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P0A8T7

- RPOC_ECOLI

UniProt

P0A8T7 - RPOC_ECOLI

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Protein

DNA-directed RNA polymerase subunit beta'

Gene

rpoC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.1 PublicationUniRule annotation

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).UniRule annotation

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-HAMAP
  2. DNA-directed RNA polymerase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. transcription, DNA-templated Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Transcription

Enzyme and pathway databases

BioCyciEcoCyc:RPOC-MONOMER.
ECOL316407:JW3951-MONOMER.
MetaCyc:RPOC-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerase subunit beta'UniRule annotation (EC:2.7.7.6UniRule annotation)
Short name:
RNAP subunit beta'UniRule annotation
Alternative name(s):
RNA polymerase subunit beta'UniRule annotation
Transcriptase subunit beta'UniRule annotation
Gene namesi
Name:rpoCUniRule annotation
Synonyms:tabB
Ordered Locus Names:b3988, JW3951
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10895. rpoC.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. DNA-directed RNA polymerase complex Source: RefGenome
  3. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14071407DNA-directed RNA polymerase subunit beta'PRO_0000067741Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei983 – 9831N6-acetyllysine1 PublicationUniRule annotation

Post-translational modificationi

Acetylated on several lysine residues in the presence of glucose.2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0A8T7.
PRIDEiP0A8T7.

PTM databases

PhosSiteiP010445.

Expressioni

Gene expression databases

GenevestigatoriP0A8T7.

Interactioni

Subunit structurei

The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
htpGP0A6Z32EBI-543604,EBI-369221
rpoBP0A8V27EBI-543604,EBI-544996
rpoDP005798EBI-543604,EBI-545104

Protein-protein interaction databases

DIPiDIP-35803N.
IntActiP0A8T7. 113 interactions.
MINTiMINT-1220667.
STRINGi511145.b3988.

Structurei

Secondary structure

1
1407
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi945 – 9484
Beta strandi949 – 9513
Beta strandi956 – 9627
Beta strandi965 – 9673
Beta strandi973 – 9753
Beta strandi981 – 9855
Beta strandi991 – 9966
Beta strandi1002 – 10054
Beta strandi1016 – 10194
Beta strandi1022 – 10287
Beta strandi1033 – 10397
Turni1043 – 10453
Beta strandi1046 – 10494
Turni1052 – 10543
Beta strandi1058 – 10614
Helixi1064 – 10663
Helixi1071 – 10733
Beta strandi1077 – 10815
Beta strandi1093 – 10964
Beta strandi1098 – 11003
Beta strandi1106 – 11094
Beta strandi1120 – 11256
Beta strandi1155 – 116612
Beta strandi1169 – 11713
Beta strandi1174 – 118310
Beta strandi1186 – 11894
Beta strandi1202 – 12043
Beta strandi1209 – 12113

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AUKX-ray2.30A/B/C/D/E944-1129[»]
2LMCNMR-B1151-1213[»]
3IYDelectron microscopy-D1-1407[»]
3LU0electron microscopy-D1-1407[»]
4IGCX-ray3.70D/I1-1407[»]
4IQZX-ray2.10A/B/C/D/E932-1141[»]
4JK1X-ray3.90D/I1-1407[»]
4JK2X-ray4.20D/I1-1407[»]
4KMUX-ray3.85D/I1-1407[»]
4KN4X-ray3.96D/I1-1407[»]
4KN7X-ray3.69D/I1-1407[»]
4MEXX-ray3.90D/J1-1407[»]
4MEYX-ray3.95D/J1-1407[»]
ProteinModelPortaliP0A8T7.
SMRiP0A8T7. Positions 15-1382.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A8T7.

Family & Domainsi

Sequence similaritiesi

Belongs to the RNA polymerase beta' chain family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0086.
HOGENOMiHOG000218386.
InParanoidiP0A8T7.
KOiK03046.
OMAiYDLVNQN.
OrthoDBiEOG6M9DS6.
PhylomeDBiP0A8T7.

Family and domain databases

HAMAPiMF_01322. RNApol_bact_RpoC.
MF_01323. RNApol_bact_RpoC1.
InterProiIPR012754. DNA-dir_RpoC_beta_prime.
IPR000722. RNA_pol_asu.
IPR006592. RNA_pol_N.
IPR007080. RNA_pol_Rpb1_1.
IPR007066. RNA_pol_Rpb1_3.
IPR007083. RNA_pol_Rpb1_4.
IPR007081. RNA_pol_Rpb1_5.
[Graphical view]
PfamiPF04997. RNA_pol_Rpb1_1. 1 hit.
PF00623. RNA_pol_Rpb1_2. 1 hit.
PF04983. RNA_pol_Rpb1_3. 1 hit.
PF05000. RNA_pol_Rpb1_4. 1 hit.
PF04998. RNA_pol_Rpb1_5. 1 hit.
[Graphical view]
SMARTiSM00663. RPOLA_N. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02386. rpoC_TIGR. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A8T7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKDLLKFLKA QTKTEEFDAI KIALASPDMI RSWSFGEVKK PETINYRTFK
60 70 80 90 100
PERDGLFCAR IFGPVKDYEC LCGKYKRLKH RGVICEKCGV EVTQTKVRRE
110 120 130 140 150
RMGHIELASP TAHIWFLKSL PSRIGLLLDM PLRDIERVLY FESYVVIEGG
160 170 180 190 200
MTNLERQQIL TEEQYLDALE EFGDEFDAKM GAEAIQALLK SMDLEQECEQ
210 220 230 240 250
LREELNETNS ETKRKKLTKR IKLLEAFVQS GNKPEWMILT VLPVLPPDLR
260 270 280 290 300
PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLLDLAAPDI IVRNEKRMLQ
310 320 330 340 350
EAVDALLDNG RRGRAITGSN KRPLKSLADM IKGKQGRFRQ NLLGKRVDYS
360 370 380 390 400
GRSVITVGPY LRLHQCGLPK KMALELFKPF IYGKLELRGL ATTIKAAKKM
410 420 430 440 450
VEREEAVVWD ILDEVIREHP VLLNRAPTLH RLGIQAFEPV LIEGKAIQLH
460 470 480 490 500
PLVCAAYNAD FDGDQMAVHV PLTLEAQLEA RALMMSTNNI LSPANGEPII
510 520 530 540 550
VPSQDVVLGL YYMTRDCVNA KGEGMVLTGP KEAERLYRSG LASLHARVKV
560 570 580 590 600
RITEYEKDAN GELVAKTSLK DTTVGRAILW MIVPKGLPYS IVNQALGKKA
610 620 630 640 650
ISKMLNTCYR ILGLKPTVIF ADQIMYTGFA YAARSGASVG IDDMVIPEKK
660 670 680 690 700
HEIISEAEAE VAEIQEQFQS GLVTAGERYN KVIDIWAAAN DRVSKAMMDN
710 720 730 740 750
LQTETVINRD GQEEKQVSFN SIYMMADSGA RGSAAQIRQL AGMRGLMAKP
760 770 780 790 800
DGSIIETPIT ANFREGLNVL QYFISTHGAR KGLADTALKT ANSGYLTRRL
810 820 830 840 850
VDVAQDLVVT EDDCGTHEGI MMTPVIEGGD VKEPLRDRVL GRVTAEDVLK
860 870 880 890 900
PGTADILVPR NTLLHEQWCD LLEENSVDAV KVRSVVSCDT DFGVCAHCYG
910 920 930 940 950
RDLARGHIIN KGEAIGVIAA QSIGEPGTQL TMRTFHIGGA ASRAAAESSI
960 970 980 990 1000
QVKNKGSIKL SNVKSVVNSS GKLVITSRNT ELKLIDEFGR TKESYKVPYG
1010 1020 1030 1040 1050
AVLAKGDGEQ VAGGETVANW DPHTMPVITE VSGFVRFTDM IDGQTITRQT
1060 1070 1080 1090 1100
DELTGLSSLV VLDSAERTAG GKDLRPALKI VDAQGNDVLI PGTDMPAQYF
1110 1120 1130 1140 1150
LPGKAIVQLE DGVQISSGDT LARIPQESGG TKDITGGLPR VADLFEARRP
1160 1170 1180 1190 1200
KEPAILAEIS GIVSFGKETK GKRRLVITPV DGSDPYEEMI PKWRQLNVFE
1210 1220 1230 1240 1250
GERVERGDVI SDGPEAPHDI LRLRGVHAVT RYIVNEVQDV YRLQGVKIND
1260 1270 1280 1290 1300
KHIEVIVRQM LRKATIVNAG SSDFLEGEQV EYSRVKIANR ELEANGKVGA
1310 1320 1330 1340 1350
TYSRDLLGIT KASLATESFI SAASFQETTR VLTEAAVAGK RDELRGLKEN
1360 1370 1380 1390 1400
VIVGRLIPAG TGYAYHQDRM RRRAAGEAPA APQVTAEDAS ASLAELLNAG

LGGSDNE
Length:1,407
Mass (Da):155,160
Last modified:July 21, 1986 - v1
Checksum:iA6878C61D15F4961
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1133 – 117745DITGG…RRLVI → ASPVVCRALRTCSKHVVRKS RQSWLKSAVSFPSVKKPKVN VVWLS(PubMed:6278450)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
V00339 Genomic DNA. Translation: CAA23626.1.
U00006 Genomic DNA. Translation: AAC43086.1.
U00096 Genomic DNA. Translation: AAC76962.1.
AP009048 Genomic DNA. Translation: BAE77332.1.
M38293 Genomic DNA. Translation: AAA24582.1.
M38303 Genomic DNA. Translation: AAA24584.1. Sequence problems.
V00340 Genomic DNA. Translation: CAA23628.1.
M38305 Genomic DNA. Translation: AAA24586.1.
M38288 Genomic DNA. Translation: AAA24408.1.
PIRiA00695. RNECC.
RefSeqiNP_418415.1. NC_000913.3.
YP_491473.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76962; AAC76962; b3988.
BAE77332; BAE77332; BAE77332.
GeneIDi12933965.
948487.
KEGGiecj:Y75_p3209.
eco:b3988.
PATRICi32123497. VBIEscCol129921_4101.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
V00339 Genomic DNA. Translation: CAA23626.1 .
U00006 Genomic DNA. Translation: AAC43086.1 .
U00096 Genomic DNA. Translation: AAC76962.1 .
AP009048 Genomic DNA. Translation: BAE77332.1 .
M38293 Genomic DNA. Translation: AAA24582.1 .
M38303 Genomic DNA. Translation: AAA24584.1 . Sequence problems.
V00340 Genomic DNA. Translation: CAA23628.1 .
M38305 Genomic DNA. Translation: AAA24586.1 .
M38288 Genomic DNA. Translation: AAA24408.1 .
PIRi A00695. RNECC.
RefSeqi NP_418415.1. NC_000913.3.
YP_491473.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2AUK X-ray 2.30 A/B/C/D/E 944-1129 [» ]
2LMC NMR - B 1151-1213 [» ]
3IYD electron microscopy - D 1-1407 [» ]
3LU0 electron microscopy - D 1-1407 [» ]
4IGC X-ray 3.70 D/I 1-1407 [» ]
4IQZ X-ray 2.10 A/B/C/D/E 932-1141 [» ]
4JK1 X-ray 3.90 D/I 1-1407 [» ]
4JK2 X-ray 4.20 D/I 1-1407 [» ]
4KMU X-ray 3.85 D/I 1-1407 [» ]
4KN4 X-ray 3.96 D/I 1-1407 [» ]
4KN7 X-ray 3.69 D/I 1-1407 [» ]
4MEX X-ray 3.90 D/J 1-1407 [» ]
4MEY X-ray 3.95 D/J 1-1407 [» ]
ProteinModelPortali P0A8T7.
SMRi P0A8T7. Positions 15-1382.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35803N.
IntActi P0A8T7. 113 interactions.
MINTi MINT-1220667.
STRINGi 511145.b3988.

Chemistry

ChEMBLi CHEMBL2364672.
DrugBanki DB00615. Rifabutin.
DB01045. Rifampicin.

PTM databases

PhosSitei P010445.

Proteomic databases

PaxDbi P0A8T7.
PRIDEi P0A8T7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76962 ; AAC76962 ; b3988 .
BAE77332 ; BAE77332 ; BAE77332 .
GeneIDi 12933965.
948487.
KEGGi ecj:Y75_p3209.
eco:b3988.
PATRICi 32123497. VBIEscCol129921_4101.

Organism-specific databases

EchoBASEi EB0888.
EcoGenei EG10895. rpoC.

Phylogenomic databases

eggNOGi COG0086.
HOGENOMi HOG000218386.
InParanoidi P0A8T7.
KOi K03046.
OMAi YDLVNQN.
OrthoDBi EOG6M9DS6.
PhylomeDBi P0A8T7.

Enzyme and pathway databases

BioCyci EcoCyc:RPOC-MONOMER.
ECOL316407:JW3951-MONOMER.
MetaCyc:RPOC-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A8T7.
PROi P0A8T7.

Gene expression databases

Genevestigatori P0A8T7.

Family and domain databases

HAMAPi MF_01322. RNApol_bact_RpoC.
MF_01323. RNApol_bact_RpoC1.
InterProi IPR012754. DNA-dir_RpoC_beta_prime.
IPR000722. RNA_pol_asu.
IPR006592. RNA_pol_N.
IPR007080. RNA_pol_Rpb1_1.
IPR007066. RNA_pol_Rpb1_3.
IPR007083. RNA_pol_Rpb1_4.
IPR007081. RNA_pol_Rpb1_5.
[Graphical view ]
Pfami PF04997. RNA_pol_Rpb1_1. 1 hit.
PF00623. RNA_pol_Rpb1_2. 1 hit.
PF04983. RNA_pol_Rpb1_3. 1 hit.
PF05000. RNA_pol_Rpb1_4. 1 hit.
PF04998. RNA_pol_Rpb1_5. 1 hit.
[Graphical view ]
SMARTi SM00663. RPOLA_N. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR02386. rpoC_TIGR. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The primary structure of E. coli RNA polymerase, Nucleotide sequence of the rpoC gene and amino acid sequence of the beta'-subunit."
    Ovchinnikov Y.A., Monastyrskaya G.S., Gubanov V.V., Guryev S.O., Salomatina I.S., Shuvaeva T.M., Lipkin V.M., Sverdlov E.D.
    Nucleic Acids Res. 10:4035-4044(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-8, PARTIAL PROTEIN SEQUENCE.
  2. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
    Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
    Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Primary structure of EcoRI-F fragment of rpoB, C genes and corresponding fragments of beta- and beta'-subunits of RNA polymerase from E.coli."
    Monastyrskaya G.S., Gubanov V.V., Guryev S.O., Lipkin V.M., Sverdlov E.D.
    Bioorg. Khim. 6:1106-1109(1980)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-176.
  6. "Structure of a central part of E.coli operon rpoBC. Nucleotide sequence of the gene for beta subunit of RNA polymerase."
    Gurevich A.I., Igoshin A.V., Kolosov M.N.
    Bioorg. Khim. 6:1580-1584(1980)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-176.
  7. "The primary structure of Escherichia coli RNA polymerase. Nucleotide sequence of the rpoB gene and amino-acid sequence of the beta-subunit."
    Ovchinnikov Y.A., Monastyrskaya G.S., Gubanov V.V., Guryev S.O., Chertov O.Y., Modyanov N.N., Grinkevich V.A., Makarova I.A., Marchenko T.V., Polovnikova I.N., Lipkin V.M., Sverdlov E.D.
    Eur. J. Biochem. 116:621-629(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-176, PROTEIN SEQUENCE OF 1-8.
  8. "The subunits of DNA-dependent RNA polymerase from E. coli: I. Amino acid analysis and primary structure of the N-terminal regions."
    Fujiki H., Zurek G.
    FEBS Lett. 55:242-244(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-4.
    Strain: K12.
  9. "Primary structure of EcoRI-D fragment of rpoC gene and corresponding fragment of beta-subunit of RNA polymerase from E.coli."
    Monastyrskaya G.S., Guryev S.O., Kalinina N.F., Sorokin A.V., Salomatina I.S., Shuvaeva T.M., Lipkin V.M., Sverdlov E.D., Ovchinnikov Y.A.
    Bioorg. Khim. 8:130-134(1982)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 175-988.
  10. "Primary structure of RNA polymerase from E.coli. Nucleotide sequence of E.coli DNA fragment containing a part of the rpoC gene and the corresponding C-terminal amino acid sequence of beta'-subunit."
    Ovchinnikov Y.A., Monastyrskaya G.S., Gubanov V.V., Salomatina I.S., Shuvaeva T.M., Lipkin V.M., Sverdlov E.D.
    Bioorg. Khim. 7:1107-1112(1981)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 987-1407.
  11. "Nucleotide sequence at the end of the gene for the RNA polymerase beta' subunit (rpoC)."
    Squires C., Krainer A., Barry G., Shen W.-F., Squires C.L.
    Nucleic Acids Res. 9:6827-6840(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1073-1407.
    Strain: K12.
  12. "Bipartite functional map of the E. coli RNA polymerase alpha subunit: involvement of the C-terminal region in transcription activation by cAMP-CRP."
    Igarashi K., Ishihama A.
    Cell 65:1015-1022(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRANSCRIPTION, SUBUNIT.
  13. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-983, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  14. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  15. "Involvement of protein acetylation in glucose-induced transcription of a stress-responsive promoter."
    Lima B.P., Antelmann H., Gronau K., Chi B.K., Becher D., Brinsmade S.R., Wolfe A.J.
    Mol. Microbiol. 81:1190-1204(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION.
  16. "Three-dimensional EM structure of an intact activator-dependent transcription initiation complex."
    Hudson B.P., Quispe J., Lara-Gonzalez S., Kim Y., Berman H.M., Arnold E., Ebright R.H., Lawson C.L.
    Proc. Natl. Acad. Sci. U.S.A. 106:19830-19835(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (19.80 ANGSTROMS) IN COMPLEX WITH RPOA; RPOB; RPOD; RPOZ; CRP AND DNA, DNA-BINDING, SUBUNIT.

Entry informationi

Entry nameiRPOC_ECOLI
AccessioniPrimary (citable) accession number: P0A8T7
Secondary accession number(s): P00577
, P00578, P78134, Q2M8S4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 29, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3