL Science 281:262-266(1998). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. This subunit plays an important role in subunit CC assembly since its dimerization is the first step in the CC sequential assembly of subunits to form the holoenzyme. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). 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 CC associated with the core the holoenzyme is formed, which can CC initiate transcription. CC -!- INTERACTION: CC P0ABQ0:coaBC; NbExp=1; IntAct=EBI-544985, EBI-548929; CC -!- DOMAIN: The N-terminal domain is essential for RNAP assembly and CC basal transcription, whereas the C-terminal domain is involved in CC interaction with transcriptional regulators and with upstream CC promoter elements. CC -!- MISCELLANEOUS: Mutant rpoA112 blocks RNA polymerase assembly. CC -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J01685; AAA24577.1; -; Genomic_DNA. DR EMBL; X00766; CAA25337.1; -; Genomic_DNA. DR EMBL; X02543; CAA26395.1; -; Genomic_DNA. DR EMBL; U18997; AAA58092.1; -; Genomic_DNA. DR EMBL; X53843; CAA37838.1; -; Genomic_DNA. DR EMBL; X53844; CAA37839.1; -; Genomic_DNA. DR EMBL; U00096; AAC76320.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77996.1; -; Genomic_DNA. DR EMBL; V00353; CAA23646.1; -; Genomic_DNA. DR EMBL; M29822; AAA24590.1; -; Genomic_DNA. DR EMBL; M29823; AAA24592.1; -; Genomic_DNA. DR EMBL; M29824; AAA24594.1; -; Genomic_DNA. DR PIR; A22884; RNECA. DR PDB; 1BDF; X-ray; A/B/C/D=1-235. DR PDB; 1COO; NMR; @=233-329. DR PDB; 1LB2; X-ray; B/E=246-329. DR PDB; 1XS9; NMR; D=249-329. DR IntAct; P0A7Z4; -. DR SWISS-2DPAGE; P0A7Z4; COLI. DR ECO2DBASE; B040.7; 6TH EDITION. DR GenomeReviews; U00096_GR; b3295. DR GenomeReviews; AP009048_GR; JW3257. DR KEGG; ecj:JW3257; -. DR KEGG; eco:b3295; -. DR EchoBASE; EB0886; -. DR EcoGene; EG10893; rpoA. DR DrugBank; APRD00094; Rifabutin. DR LinkHub; P0A7Z4; -. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR HAMAP; MF_00059; -; 1. DR InterPro; IPR011260; RNAP_alpha_C. DR InterPro; IPR011261; RNAP_dimersation. DR InterPro; IPR011262; RNAP_insert. DR InterPro; IPR009025; RNAP_RBP11-like. DR InterPro; IPR011263; RNAP_RpoA_D_Rpb3. DR InterPro; IPR011773; RpoA. DR Gene3D; G3DSA:2.170.120.12; RNAP_insert; 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 ProDom; PD001179; RNAP_alpha_C; 1. DR SMART; SM00662; RPOLD; 1. DR TIGRFAMs; TIGR02027; rpoA; 1. KW 3D-structure; Complete proteome; Direct protein sequencing; KW DNA-directed RNA polymerase; Nucleotidyltransferase; Transcription; KW Transferase. FT CHAIN 1 329 DNA-directed RNA polymerase alpha chain. FT /FTId=PRO_0000175304. FT REGION 1 235 Alpha N-terminal domain (alpha-NTD). FT REGION 249 329 Alpha C-terminal domain (alpha-CTD). FT VARIANT 45 45 R -> C (in mutant rpoA112; temperature- FT sensitive). FT VARIANT 191 191 R -> C (in mutant rpoA101; temperature- FT sensitive). FT CONFLICT 208 208 N -> T (in Ref. 4). FT STRAND 13 32 FT TURN 33 34 FT HELIX 35 47 FT TURN 48 49 FT STRAND 54 61 FT TURN 62 63 FT TURN 67 68 FT TURN 72 73 FT STRAND 74 76 FT HELIX 78 86 FT TURN 87 87 FT STRAND 96 111 FT HELIX 112 114 FT STRAND 122 124 FT TURN 126 127 FT STRAND 129 133 FT TURN 136 137 FT STRAND 139 148 FT STRAND 151 153 FT HELIX 155 157 FT TURN 158 158 FT STRAND 179 186 FT STRAND 196 207 FT STRAND 209 211 FT HELIX 213 227 FT HELIX 228 231 FT TURN 252 254 FT HELIX 257 260 FT HELIX 264 272 FT TURN 273 274 FT HELIX 278 282 FT TURN 283 283 FT HELIX 286 291 FT TURN 293 294 FT HELIX 297 309 FT TURN 310 311 SQ SEQUENCE 329 AA; 36512 MW; 12A14B75A3CAEA19 CRC64; MQGSVTEFLK PRLVDIEQVS STHAKVTLEP LERGFGHTLG NALRRILLSS MPGCAVTEVE IDGVLHEYST KEGVQEDILE ILLNLKGLAV RVQGKDEVIL TLNKSGIGPV TAADITHDGD VEIVKPQHVI CHLTDENASI SMRIKVQRGR GYVPASTRIH SEEDERPIGR LLVDACYSPV ERIAYNVEAA RVEQRTDLDK LVIEMETNGT IDPEEAIRRA ATILAEQLEA FVDLRDVRQP EVKEEKPEFD PILLRPVDDL ELTVRSANCL KAEAIHYIGD LVQRTEVELL KTPNLGKKSL TEIKDVLASR GLSLGMRLEN WPPASIADE //