Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0A7Z4

- RPOA_ECOLI

UniProt

P0A7Z4 - RPOA_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

DNA-directed RNA polymerase subunit alpha

Gene

rpoA

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

Functioni

DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme.1 Publication

Catalytic activityi

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

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-HAMAP
  2. DNA-directed RNA polymerase activity Source: UniProtKB-HAMAP
  3. zinc ion binding Source: EcoliWiki

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:EG10893-MONOMER.
ECOL316407:JW3257-MONOMER.
MetaCyc:EG10893-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerase subunit alpha (EC:2.7.7.6)
Short name:
RNAP subunit alpha
Alternative name(s):
RNA polymerase subunit alpha
Transcriptase subunit alpha
Gene namesi
Name:rpoA
Synonyms:pez, phs, sez
Ordered Locus Names:b3295, JW3257
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10893. rpoA.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi45 – 451R → C in rpoA112; temperature-sensitive, blocks RNA polymerase assembly. 1 Publication
Mutagenesisi162 – 1654EEDE → AAAA: 5-fold decrease in CRP-class II promoter-dependent transcription. 1 Publication
Mutagenesisi165 – 1651E → K: 5-fold decrease in CRP-class II promoter-dependent transcription. 1 Publication
Mutagenesisi191 – 1911R → C in rpoA101; temperature-sensitive. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 329329DNA-directed RNA polymerase subunit alphaPRO_0000175304Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei297 – 2971N6-acetyllysine1 Publication
Modified residuei298 – 2981N6-acetyllysine; by Pka1 Publication

Post-translational modificationi

Acetylated on Lys-297 and Lys-298 in the presence of glucose. Pka controls acetylation of Lys-298 but not of Lys-297.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0A7Z4.
PRIDEiP0A7Z4.

2D gel databases

SWISS-2DPAGEP0A7Z4.

Expressioni

Gene expression databases

GenevestigatoriP0A7Z4.

Interactioni

Subunit structurei

Homodimer. 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. Both the N- and C-terminus interact with different regions of transcriptional regulator CRP.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
rplBP604225EBI-544985,EBI-543515

Protein-protein interaction databases

BioGridi852106. 1 interaction.
DIPiDIP-35879N.
IntActiP0A7Z4. 85 interactions.
MINTiMINT-6478247.
STRINGi511145.b3295.

Structurei

Secondary structure

1
329
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 3220Combined sources
Helixi35 – 4713Combined sources
Beta strandi54 – 618Combined sources
Beta strandi74 – 763Combined sources
Helixi78 – 869Combined sources
Beta strandi96 – 11116Combined sources
Helixi112 – 1143Combined sources
Beta strandi122 – 1243Combined sources
Beta strandi129 – 1335Combined sources
Beta strandi139 – 14810Combined sources
Beta strandi151 – 1533Combined sources
Helixi155 – 1573Combined sources
Beta strandi179 – 1868Combined sources
Beta strandi196 – 20712Combined sources
Beta strandi209 – 2113Combined sources
Helixi213 – 22715Combined sources
Helixi228 – 2314Combined sources
Helixi251 – 2544Combined sources
Helixi257 – 2604Combined sources
Helixi264 – 2729Combined sources
Helixi278 – 2836Combined sources
Helixi286 – 2905Combined sources
Beta strandi292 – 2943Combined sources
Helixi297 – 30812Combined sources
Turni309 – 3113Combined sources
Beta strandi318 – 3225Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BDFX-ray2.50A/B/C/D1-235[»]
1COONMR-A233-329[»]
1LB2X-ray3.10B/E246-329[»]
1XS9NMR-D249-329[»]
3IYDelectron microscopy-A/B1-329[»]
3K4GX-ray2.05A/B/C/D/E/F/G/H245-329[»]
3LU0electron microscopy-A/B1-329[»]
3N4MX-ray2.99B/C246-329[»]
3N97X-ray3.25B/C246-329[»]
4IGCX-ray3.70A/B/F/G1-329[»]
4JK1X-ray3.90A/B/F/G1-329[»]
4JK2X-ray4.20A/B/F/G1-329[»]
4KMUX-ray3.85A/B/F/G1-329[»]
4KN4X-ray3.96A/B/F/G1-329[»]
4KN7X-ray3.69A/B/F/G1-329[»]
4MEXX-ray3.90A/B/G/H1-329[»]
4MEYX-ray3.95A/B/G/H1-329[»]
ProteinModelPortaliP0A7Z4.
SMRiP0A7Z4. Positions 3-325.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7Z4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 235235Alpha N-terminal domain (alpha-NTD)Add
BLAST
Regioni162 – 1654Required for interaction with Crp at class II promoters
Regioni249 – 32981Alpha C-terminal domain (alpha-CTD); not required for RNAP assembly or functionAdd
BLAST

Domaini

The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators (such as CRP) and with upstream promoter elements.2 Publications

Sequence similaritiesi

Belongs to the RNA polymerase alpha chain family.Curated

Phylogenomic databases

eggNOGiCOG0202.
HOGENOMiHOG000218481.
InParanoidiP0A7Z4.
KOiK03040.
OMAiKAESIHY.
OrthoDBiEOG68WR84.
PhylomeDBiP0A7Z4.

Family and domain databases

Gene3Di2.170.120.12. 1 hit.
HAMAPiMF_00059. RNApol_bact_RpoA.
InterProiIPR011262. DNA-dir_RNA_pol_insert.
IPR011263. DNA-dir_RNA_pol_RpoA/D/Rpb3.
IPR011773. DNA-dir_RpoA.
IPR009025. RBP11-like_dimer.
IPR011260. RNAP_asu_C.
[Graphical view]
PfamiPF01000. RNA_pol_A_bac. 1 hit.
PF03118. RNA_pol_A_CTD. 1 hit.
PF01193. RNA_pol_L. 1 hit.
[Graphical view]
ProDomiPD001179. RNAP_asu_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00662. RPOLD. 1 hit.
[Graphical view]
SUPFAMiSSF55257. SSF55257. 2 hits.
SSF56553. SSF56553. 1 hit.
TIGRFAMsiTIGR02027. rpoA. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A7Z4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQGSVTEFLK PRLVDIEQVS STHAKVTLEP LERGFGHTLG NALRRILLSS
60 70 80 90 100
MPGCAVTEVE IDGVLHEYST KEGVQEDILE ILLNLKGLAV RVQGKDEVIL
110 120 130 140 150
TLNKSGIGPV TAADITHDGD VEIVKPQHVI CHLTDENASI SMRIKVQRGR
160 170 180 190 200
GYVPASTRIH SEEDERPIGR LLVDACYSPV ERIAYNVEAA RVEQRTDLDK
210 220 230 240 250
LVIEMETNGT IDPEEAIRRA ATILAEQLEA FVDLRDVRQP EVKEEKPEFD
260 270 280 290 300
PILLRPVDDL ELTVRSANCL KAEAIHYIGD LVQRTEVELL KTPNLGKKSL
310 320
TEIKDVLASR GLSLGMRLEN WPPASIADE
Length:329
Mass (Da):36,512
Last modified:July 21, 1986 - v1
Checksum:i12A14B75A3CAEA19
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41S → N AA sequence (PubMed:1095419)Curated
Sequence conflicti208 – 2081N → T in CAA26395. (PubMed:2989779)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01685 Genomic DNA. Translation: AAA24577.1.
X00766 Genomic DNA. Translation: CAA25337.1.
X02543 Genomic DNA. Translation: CAA26395.1.
U18997 Genomic DNA. Translation: AAA58092.1.
X53843 Genomic DNA. Translation: CAA37838.1.
X53844 Genomic DNA. Translation: CAA37839.1.
U00096 Genomic DNA. Translation: AAC76320.1.
AP009048 Genomic DNA. Translation: BAE77996.1.
V00353 Genomic DNA. Translation: CAA23646.1.
M29822 Genomic DNA. Translation: AAA24590.1.
M29823 Genomic DNA. Translation: AAA24592.1.
M29824 Genomic DNA. Translation: AAA24594.1.
PIRiA22884. RNECA.
RefSeqiNP_417754.1. NC_000913.3.
YP_492137.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76320; AAC76320; b3295.
BAE77996; BAE77996; BAE77996.
GeneIDi12934404.
947794.
KEGGiecj:Y75_p3881.
eco:b3295.
PATRICi32122022. VBIEscCol129921_3388.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01685 Genomic DNA. Translation: AAA24577.1 .
X00766 Genomic DNA. Translation: CAA25337.1 .
X02543 Genomic DNA. Translation: CAA26395.1 .
U18997 Genomic DNA. Translation: AAA58092.1 .
X53843 Genomic DNA. Translation: CAA37838.1 .
X53844 Genomic DNA. Translation: CAA37839.1 .
U00096 Genomic DNA. Translation: AAC76320.1 .
AP009048 Genomic DNA. Translation: BAE77996.1 .
V00353 Genomic DNA. Translation: CAA23646.1 .
M29822 Genomic DNA. Translation: AAA24590.1 .
M29823 Genomic DNA. Translation: AAA24592.1 .
M29824 Genomic DNA. Translation: AAA24594.1 .
PIRi A22884. RNECA.
RefSeqi NP_417754.1. NC_000913.3.
YP_492137.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BDF X-ray 2.50 A/B/C/D 1-235 [» ]
1COO NMR - A 233-329 [» ]
1LB2 X-ray 3.10 B/E 246-329 [» ]
1XS9 NMR - D 249-329 [» ]
3IYD electron microscopy - A/B 1-329 [» ]
3K4G X-ray 2.05 A/B/C/D/E/F/G/H 245-329 [» ]
3LU0 electron microscopy - A/B 1-329 [» ]
3N4M X-ray 2.99 B/C 246-329 [» ]
3N97 X-ray 3.25 B/C 246-329 [» ]
4IGC X-ray 3.70 A/B/F/G 1-329 [» ]
4JK1 X-ray 3.90 A/B/F/G 1-329 [» ]
4JK2 X-ray 4.20 A/B/F/G 1-329 [» ]
4KMU X-ray 3.85 A/B/F/G 1-329 [» ]
4KN4 X-ray 3.96 A/B/F/G 1-329 [» ]
4KN7 X-ray 3.69 A/B/F/G 1-329 [» ]
4MEX X-ray 3.90 A/B/G/H 1-329 [» ]
4MEY X-ray 3.95 A/B/G/H 1-329 [» ]
ProteinModelPortali P0A7Z4.
SMRi P0A7Z4. Positions 3-325.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 852106. 1 interaction.
DIPi DIP-35879N.
IntActi P0A7Z4. 85 interactions.
MINTi MINT-6478247.
STRINGi 511145.b3295.

Chemistry

ChEMBLi CHEMBL2364672.
DrugBanki DB00615. Rifabutin.

2D gel databases

SWISS-2DPAGE P0A7Z4.

Proteomic databases

PaxDbi P0A7Z4.
PRIDEi P0A7Z4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76320 ; AAC76320 ; b3295 .
BAE77996 ; BAE77996 ; BAE77996 .
GeneIDi 12934404.
947794.
KEGGi ecj:Y75_p3881.
eco:b3295.
PATRICi 32122022. VBIEscCol129921_3388.

Organism-specific databases

EchoBASEi EB0886.
EcoGenei EG10893. rpoA.

Phylogenomic databases

eggNOGi COG0202.
HOGENOMi HOG000218481.
InParanoidi P0A7Z4.
KOi K03040.
OMAi KAESIHY.
OrthoDBi EOG68WR84.
PhylomeDBi P0A7Z4.

Enzyme and pathway databases

BioCyci EcoCyc:EG10893-MONOMER.
ECOL316407:JW3257-MONOMER.
MetaCyc:EG10893-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A7Z4.
PROi P0A7Z4.

Gene expression databases

Genevestigatori P0A7Z4.

Family and domain databases

Gene3Di 2.170.120.12. 1 hit.
HAMAPi MF_00059. RNApol_bact_RpoA.
InterProi IPR011262. DNA-dir_RNA_pol_insert.
IPR011263. DNA-dir_RNA_pol_RpoA/D/Rpb3.
IPR011773. DNA-dir_RpoA.
IPR009025. RBP11-like_dimer.
IPR011260. RNAP_asu_C.
[Graphical view ]
Pfami PF01000. RNA_pol_A_bac. 1 hit.
PF03118. RNA_pol_A_CTD. 1 hit.
PF01193. RNA_pol_L. 1 hit.
[Graphical view ]
ProDomi PD001179. RNAP_asu_C. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00662. RPOLD. 1 hit.
[Graphical view ]
SUPFAMi SSF55257. SSF55257. 2 hits.
SSF56553. SSF56553. 1 hit.
TIGRFAMsi TIGR02027. rpoA. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of alpha-subunit of DNA-dependent RNA polymerase from Escherichia coli."
    Ovchinnikov Y.A., Lipkin V.M., Modyanov N.N., Chertov O.Y., Smirnov Y.V.
    FEBS Lett. 76:108-111(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. "The primary structure of alpha-subunit of DNA-dependent RNA polymerase from E. coli. V. The cyanogen bromide peptides."
    Modyanov N.N., Lipkin V.M., Smirnov Y.V., Shuvaeva T.M., Kocherginskaya S.A.
    Bioorg. Khim. 4:437-449(1978)
    Cited for: PROTEIN SEQUENCE.
  3. "Nucleotide sequence of the rpoA-rplQ DNA of Escherichia coli: a second regulatory binding site for protein S4?"
    Meek D.W., Hayward R.S.
    Nucleic Acids Res. 12:5813-5821(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Nucleotide sequence of the alpha ribosomal protein operon of Escherichia coli."
    Bedwell D.M., Davis G.R., Gosink M., Post L.E., Nomura M., Kestler H., Zengel J.M., Lindahl L.
    Nucleic Acids Res. 13:3891-3903(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  5. "Sequence analysis of two temperature-sensitive mutations in the alpha subunit gene (rpoA) of Escherichia coli RNA polymerase."
    Igarashi K., Fujita N., Ishihama A.
    Nucleic Acids Res. 18:5945-5948(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DOMAIN, SUBUNIT, MUTAGENESIS OF ARG-45 AND ARG-191.
    Strain: K12.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  7. "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.
  8. "Nucleotide sequence of the intercistronic region preceding the gene for RNA polymerase subunit alpha in Escherichia coli."
    Post L.E., Nomura M.
    J. Biol. Chem. 254:10604-10606(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-159.
  9. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-19.
    Strain: K12 / EMG2.
  10. "Unstable mutations caused by regional tandem multiplications in the gene for ribosomal protein S4 show thermosensitivity in Escherichia coli."
    Schnier J., Isono S., Cumberlidge A.G., Isono K.
    Mol. Gen. Genet. 199:265-270(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
    Strain: K12.
  11. "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.
  12. "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.
  13. "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, PROBABLE INTERACTION WITH CRP, SUBUNIT, DOMAIN.
  14. "Transcription activation at class II CAP-dependent promoters: two interactions between CAP and RNA polymerase."
    Niu W., Kim Y., Tau G., Heyduk T., Ebright R.H.
    Cell 87:1123-1134(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CRP, MUTAGENESIS OF 162-GLU--GLU-165 AND GLU-165.
  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 AT LYS-297 AND LYS-298.
  16. "Solution structure of the activator contact domain of the RNA polymerase alpha subunit."
    Jeon Y.H., Negishi T., Shirakawa M., Yamazaki T., Fujita N., Ishihama A., Kyogoku Y.
    Science 270:1495-1497(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 233-349.
  17. "Structure of the Escherichia coli RNA polymerase alpha subunit amino-terminal domain."
    Zhang G., Darst S.A.
    Science 281:262-266(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-235.
  18. "Structural basis of transcription activation: the CAP-alpha CTD-DNA complex."
    Benoff B., Yang H., Lawson C.L., Parkinson G., Liu J., Blatter E., Ebright Y.W., Berman H.M., Ebright R.H.
    Science 297:1562-1566(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 246-329 IN COMPLEX WITH DNA AND CRP, INTERACTION WITH CRP, DNA-BINDING, SUBUNIT.
  19. "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 RPOB; RPOC; RPOD; RPOZ CRP AND DNA, INTERACTION WITH CRP, DNA-BINDING, SUBUNIT.

Entry informationi

Entry nameiRPOA_ECOLI
AccessioniPrimary (citable) accession number: P0A7Z4
Secondary accession number(s): P00574, Q2M6W0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 26, 2014
This is version 102 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