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 27-MAR-2024, entry version 169. 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; Synonyms=pez, phs, sez; OrderedLocusNames=b3295, JW3257; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP PROTEIN SEQUENCE. RX PubMed=323055; DOI=10.1016/0014-5793(77)80131-2; RA Ovchinnikov Y.A., Lipkin V.M., Modyanov N.N., Chertov O.Y., Smirnov Y.V.; RT "Primary structure of alpha-subunit of DNA-dependent RNA polymerase from RT 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 polymerase RT from E. coli. V. The cyanogen bromide peptides."; RL Bioorg. Khim. 4:437-449(1978). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6379605; DOI=10.1093/nar/12.14.5813; RA Meek D.W., Hayward R.S.; RT "Nucleotide sequence of the rpoA-rplQ DNA of Escherichia coli: a second RT 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 PubMed=2989779; DOI=10.1093/nar/13.11.3891; 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 Escherichia RT coli."; RL Nucleic Acids Res. 13:3891-3903(1985). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DOMAIN, SUBUNIT, AND MUTAGENESIS OF RP ARG-45 AND ARG-191. RC STRAIN=K12; RX PubMed=2235479; DOI=10.1093/nar/18.20.5945; 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 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., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(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 MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-159. RX PubMed=387752; DOI=10.1016/s0021-9258(19)86562-6; RA Post L.E., Nomura M.; RT "Nucleotide sequence of the intercistronic region preceding the gene for RT 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 PubMed=9298646; DOI=10.1002/elps.1150180807; RA Link A.J., Robison K., Church G.M.; RT "Comparing the predicted and observed properties of proteins encoded in the RT 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 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 gene RT for ribosomal protein S4 show thermosensitivity in Escherichia coli."; RL Mol. Gen. Genet. 199:265-270(1985). RN [11] RP PROTEIN SEQUENCE OF 1-4. RC STRAIN=K12; RX PubMed=1095419; DOI=10.1016/0014-5793(75)81001-5; RA Fujiki H., Zurek G.; RT "The subunits of DNA-dependent RNA polymerase from E. coli: I. Amino acid RT analysis and primary structure of the N-terminal regions."; RL FEBS Lett. 55:242-244(1975). RN [12] RP IDENTIFICATION BY 2D-GEL. RX PubMed=9298644; DOI=10.1002/elps.1150180805; RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). RN [13] RP FUNCTION IN TRANSCRIPTION, PROBABLE INTERACTION WITH CRP, SUBUNIT, AND RP DOMAIN. RX PubMed=1646077; DOI=10.1016/0092-8674(91)90553-b; RA Igarashi K., Ishihama A.; RT "Bipartite functional map of the E. coli RNA polymerase alpha subunit: RT involvement of the C-terminal region in transcription activation by cAMP- RT CRP."; RL Cell 65:1015-1022(1991). RN [14] RP INTERACTION WITH CRP, AND MUTAGENESIS OF 162-GLU--GLU-165 AND GLU-165. RX PubMed=8978616; DOI=10.1016/s0092-8674(00)81806-1; RA Niu W., Kim Y., Tau G., Heyduk T., Ebright R.H.; RT "Transcription activation at class II CAP-dependent promoters: two RT interactions between CAP and RNA polymerase."; RL Cell 87:1123-1134(1996). RN [15] RP ADP-RIBOSYLATION AT ARG-265 (MICROBIAL INFECTION). RX PubMed=4371081; DOI=10.1016/s0021-9258(19)42238-2; RA Goff C.G.; RT "Chemical structure of a modification of the Escherichia coli ribonucleic RT acid polymerase alpha polypeptides induced by bacteriophage T4 infection."; RL J. Biol. Chem. 249:6181-6190(1974). RN [16] RP ADP-RIBOSYLATION (MICROBIAL INFECTION). RX PubMed=10634320; RA Tiemann B., Depping R., Rueger W.; RT "Overexpression, purification, and partial characterization of ADP- RT ribosyltransferases modA and modB of bacteriophage T4."; RL Gene Expr. 8:187-196(1999). RN [17] RP ADP-RIBOSYLATION (MICROBIAL INFECTION). RX PubMed=15489438; DOI=10.1128/jb.186.21.7262-7272.2004; RA Tiemann B., Depping R., Gineikiene E., Kaliniene L., Nivinskas R., RA Ruger W.; RT "ModA and ModB, two ADP-ribosyltransferases encoded by bacteriophage T4: RT catalytic properties and mutation analysis."; RL J. Bacteriol. 186:7262-7272(2004). RN [18] RP ACETYLATION AT LYS-297 AND LYS-298. RX PubMed=21696463; DOI=10.1111/j.1365-2958.2011.07742.x; RA Lima B.P., Antelmann H., Gronau K., Chi B.K., Becher D., Brinsmade S.R., RA Wolfe A.J.; RT "Involvement of protein acetylation in glucose-induced transcription of a RT stress-responsive promoter."; RL Mol. Microbiol. 81:1190-1204(2011). RN [19] RP STRUCTURE BY NMR OF 233-349. RX PubMed=7491496; DOI=10.1126/science.270.5241.1495; RA Jeon Y.H., Negishi T., Shirakawa M., Yamazaki T., Fujita N., Ishihama A., RA Kyogoku Y.; RT "Solution structure of the activator contact domain of the RNA polymerase RT alpha subunit."; RL Science 270:1495-1497(1995). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-235. RX 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). RN [21] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 246-329 IN COMPLEX WITH DNA AND RP CRP, INTERACTION WITH CRP, DNA-BINDING, AND SUBUNIT. RX PubMed=12202833; DOI=10.1126/science.1076376; RA Benoff B., Yang H., Lawson C.L., Parkinson G., Liu J., Blatter E., RA Ebright Y.W., Berman H.M., Ebright R.H.; RT "Structural basis of transcription activation: the CAP-alpha CTD-DNA RT complex."; RL Science 297:1562-1566(2002). RN [22] {ECO:0007744|PDB:3IYD} RP STRUCTURE BY ELECTRON MICROSCOPY (19.80 ANGSTROMS) IN COMPLEX WITH RPOB; RP RPOC; RPOD; RPOZ; CRP AND DNA, INTERACTION WITH CRP, DNA-BINDING, AND RP SUBUNIT. RX PubMed=19903881; DOI=10.1073/pnas.0908782106; RA Hudson B.P., Quispe J., Lara-Gonzalez S., Kim Y., Berman H.M., Arnold E., RA Ebright R.H., Lawson C.L.; RT "Three-dimensional EM structure of an intact activator-dependent RT transcription initiation complex."; RL Proc. Natl. Acad. Sci. U.S.A. 106:19830-19835(2009). RN [23] {ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY} RP X-RAY CRYSTALLOGRAPHY (3.90 ANGSTROMS) OF 2-329 IN COMPLEX WITH RPOB; RPOC; RP RPOD; RPOZ AND SALINAMIDE A, FUNCTION, AND SUBUNIT. RX PubMed=24843001; DOI=10.7554/elife.02451; RA Degen D., Feng Y., Zhang Y., Ebright K.Y., Ebright Y.W., Gigliotti M., RA Vahedian-Movahed H., Mandal S., Talaue M., Connell N., Arnold E., RA Fenical W., Ebright R.H.; RT "Transcription inhibition by the depsipeptide antibiotic salinamide A."; RL Elife 3:e02451-e02451(2014). RN [24] {ECO:0007744|PDB:6TQN, ECO:0007744|PDB:6TQO} RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF RRNA RP TRANSCRIPTION-ELONGATION-ANTITERMINATION COMPLEXES WITH AND WITHOUT S4, RP FUNCTION, AND SUBUNIT. RX PubMed=32871103; DOI=10.1016/j.molcel.2020.08.010; RA Huang Y.H., Hilal T., Loll B., Buerger J., Mielke T., Boettcher C., RA Said N., Wahl M.C.; RT "Structure-Based Mechanisms of a Molecular RNA Polymerase/Chaperone Machine RT Required for Ribosome Biosynthesis."; RL Mol. Cell 0:0-0(2020). 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 plays an important role in CC subunit assembly since its dimerization is the first step in the CC sequential assembly of subunits to form the holoenzyme. CC {ECO:0000269|PubMed:1646077, ECO:0000269|PubMed:24843001}. CC -!- FUNCTION: Part of the processive rRNA transcription and antitermination CC complex (rrnTAC). The complex forms an RNA-chaperone ring around the CC RNA exit tunnel of RNAP. It supports rapid transcription and CC antitermination of rRNA operons, cotranscriptional rRNA folding, and CC annealing of distal rRNA regions to allow correct ribosome biogenesis. CC {ECO:0000269|PubMed:32871103}. 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. Both the N- and C-terminus interact with different CC regions of transcriptional regulator CRP. The rRNA transcription and CC antitermination complex (rrnTAC) consists of RNAP, NusA, NusB, NusE CC (rpsJ), NusG, SubB, ribosomal protein S4, DNA and precursor rRNA; S4 is CC more flexible than other subunits (PubMed:32871103). CC {ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1646077, CC ECO:0000269|PubMed:19903881, ECO:0000269|PubMed:2235479, CC ECO:0000269|PubMed:24843001, ECO:0000269|PubMed:32871103}. CC -!- INTERACTION: CC P0A7Z4; P0ABQ0: coaBC; NbExp=2; IntAct=EBI-544985, EBI-548929; CC P0A7Z4; P0AFF6: nusA; NbExp=7; IntAct=EBI-544985, EBI-551571; CC P0A7Z4; P60422: rplB; NbExp=6; IntAct=EBI-544985, EBI-543515; 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 (such as CRP) and with upstream CC promoter elements. {ECO:0000269|PubMed:1646077, CC ECO:0000269|PubMed:2235479}. CC -!- PTM: Acetylated on Lys-297 and Lys-298 in the presence of glucose. PatZ CC controls acetylation of Lys-298 but not of Lys-297. CC {ECO:0000269|PubMed:21696463}. CC -!- PTM: (Microbial infection) ADP-ribosylated on both alpha subunits by CC the phage T4 protein ModA (PubMed:10634320, PubMed:15489438). ADP- CC ribosylated on only one of the alpha subunits by the phage T4 protein CC Alt (PubMed:15489438). {ECO:0000269|PubMed:10634320, CC ECO:0000269|PubMed:15489438}. CC -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) 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 RefSeq; NP_417754.1; NC_000913.3. DR RefSeq; WP_001162094.1; NZ_STEB01000038.1. DR PDB; 1BDF; X-ray; 2.50 A; A/B/C/D=1-235. DR PDB; 1COO; NMR; -; A=233-329. DR PDB; 1LB2; X-ray; 3.10 A; B/E=246-329. DR PDB; 1XS9; NMR; -; D=249-329. DR PDB; 3IYD; EM; -; A/B=1-329. DR PDB; 3K4G; X-ray; 2.05 A; A/B/C/D/E/F/G/H=245-329. DR PDB; 3LU0; EM; -; A/B=1-329. DR PDB; 3N4M; X-ray; 2.99 A; B/C=246-329. DR PDB; 3N97; X-ray; 3.25 A; B/C=246-329. DR PDB; 4JK1; X-ray; 3.90 A; A/B/F/G=1-329. DR PDB; 4JK2; X-ray; 4.20 A; A/B/F/G=1-329. DR PDB; 4KMU; X-ray; 3.85 A; A/B/F/G=1-329. DR PDB; 4KN4; X-ray; 3.96 A; A/B/F/G=1-329. DR PDB; 4KN7; X-ray; 3.69 A; A/B/F/G=1-329. DR PDB; 4MEX; X-ray; 3.90 A; A/B/G/H=1-329. DR PDB; 4MEY; X-ray; 3.95 A; A/B/G/H=1-329. DR PDB; 4S20; X-ray; 4.70 A; A/B/F/G=1-329. DR PDB; 4XSX; X-ray; 3.71 A; A/B/G/H=1-234. DR PDB; 4XSY; X-ray; 4.01 A; A/B/G/H=1-234. DR PDB; 4XSZ; X-ray; 3.68 A; A/B/G/H=1-234. DR PDB; 4YG2; X-ray; 3.70 A; A/B/G/H=1-329. DR PDB; 4YLN; X-ray; 5.50 A; A/B/G/H/M/N=1-235. DR PDB; 4YLO; X-ray; 6.00 A; A/B/G/H/M/N=1-235. DR PDB; 4YLP; X-ray; 5.50 A; A/B/G/H/M/N=1-235. DR PDB; 4ZH2; X-ray; 4.20 A; A/B/G/H=2-329. DR PDB; 4ZH3; X-ray; 4.08 A; A/B/G/H=2-329. DR PDB; 4ZH4; X-ray; 3.99 A; A/B/G/H=2-329. DR PDB; 5CIZ; X-ray; 5.01 A; B=246-329. DR PDB; 5EZK; X-ray; 8.50 A; A/B=1-329. DR PDB; 5IPL; X-ray; 3.60 A; A/B=1-235. DR PDB; 5IPM; X-ray; 4.20 A; A/B=1-235. DR PDB; 5IPN; X-ray; 4.61 A; A/B=1-235. DR PDB; 5MS0; EM; 9.80 A; A/B=1-329. DR PDB; 5MY1; EM; 7.60 A; V/W=1-329. DR PDB; 5NSR; EM; 3.80 A; A/B=1-329. DR PDB; 5NSS; EM; 5.80 A; A/B=1-329. DR PDB; 5NWT; X-ray; 3.76 A; A/B=1-329. DR PDB; 5UAC; X-ray; 3.80 A; A/B/G/H=1-329. DR PDB; 5UAG; X-ray; 3.40 A; A/B/G/H=1-320. DR PDB; 5UAH; X-ray; 4.10 A; A/B/G/H=1-329. DR PDB; 5UAJ; X-ray; 3.92 A; A/B/G/H=1-329. DR PDB; 5UAL; X-ray; 3.89 A; A/B/G/H=1-329. DR PDB; 5UAQ; X-ray; 3.60 A; A/B/G/H=1-329. DR PDB; 5UI8; X-ray; 3.76 A; G/H=1-329. DR PDB; 5VSW; X-ray; 4.29 A; A/B/G/H=1-329. DR PDB; 5VT0; EM; 3.78 A; G/H=1-234. DR PDB; 5W1S; X-ray; 3.81 A; A/B/G/H=1-329. DR PDB; 5W1T; X-ray; 4.50 A; A/B/G/H=1-329. DR PDB; 6ALF; EM; 4.10 A; G/H=1-234. DR PDB; 6ALG; EM; 3.70 A; G/H=1-234. DR PDB; 6ALH; EM; 4.40 A; G/H=1-234. DR PDB; 6ASX; EM; 3.80 A; G/H=1-234. DR PDB; 6AWB; EM; 6.70 A; 01/02=6-234. DR PDB; 6AWC; EM; 7.90 A; 01/02=6-234. DR PDB; 6AWD; EM; 8.10 A; 01/02=6-234. DR PDB; 6BJS; EM; 5.50 A; G/H=1-234. DR PDB; 6BYU; X-ray; 3.60 A; A/B/G/H=1-329. DR PDB; 6C6S; EM; 3.70 A; G/H=1-234. DR PDB; 6C6T; EM; 3.50 A; G/H=1-234. DR PDB; 6C6U; EM; 3.70 A; G/H=1-234. DR PDB; 6C9Y; EM; 4.25 A; A/B=1-329. DR PDB; 6CA0; EM; 5.75 A; A/B=1-329. DR PDB; 6CUX; X-ray; 4.10 A; A/B/G/H=1-329. DR PDB; 6FLP; EM; 4.10 A; A/B=1-329. DR PDB; 6FLQ; EM; 4.10 A; A/B=1-329. DR PDB; 6GFW; EM; 3.70 A; A/B=1-329. DR PDB; 6GH5; EM; 3.40 A; A/B=1-329. DR PDB; 6GH6; EM; 4.10 A; A/B=1-329. DR PDB; 6GOV; EM; 3.70 A; U/V=1-329. DR PDB; 6JBQ; EM; 4.02 A; A/B=1-329. DR PDB; 6JNX; EM; 4.08 A; A/B=1-329. DR PDB; 6K4Y; EM; 3.79 A; A/B=1-329. DR PDB; 6KJ6; EM; 3.80 A; A/B=1-329. DR PDB; 6LDI; EM; 3.69 A; A/B=1-329. DR PDB; 6N4C; EM; 17.00 A; A=6-321, B=6-315. DR PDB; 6N57; EM; 3.70 A; G/H=1-329. DR PDB; 6N58; EM; 3.78 A; G/H=1-329. DR PDB; 6N60; X-ray; 3.68 A; A/B=1-234. DR PDB; 6N61; X-ray; 3.25 A; A/B=1-234. DR PDB; 6N62; X-ray; 3.80 A; A/B=1-234. DR PDB; 6OMF; EM; 3.26 A; A/B=1-234. DR PDB; 6OUL; EM; 3.40 A; G/H/R=1-329. DR PDB; 6P18; EM; 3.50 A; A/B=1-329. DR PDB; 6P19; EM; 3.80 A; A/B=1-329. DR PDB; 6P1K; EM; 4.05 A; G/H=1-329. DR PDB; 6PB4; EM; 4.35 A; A/B=1-329. DR PDB; 6PB5; EM; 4.52 A; A/B=1-329. DR PDB; 6PB6; EM; 4.29 A; A/B=1-329. DR PDB; 6PMI; EM; 3.86 A; A/B=1-329. DR PDB; 6PMJ; EM; 3.91 A; A/B=1-329. DR PDB; 6PSQ; EM; 3.40 A; G/H/M=1-329. DR PDB; 6PSR; EM; 3.40 A; G/H/M=1-329. DR PDB; 6PSS; EM; 3.50 A; G/H/M=1-329. DR PDB; 6PST; EM; 3.00 A; G/H/M=1-329. DR PDB; 6PSU; EM; 3.90 A; G/H/M=1-329. DR PDB; 6PSV; EM; 3.50 A; G/H/M=1-329. DR PDB; 6PSW; EM; 3.70 A; G/H/M=1-329. DR PDB; 6R9B; EM; 3.80 A; A/B=1-329. DR PDB; 6R9G; EM; 3.70 A; A/B=1-329. DR PDB; 6RH3; EM; 3.60 A; A/B=1-329. DR PDB; 6RI7; EM; 3.90 A; A/B=1-329. DR PDB; 6RI9; EM; 3.70 A; A/B=1-329. DR PDB; 6RIN; EM; 3.70 A; A/B=1-329. DR PDB; 6RIP; EM; 3.40 A; A/B=1-329. DR PDB; 6TQN; EM; 3.80 A; U/V=1-329. DR PDB; 6TQO; EM; 3.80 A; U/V=1-329. DR PDB; 6UTW; X-ray; 3.85 A; AAA/BBB=1-235. DR PDB; 6UTX; X-ray; 4.05 A; AAA/BBB=1-235. DR PDB; 6UTY; X-ray; 4.15 A; AAA/BBB=1-235. DR PDB; 6UTZ; X-ray; 3.80 A; AAA/BBB=1-235. DR PDB; 6UU0; X-ray; 3.90 A; AAA/BBB=1-235. DR PDB; 6UU1; X-ray; 4.10 A; AAA/BBB=1-235. DR PDB; 6UU2; X-ray; 4.40 A; AAA/BBB=1-235. DR PDB; 6UU3; X-ray; 4.00 A; AAA/BBB=1-235. DR PDB; 6UU4; X-ray; 4.30 A; AAA/BBB=1-235. DR PDB; 6UU5; X-ray; 5.40 A; AAA/BBB=1-235. DR PDB; 6UU6; X-ray; 4.20 A; AAA/BBB=1-235. DR PDB; 6UU7; X-ray; 4.40 A; AAA/BBB=1-235. DR PDB; 6UU8; X-ray; 4.40 A; AAA/BBB=1-235. DR PDB; 6UU9; X-ray; 5.40 A; AAA/BBB=1-235. DR PDB; 6UUA; X-ray; 4.00 A; AAA/BBB=1-235. DR PDB; 6UUB; X-ray; 3.96 A; AAA/BBB=1-235. DR PDB; 6UUC; X-ray; 4.10 A; AAA/BBB=1-235. DR PDB; 6VJS; X-ray; 4.02 A; A/B/F/G=1-329. DR PDB; 6VU3; EM; 3.70 A; AC/AD=6-235. DR PDB; 6VYQ; EM; 3.70 A; AC/AD=1-329. DR PDB; 6VYR; EM; 3.80 A; AC/AD=1-329. DR PDB; 6VYS; EM; 3.70 A; AC/AD=1-329. DR PDB; 6VYT; EM; 14.00 A; AC/AD=1-329. DR PDB; 6VYU; EM; 7.00 A; AC/AD=1-329. DR PDB; 6VYW; EM; 7.00 A; AC/AD=1-329. DR PDB; 6VYX; EM; 9.90 A; AC/AD=1-329. DR PDB; 6VYY; EM; 9.90 A; AC/AD=1-329. DR PDB; 6VYZ; EM; 9.90 A; AC/AD=1-329. DR PDB; 6VZ2; EM; 10.00 A; AC/AD=1-329. DR PDB; 6VZ3; EM; 8.90 A; AC/AD=6-235. DR PDB; 6VZ5; EM; 8.90 A; AC/AD=1-329. DR PDB; 6VZ7; EM; 7.00 A; AC/AD=6-235. DR PDB; 6VZJ; EM; 4.10 A; AC/AD=1-329. DR PDB; 6WMU; EM; 3.18 A; A/B=1-329. DR PDB; 6X26; EM; 4.10 A; G/H=1-329. DR PDB; 6X2F; EM; 4.00 A; G/H=1-329. DR PDB; 6X2N; EM; 3.90 A; G/H=1-329. DR PDB; 6X43; EM; 3.60 A; G/H=1-329. DR PDB; 6X4W; EM; 3.80 A; G/H=1-329. DR PDB; 6X4Y; EM; 3.60 A; G/H=1-329. DR PDB; 6X50; EM; 3.30 A; G/H=1-329. DR PDB; 6X6T; EM; 3.20 A; AC/AD=1-329. DR PDB; 6X7F; EM; 3.50 A; AC/AD=1-329. DR PDB; 6X7K; EM; 3.10 A; AC/AD=1-329. DR PDB; 6X9Q; EM; 4.80 A; AC/AD=1-329. DR PDB; 6XAS; EM; 3.80 A; H/K=1-329. DR PDB; 6XAV; EM; 7.70 A; H/K=1-329. DR PDB; 6XDQ; EM; 3.70 A; AC/AD=1-329. DR PDB; 6XDR; EM; 4.70 A; AC/AD=1-329. DR PDB; 6XGF; EM; 5.00 A; AC/AD=1-329. DR PDB; 6XH7; EM; 3.90 A; A/B=1-329. DR PDB; 6XH8; EM; 4.10 A; A/B=1-329. DR PDB; 6XII; EM; 7.00 A; AC/AD=1-329. DR PDB; 6XIJ; EM; 8.00 A; AC/AD=1-329. DR PDB; 6XL5; EM; 2.50 A; A/B=1-329. DR PDB; 6XL9; EM; 2.50 A; A/B=1-329. DR PDB; 6XLJ; EM; 2.70 A; A/B=1-329. DR PDB; 6XLL; EM; 2.70 A; A/B=1-329. DR PDB; 6XLM; EM; 3.20 A; A/B=1-329. DR PDB; 6XLN; EM; 2.80 A; A/B=1-329. DR PDB; 6Z9P; EM; 3.90 A; U/V=1-329. DR PDB; 6Z9Q; EM; 5.70 A; U/V=1-329. DR PDB; 6Z9R; EM; 4.10 A; U/V=1-329. DR PDB; 6Z9S; EM; 4.40 A; U/V=1-329. DR PDB; 6Z9T; EM; 4.10 A; U/V=1-329. DR PDB; 6ZTJ; EM; 3.40 A; CA/CB=1-329. DR PDB; 6ZTL; EM; 3.50 A; CA/CB=1-329. DR PDB; 6ZTM; EM; 3.30 A; CA/CB=1-329. DR PDB; 6ZTN; EM; 3.90 A; CA/CB=1-329. DR PDB; 6ZTO; EM; 3.00 A; CA/CB=1-329. DR PDB; 6ZTP; EM; 3.00 A; CA/CB=1-329. DR PDB; 6ZU1; EM; 3.00 A; CA/CB=1-329. DR PDB; 7ADB; EM; 4.40 A; U/V=1-329. DR PDB; 7ADC; EM; 4.00 A; U/V=1-329. DR PDB; 7ADD; EM; 4.30 A; U/V=1-329. DR PDB; 7ADE; EM; 4.20 A; U/V=1-329. DR PDB; 7BEF; EM; 4.50 A; A/B=1-329. DR PDB; 7BEG; EM; 4.20 A; A/B=1-329. DR PDB; 7C17; EM; 4.22 A; A/B=1-329. DR PDB; 7C97; EM; 3.68 A; A/B/K=1-329. DR PDB; 7CHW; EM; 3.58 A; A/B/K=1-329. DR PDB; 7DY6; EM; 3.68 A; A/B/K=1-329. DR PDB; 7KHB; EM; 3.53 A; A/B=1-329. DR PDB; 7KHC; EM; 4.14 A; A/B=1-329. DR PDB; 7KHE; EM; 3.58 A; A/B=1-236. DR PDB; 7KHI; EM; 3.62 A; A/B=1-236. DR PDB; 7M8E; EM; 3.40 A; A/B=1-329. DR PDB; 7MKD; EM; 3.20 A; G/H/R=1-329. DR PDB; 7MKE; EM; 3.70 A; G/H=1-329. DR PDB; 7MKI; EM; 3.50 A; G/H=1-329. DR PDB; 7MKJ; EM; 2.90 A; G/H/R=1-329. DR PDB; 7MKN; EM; 3.30 A; A/B=1-237. DR PDB; 7MKO; EM; 3.15 A; A/B=1-237. DR PDB; 7MKP; EM; 3.41 A; A/B=1-237. DR PDB; 7MKQ; EM; 4.80 A; A/B=1-237. DR PDB; 7N4E; EM; 3.80 A; A/B=1-329. DR PDB; 7PY0; EM; 4.50 A; A/B=1-329. DR PDB; 7PY1; EM; 3.80 A; A/B=1-329. DR PDB; 7PY3; EM; 3.80 A; A/B=1-329. DR PDB; 7PY5; EM; 3.90 A; A/B=1-329. DR PDB; 7PY6; EM; 4.10 A; A/B=1-329. DR PDB; 7PY7; EM; 4.10 A; A/B=1-329. DR PDB; 7PY8; EM; 3.80 A; A/B=1-329. DR PDB; 7PYJ; EM; 4.20 A; A/B=1-329. DR PDB; 7PYK; EM; 4.10 A; A/B=1-329. DR PDB; 7Q0J; EM; 4.30 A; A/B=1-329. DR PDB; 7Q0K; EM; 4.00 A; A/B=1-329. DR PDB; 7QV9; EM; 3.50 A; A/B=1-329. DR PDB; 7QWP; EM; 3.40 A; A/B=1-329. DR PDB; 7QXI; EM; 3.40 A; A/B=1-329. DR PDB; 7SZJ; EM; 3.11 A; A/B=1-329. DR PDB; 7SZK; EM; 2.94 A; A/B=1-329. DR PDB; 7UBM; EM; 3.13 A; A/B=1-329. DR PDB; 7UBN; EM; 3.36 A; A/B=1-329. DR PDB; 7UWE; EM; 2.90 A; G/H=1-329. DR PDB; 7UWH; EM; 3.10 A; G/H=1-329. DR PDB; 7VWY; EM; 4.57 A; A/B=1-329. DR PDB; 7VWZ; EM; 4.00 A; A/B=1-329. DR PDB; 7W5W; EM; 4.55 A; A/B=1-329. DR PDB; 7W5X; EM; 3.40 A; A/B=1-329. DR PDB; 7W5Y; EM; 4.20 A; A/B=1-329. DR PDB; 7XUE; EM; 3.17 A; G/H=1-329. DR PDB; 7XUG; EM; 3.57 A; G/H=1-329. DR PDB; 7XUI; EM; 3.61 A; G/H=1-329. DR PDB; 7YP9; EM; 3.58 A; A/B=1-329. DR PDB; 7YPA; EM; 3.05 A; A/B=1-329. DR PDB; 7YPB; EM; 3.48 A; A/B=1-329. DR PDB; 8ABY; EM; 3.70 A; A/B=1-329. DR PDB; 8ABZ; EM; 3.40 A; A/B=1-329. DR PDB; 8AC0; EM; 4.10 A; A/B=1-329. DR PDB; 8AC1; EM; 4.06 A; A/B=1-329. DR PDB; 8AC2; EM; 3.70 A; A/B=1-329. DR PDB; 8ACP; EM; 4.50 A; A/B=1-329. DR PDB; 8AD1; EM; 4.10 A; A/B=1-329. DR PDB; 8E3F; EM; 6.50 A; C/D=1-329. DR PDB; 8E5K; EM; 4.20 A; C/D=1-329. DR PDB; 8E5O; EM; 4.40 A; C/D=1-329. DR PDB; 8E6X; EM; 4.27 A; C/D=1-329. DR PDB; 8E6Z; EM; 4.10 A; C/D=1-329. DR PDB; 8EG7; EM; 3.20 A; G/H=1-234. DR PDB; 8EG8; EM; 3.30 A; G/H=1-234. DR PDB; 8EGB; EM; 3.80 A; G/H=1-234. DR PDB; 8EH8; EM; 3.40 A; G/H=1-234. DR PDB; 8EH9; EM; 3.90 A; G/H=1-234. DR PDB; 8EHA; EM; 3.70 A; G/H=1-234. DR PDB; 8EHF; EM; 3.30 A; G/H=1-234. DR PDB; 8EHI; EM; 5.50 A; G/H=1-234. DR PDB; 8F1I; EM; 3.00 A; G/H=1-329. DR PDB; 8F1J; EM; 2.60 A; G/H=1-329. DR PDB; 8F1K; EM; 2.80 A; G/H=1-329. DR PDB; 8F3C; EM; 3.40 A; G/H=1-328. DR PDB; 8FIX; EM; 3.90 A; A/B=1-329. DR PDB; 8FIY; EM; 7.30 A; A/B=1-329. DR PDB; 8FVR; EM; 2.42 A; D/E=1-329. DR PDB; 8FVW; EM; 2.10 A; D/E=1-329. DR PDB; 8HKC; EM; 2.49 A; A/B=1-329. DR PDB; 8IGR; EM; 3.10 A; G/H=1-329. DR PDB; 8IGS; EM; 3.40 A; H=1-329. DR PDB; 8JO2; EM; 2.74 A; A/B=1-329. DR PDBsum; 1BDF; -. DR PDBsum; 1COO; -. DR PDBsum; 1LB2; -. DR PDBsum; 1XS9; -. DR PDBsum; 3IYD; -. DR PDBsum; 3K4G; -. DR PDBsum; 3LU0; -. DR PDBsum; 3N4M; -. DR PDBsum; 3N97; -. DR PDBsum; 4JK1; -. DR PDBsum; 4JK2; -. DR PDBsum; 4KMU; -. DR PDBsum; 4KN4; -. DR PDBsum; 4KN7; -. DR PDBsum; 4MEX; -. DR PDBsum; 4MEY; -. DR PDBsum; 4S20; -. DR PDBsum; 4XSX; -. DR PDBsum; 4XSY; -. DR PDBsum; 4XSZ; -. DR PDBsum; 4YG2; -. DR PDBsum; 4YLN; -. DR PDBsum; 4YLO; -. DR PDBsum; 4YLP; -. DR PDBsum; 4ZH2; -. DR PDBsum; 4ZH3; -. DR PDBsum; 4ZH4; -. DR PDBsum; 5CIZ; -. DR PDBsum; 5EZK; -. DR PDBsum; 5IPL; -. DR PDBsum; 5IPM; -. DR PDBsum; 5IPN; -. DR PDBsum; 5MS0; -. DR PDBsum; 5MY1; -. DR PDBsum; 5NSR; -. DR PDBsum; 5NSS; -. DR PDBsum; 5NWT; -. DR PDBsum; 5UAC; -. DR PDBsum; 5UAG; -. DR PDBsum; 5UAH; -. DR PDBsum; 5UAJ; -. DR PDBsum; 5UAL; -. DR PDBsum; 5UAQ; -. DR PDBsum; 5UI8; -. DR PDBsum; 5VSW; -. DR PDBsum; 5VT0; -. DR PDBsum; 5W1S; -. DR PDBsum; 5W1T; -. DR PDBsum; 6ALF; -. DR PDBsum; 6ALG; -. DR PDBsum; 6ALH; -. DR PDBsum; 6ASX; -. DR PDBsum; 6AWB; -. DR PDBsum; 6AWC; -. DR PDBsum; 6AWD; -. DR PDBsum; 6BJS; -. DR PDBsum; 6BYU; -. DR PDBsum; 6C6S; -. DR PDBsum; 6C6T; -. DR PDBsum; 6C6U; -. DR PDBsum; 6C9Y; -. DR PDBsum; 6CA0; -. DR PDBsum; 6CUX; -. DR PDBsum; 6FLP; -. DR PDBsum; 6FLQ; -. DR PDBsum; 6GFW; -. DR PDBsum; 6GH5; -. DR PDBsum; 6GH6; -. DR PDBsum; 6GOV; -. DR PDBsum; 6JBQ; -. DR PDBsum; 6JNX; -. DR PDBsum; 6K4Y; -. DR PDBsum; 6KJ6; -. DR PDBsum; 6LDI; -. DR PDBsum; 6N4C; -. DR PDBsum; 6N57; -. DR PDBsum; 6N58; -. DR PDBsum; 6N60; -. DR PDBsum; 6N61; -. DR PDBsum; 6N62; -. DR PDBsum; 6OMF; -. DR PDBsum; 6OUL; -. DR PDBsum; 6P18; -. DR PDBsum; 6P19; -. DR PDBsum; 6P1K; -. DR PDBsum; 6PB4; -. DR PDBsum; 6PB5; -. DR PDBsum; 6PB6; -. DR PDBsum; 6PMI; -. DR PDBsum; 6PMJ; -. DR PDBsum; 6PSQ; -. DR PDBsum; 6PSR; -. DR PDBsum; 6PSS; -. DR PDBsum; 6PST; -. DR PDBsum; 6PSU; -. DR PDBsum; 6PSV; -. DR PDBsum; 6PSW; -. DR PDBsum; 6R9B; -. DR PDBsum; 6R9G; -. DR PDBsum; 6RH3; -. DR PDBsum; 6RI7; -. DR PDBsum; 6RI9; -. DR PDBsum; 6RIN; -. DR PDBsum; 6RIP; -. DR PDBsum; 6TQN; -. DR PDBsum; 6TQO; -. DR PDBsum; 6UTW; -. DR PDBsum; 6UTX; -. DR PDBsum; 6UTY; -. DR PDBsum; 6UTZ; -. DR PDBsum; 6UU0; -. DR PDBsum; 6UU1; -. DR PDBsum; 6UU2; -. DR PDBsum; 6UU3; -. DR PDBsum; 6UU4; -. DR PDBsum; 6UU5; -. DR PDBsum; 6UU6; -. DR PDBsum; 6UU7; -. DR PDBsum; 6UU8; -. DR PDBsum; 6UU9; -. DR PDBsum; 6UUA; -. DR PDBsum; 6UUB; -. DR PDBsum; 6UUC; -. DR PDBsum; 6VJS; -. DR PDBsum; 6VU3; -. DR PDBsum; 6VYQ; -. DR PDBsum; 6VYR; -. DR PDBsum; 6VYS; -. DR PDBsum; 6VYT; -. DR PDBsum; 6VYU; -. DR PDBsum; 6VYW; -. DR PDBsum; 6VYX; -. DR PDBsum; 6VYY; -. DR PDBsum; 6VYZ; -. DR PDBsum; 6VZ2; -. DR PDBsum; 6VZ3; -. DR PDBsum; 6VZ5; -. DR PDBsum; 6VZ7; -. DR PDBsum; 6VZJ; -. DR PDBsum; 6WMU; -. DR PDBsum; 6X26; -. DR PDBsum; 6X2F; -. DR PDBsum; 6X2N; -. DR PDBsum; 6X43; -. DR PDBsum; 6X4W; -. DR PDBsum; 6X4Y; -. DR PDBsum; 6X50; -. DR PDBsum; 6X6T; -. DR PDBsum; 6X7F; -. DR PDBsum; 6X7K; -. DR PDBsum; 6X9Q; -. DR PDBsum; 6XAS; -. DR PDBsum; 6XAV; -. DR PDBsum; 6XDQ; -. DR PDBsum; 6XDR; -. DR PDBsum; 6XGF; -. DR PDBsum; 6XH7; -. DR PDBsum; 6XH8; -. DR PDBsum; 6XII; -. DR PDBsum; 6XIJ; -. DR PDBsum; 6XL5; -. DR PDBsum; 6XL9; -. DR PDBsum; 6XLJ; -. DR PDBsum; 6XLL; -. DR PDBsum; 6XLM; -. DR PDBsum; 6XLN; -. DR PDBsum; 6Z9P; -. DR PDBsum; 6Z9Q; -. DR PDBsum; 6Z9R; -. DR PDBsum; 6Z9S; -. DR PDBsum; 6Z9T; -. DR PDBsum; 6ZTJ; -. DR PDBsum; 6ZTL; -. DR PDBsum; 6ZTM; -. DR PDBsum; 6ZTN; -. DR PDBsum; 6ZTO; -. DR PDBsum; 6ZTP; -. DR PDBsum; 6ZU1; -. DR PDBsum; 7ADB; -. DR PDBsum; 7ADC; -. DR PDBsum; 7ADD; -. DR PDBsum; 7ADE; -. DR PDBsum; 7BEF; -. DR PDBsum; 7BEG; -. DR PDBsum; 7C17; -. DR PDBsum; 7C97; -. DR PDBsum; 7CHW; -. DR PDBsum; 7DY6; -. DR PDBsum; 7KHB; -. DR PDBsum; 7KHC; -. DR PDBsum; 7KHE; -. DR PDBsum; 7KHI; -. DR PDBsum; 7M8E; -. DR PDBsum; 7MKD; -. DR PDBsum; 7MKE; -. DR PDBsum; 7MKI; -. DR PDBsum; 7MKJ; -. DR PDBsum; 7MKN; -. DR PDBsum; 7MKO; -. DR PDBsum; 7MKP; -. DR PDBsum; 7MKQ; -. DR PDBsum; 7N4E; -. DR PDBsum; 7PY0; -. DR PDBsum; 7PY1; -. DR PDBsum; 7PY3; -. DR PDBsum; 7PY5; -. DR PDBsum; 7PY6; -. DR PDBsum; 7PY7; -. DR PDBsum; 7PY8; -. DR PDBsum; 7PYJ; -. DR PDBsum; 7PYK; -. DR PDBsum; 7Q0J; -. DR PDBsum; 7Q0K; -. DR PDBsum; 7QV9; -. DR PDBsum; 7QWP; -. DR PDBsum; 7QXI; -. DR PDBsum; 7SZJ; -. DR PDBsum; 7SZK; -. DR PDBsum; 7UBM; -. DR PDBsum; 7UBN; -. DR PDBsum; 7UWE; -. DR PDBsum; 7UWH; -. DR PDBsum; 7VWY; -. DR PDBsum; 7VWZ; -. DR PDBsum; 7W5W; -. DR PDBsum; 7W5X; -. DR PDBsum; 7W5Y; -. DR PDBsum; 7XUE; -. DR PDBsum; 7XUG; -. DR PDBsum; 7XUI; -. DR PDBsum; 7YP9; -. DR PDBsum; 7YPA; -. DR PDBsum; 7YPB; -. DR PDBsum; 8ABY; -. DR PDBsum; 8ABZ; -. DR PDBsum; 8AC0; -. DR PDBsum; 8AC1; -. DR PDBsum; 8AC2; -. DR PDBsum; 8ACP; -. DR PDBsum; 8AD1; -. DR PDBsum; 8E3F; -. DR PDBsum; 8E5K; -. DR PDBsum; 8E5O; -. DR PDBsum; 8E6X; -. DR PDBsum; 8E6Z; -. DR PDBsum; 8EG7; -. DR PDBsum; 8EG8; -. DR PDBsum; 8EGB; -. DR PDBsum; 8EH8; -. DR PDBsum; 8EH9; -. DR PDBsum; 8EHA; -. DR PDBsum; 8EHF; -. DR PDBsum; 8EHI; -. DR PDBsum; 8F1I; -. DR PDBsum; 8F1J; -. DR PDBsum; 8F1K; -. DR PDBsum; 8F3C; -. DR PDBsum; 8FIX; -. DR PDBsum; 8FIY; -. DR PDBsum; 8FVR; -. DR PDBsum; 8FVW; -. DR PDBsum; 8HKC; -. DR PDBsum; 8IGR; -. DR PDBsum; 8IGS; -. DR PDBsum; 8JO2; -. DR AlphaFoldDB; P0A7Z4; -. DR EMDB; EMD-0001; -. DR EMDB; EMD-0002; -. DR EMDB; EMD-0340; -. DR EMDB; EMD-0348; -. DR EMDB; EMD-0349; -. DR EMDB; EMD-0700; -. DR EMDB; EMD-0874; -. DR EMDB; EMD-11418; -. DR EMDB; EMD-11419; -. DR EMDB; EMD-11420; -. DR EMDB; EMD-11421; -. DR EMDB; EMD-11422; -. DR EMDB; EMD-11423; -. DR EMDB; EMD-11426; -. DR EMDB; EMD-11722; -. DR EMDB; EMD-11723; -. DR EMDB; EMD-11724; -. DR EMDB; EMD-11725; -. DR EMDB; EMD-12156; -. DR EMDB; EMD-12157; -. DR EMDB; EMD-13706; -. DR EMDB; EMD-13707; -. DR EMDB; EMD-13709; -. DR EMDB; EMD-13713; -. DR EMDB; EMD-13714; -. DR EMDB; EMD-13715; -. DR EMDB; EMD-13716; -. DR EMDB; EMD-13717; -. DR EMDB; EMD-13718; -. DR EMDB; EMD-13745; -. DR EMDB; EMD-13746; -. DR EMDB; EMD-14171; -. DR EMDB; EMD-14190; -. DR EMDB; EMD-14200; -. DR EMDB; EMD-15327; -. DR EMDB; EMD-15328; -. DR EMDB; EMD-15329; -. DR EMDB; EMD-15330; -. DR EMDB; EMD-15331; -. DR EMDB; EMD-15352; -. DR EMDB; EMD-15357; -. DR EMDB; EMD-20090; -. DR EMDB; EMD-20203; -. DR EMDB; EMD-20233; -. DR EMDB; EMD-20234; -. DR EMDB; EMD-20286; -. DR EMDB; EMD-20287; -. DR EMDB; EMD-20288; -. DR EMDB; EMD-20394; -. DR EMDB; EMD-20395; -. DR EMDB; EMD-20460; -. DR EMDB; EMD-20461; -. DR EMDB; EMD-20462; -. DR EMDB; EMD-20463; -. DR EMDB; EMD-20464; -. DR EMDB; EMD-20465; -. DR EMDB; EMD-20466; -. DR EMDB; EMD-21853; -. DR EMDB; EMD-21879; -. DR EMDB; EMD-21881; -. DR EMDB; EMD-21883; -. DR EMDB; EMD-21996; -. DR EMDB; EMD-22006; -. DR EMDB; EMD-22012; -. DR EMDB; EMD-22039; -. DR EMDB; EMD-22043; -. DR EMDB; EMD-22044; -. DR EMDB; EMD-22045; -. DR EMDB; EMD-22114; -. DR EMDB; EMD-22115; -. DR EMDB; EMD-22184; -. DR EMDB; EMD-22185; -. DR EMDB; EMD-22234; -. DR EMDB; EMD-22236; -. DR EMDB; EMD-22245; -. DR EMDB; EMD-22247; -. DR EMDB; EMD-22248; -. DR EMDB; EMD-22249; -. DR EMDB; EMD-23716; -. DR EMDB; EMD-23892; -. DR EMDB; EMD-23893; -. DR EMDB; EMD-23895; -. DR EMDB; EMD-23897; -. DR EMDB; EMD-23900; -. DR EMDB; EMD-23901; -. DR EMDB; EMD-23902; -. DR EMDB; EMD-23903; -. DR EMDB; EMD-25570; -. DR EMDB; EMD-25571; -. DR EMDB; EMD-26438; -. DR EMDB; EMD-26439; -. DR EMDB; EMD-27864; -. DR EMDB; EMD-27913; -. DR EMDB; EMD-27916; -. DR EMDB; EMD-27930; -. DR EMDB; EMD-27931; -. DR EMDB; EMD-29212; -. DR EMDB; EMD-29213; -. DR EMDB; EMD-29491; -. DR EMDB; EMD-29494; -. DR EMDB; EMD-30268; -. DR EMDB; EMD-30307; -. DR EMDB; EMD-30376; -. DR EMDB; EMD-30914; -. DR EMDB; EMD-32165; -. DR EMDB; EMD-32166; -. DR EMDB; EMD-32322; -. DR EMDB; EMD-32323; -. DR EMDB; EMD-32324; -. DR EMDB; EMD-33466; -. DR EMDB; EMD-33468; -. DR EMDB; EMD-33470; -. DR EMDB; EMD-33996; -. DR EMDB; EMD-33997; -. DR EMDB; EMD-33998; -. DR EMDB; EMD-35438; -. DR EMDB; EMD-35439; -. DR EMDB; EMD-3561; -. DR EMDB; EMD-3580; -. DR EMDB; EMD-36453; -. DR EMDB; EMD-3695; -. DR EMDB; EMD-3696; -. DR EMDB; EMD-4274; -. DR EMDB; EMD-4275; -. DR EMDB; EMD-4397; -. DR EMDB; EMD-4769; -. DR EMDB; EMD-4770; -. DR EMDB; EMD-4882; -. DR EMDB; EMD-4885; -. DR EMDB; EMD-4886; -. DR EMDB; EMD-4892; -. DR EMDB; EMD-4893; -. DR EMDB; EMD-7002; -. DR EMDB; EMD-7103; -. DR EMDB; EMD-7349; -. DR EMDB; EMD-7350; -. DR EMDB; EMD-7351; -. DR EMDB; EMD-7438; -. DR EMDB; EMD-7439; -. DR EMDB; EMD-8584; -. DR EMDB; EMD-8586; -. DR EMDB; EMD-8732; -. DR EMDB; EMD-9792; -. DR EMDB; EMD-9852; -. DR EMDB; EMD-9916; -. DR SMR; P0A7Z4; -. DR BioGRID; 4263398; 114. DR BioGRID; 852106; 1. DR ComplexPortal; CPX-4881; DNA-directed RNA polymerase holoenzyme complex, Sigma70 variant. DR ComplexPortal; CPX-4883; DNA-directed RNA polymerase holoenzyme complex, SigmaS variant. DR ComplexPortal; CPX-4884; DNA-directed RNA polymerase holoenzyme complex, Sigma54 variant. DR ComplexPortal; CPX-4885; DNA-directed RNA polymerase holoenzyme complex, SigmaE variant. DR ComplexPortal; CPX-4886; DNA-directed RNA polymerase holoenzyme complex, SigmaF variant. DR ComplexPortal; CPX-4887; DNA-directed RNA polymerase holoenzyme complex, SigmaH variant. DR ComplexPortal; CPX-4888; DNA-directed RNA polymerase holoenzyme complex, Sigma fecI variant. DR ComplexPortal; CPX-5674; Transcription elongation complex. DR ComplexPortal; CPX-5780; lambdaN-dependent processive transcription antitermination complex. DR DIP; DIP-35879N; -. DR IntAct; P0A7Z4; 97. DR MINT; P0A7Z4; -. DR STRING; 511145.b3295; -. DR BindingDB; P0A7Z4; -. DR ChEMBL; CHEMBL2364672; -. DR ChEMBL; CHEMBL4296169; -. DR DrugBank; DB00615; Rifabutin. DR DrugBank; DB11753; Rifamycin. DR DrugCentral; P0A7Z4; -. DR iPTMnet; P0A7Z4; -. DR jPOST; P0A7Z4; -. DR PaxDb; 511145-b3295; -. DR EnsemblBacteria; AAC76320; AAC76320; b3295. DR GeneID; 84234862; -. DR GeneID; 947794; -. DR KEGG; ecj:JW3257; -. DR KEGG; eco:b3295; -. DR PATRIC; fig|1411691.4.peg.3436; -. DR EchoBASE; EB0886; -. DR eggNOG; COG0202; Bacteria. DR HOGENOM; CLU_053084_0_0_6; -. DR InParanoid; P0A7Z4; -. DR OMA; PIKNVKY; -. DR OrthoDB; 9805706at2; -. DR PhylomeDB; P0A7Z4; -. DR BioCyc; EcoCyc:EG10893-MONOMER; -. DR BioCyc; MetaCyc:EG10893-MONOMER; -. DR BRENDA; 2.7.7.6; 2026. DR EvolutionaryTrace; P0A7Z4; -. DR PRO; PR:P0A7Z4; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005737; C:cytoplasm; HDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0000345; C:cytosolic DNA-directed RNA polymerase complex; IPI:ComplexPortal. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0008023; C:transcription elongation factor complex; NAS:ComplexPortal. 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:0044780; P:bacterial-type flagellum assembly; NAS:ComplexPortal. DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; NAS:ComplexPortal. DR GO; GO:0048870; P:cell motility; NAS:ComplexPortal. DR GO; GO:0036460; P:cellular response to cell envelope stress; NAS:ComplexPortal. DR GO; GO:0006352; P:DNA-templated transcription initiation; IDA:ComplexPortal. DR GO; GO:0006879; P:intracellular iron ion homeostasis; NAS:ComplexPortal. DR GO; GO:0042128; P:nitrate assimilation; NAS:ComplexPortal. DR GO; GO:0032784; P:regulation of DNA-templated transcription elongation; NAS:ComplexPortal. DR GO; GO:2000142; P:regulation of DNA-templated transcription initiation; IDA:ComplexPortal. DR GO; GO:0009408; P:response to heat; NAS:ComplexPortal. DR GO; GO:0090605; P:submerged biofilm formation; NAS:ComplexPortal. DR GO; GO:0031564; P:transcription antitermination; IDA:ComplexPortal. DR CDD; cd06928; RNAP_alpha_NTD; 1. DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1. DR Gene3D; 2.170.120.12; DNA-directed RNA polymerase, insert domain; 1. DR Gene3D; 3.30.1360.10; RNA polymerase, RBP11-like subunit; 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 NCBIfam; TIGR02027; rpoA; 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; SSF47789; C-terminal domain of RNA polymerase alpha subunit; 1. DR SUPFAM; SSF56553; Insert subdomain of RNA polymerase alpha subunit; 1. DR SUPFAM; SSF55257; RBP11-like subunits of RNA polymerase; 1. DR SWISS-2DPAGE; P0A7Z4; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ADP-ribosylation; Direct protein sequencing; KW DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome; KW Transcription; Transferase. FT CHAIN 1..329 FT /note="DNA-directed RNA polymerase subunit alpha" FT /id="PRO_0000175304" FT REGION 1..235 FT /note="Alpha N-terminal domain (alpha-NTD)" FT REGION 162..165 FT /note="Required for interaction with Crp at class II FT promoters" FT REGION 249..329 FT /note="Alpha C-terminal domain (alpha-CTD); not required FT for RNAP assembly or function" FT MOD_RES 265 FT /note="ADP-ribosylarginine" FT /evidence="ECO:0000269|PubMed:4371081" FT MOD_RES 297 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:21696463" FT MOD_RES 298 FT /note="N6-acetyllysine; by PatZ" FT /evidence="ECO:0000269|PubMed:21696463" FT MUTAGEN 45 FT /note="R->C: In rpoA112; temperature-sensitive, blocks RNA FT polymerase assembly." FT /evidence="ECO:0000269|PubMed:2235479" FT MUTAGEN 162..165 FT /note="EEDE->AAAA: 5-fold decrease in CRP-class II FT promoter-dependent transcription." FT /evidence="ECO:0000269|PubMed:8978616" FT MUTAGEN 165 FT /note="E->K: 5-fold decrease in CRP-class II FT promoter-dependent transcription." FT /evidence="ECO:0000269|PubMed:8978616" FT MUTAGEN 191 FT /note="R->C: In rpoA101; temperature-sensitive." FT /evidence="ECO:0000269|PubMed:2235479" FT CONFLICT 4 FT /note="S -> N (in Ref. 11; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 208 FT /note="N -> T (in Ref. 4; CAA26395)" FT /evidence="ECO:0000305" FT STRAND 12..18 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 20..31 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 35..50 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 52..61 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 67..69 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 78..86 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 90..92 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 96..111 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 112..114 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 121..124 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 129..133 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 135..137 FT /evidence="ECO:0007829|PDB:8FVR" FT STRAND 139..153 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 155..157 FT /evidence="ECO:0007829|PDB:8FVR" FT STRAND 159..161 FT /evidence="ECO:0007829|PDB:6XL5" FT STRAND 162..164 FT /evidence="ECO:0007829|PDB:6OUL" FT TURN 167..169 FT /evidence="ECO:0007829|PDB:7UWH" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 175..177 FT /evidence="ECO:0007829|PDB:7UWE" FT STRAND 180..189 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 193..196 FT /evidence="ECO:0007829|PDB:5UAG" FT STRAND 199..207 FT /evidence="ECO:0007829|PDB:8FVW" FT STRAND 209..211 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 213..232 FT /evidence="ECO:0007829|PDB:8FVW" FT HELIX 251..254 FT /evidence="ECO:0007829|PDB:3K4G" FT HELIX 257..260 FT /evidence="ECO:0007829|PDB:3K4G" FT HELIX 264..270 FT /evidence="ECO:0007829|PDB:3K4G" FT TURN 271..274 FT /evidence="ECO:0007829|PDB:3N4M" FT HELIX 278..283 FT /evidence="ECO:0007829|PDB:3K4G" FT HELIX 286..290 FT /evidence="ECO:0007829|PDB:3K4G" FT STRAND 292..294 FT /evidence="ECO:0007829|PDB:7QWP" FT HELIX 297..299 FT /evidence="ECO:0007829|PDB:1XS9" FT HELIX 300..303 FT /evidence="ECO:0007829|PDB:3K4G" FT HELIX 308..310 FT /evidence="ECO:0007829|PDB:3K4G" FT TURN 312..314 FT /evidence="ECO:0007829|PDB:7QV9" FT STRAND 318..322 FT /evidence="ECO:0007829|PDB:3K4G" 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 //