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Protein

Transcription termination factor Rho

Gene

rho

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

Functioni

Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template. RNA-dependent NTPase which utilizes all four ribonucleoside triphosphates as substrates.2 Publications

Enzyme regulationi

ATPase activity is inhibited by bicyclomycin and dihydrobicyclomycin.1 Publication

Kineticsi

  1. KM=11 µM for ATP1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei212 – 2121ATP
    Sitei326 – 3261RNA-binding 2

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi169 – 1746ATPSequence analysis
    Nucleotide bindingi181 – 1866ATP

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-HAMAP
    • helicase activity Source: UniProtKB-HAMAP
    • identical protein binding Source: IntAct
    • RNA binding Source: EcoCyc
    • RNA-dependent ATPase activity Source: InterPro

    GO - Biological processi

    • DNA-templated transcription, termination Source: EcoCyc
    • regulation of transcription, DNA-templated Source: UniProtKB-KW
    • transcription, DNA-templated Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    Transcription, Transcription regulation, Transcription termination

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10845-MONOMER.
    ECOL316407:JW3756-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription termination factor Rho (EC:3.6.4.-)
    Alternative name(s):
    ATP-dependent helicase Rho
    Gene namesi
    Name:rho
    Synonyms:nitA, psuA, rnsC, sbaA, tsu
    Ordered Locus Names:b3783, JW3756
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10845. rho.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    • membrane Source: UniProtKB
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi62 – 621F → L or A: Defective for RNA-binding. 1 Publication
    Mutagenesisi64 – 641F → L or A: Defective for RNA-binding. 1 Publication
    Mutagenesisi181 – 1811K → Q: Partial loss of ATPase, helicase and termination activity. 1 Publication
    Mutagenesisi184 – 1841K → Q: Improves ATPase and helicase activity but reduced termination activity. 1 Publication
    Mutagenesisi202 – 2021C → G or S: Does not affect the kinetics of ATP hydrolysis and inhibition by bicyclomycin. 1 Publication
    Mutagenesisi265 – 2651D → N: Loss of ATPase activity, helicase and termination activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 419419Transcription termination factor RhoPRO_0000188962Add
    BLAST

    Proteomic databases

    EPDiP0AG30.
    PaxDbiP0AG30.
    PRIDEiP0AG30.

    Interactioni

    Subunit structurei

    Homohexamer. The homohexamer assembles into an open ring structure.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-545468,EBI-545468
    gssP0AES04EBI-545468,EBI-557080
    hfqP0A6X34EBI-545468,EBI-547637
    nusGP0AFG06EBI-545468,EBI-369628
    rofP0AFW82EBI-545468,EBI-1114609

    GO - Molecular functioni

    • identical protein binding Source: IntAct

    Protein-protein interaction databases

    DIPiDIP-35363N.
    IntActiP0AG30. 64 interactions.
    MINTiMINT-1222551.
    STRINGi511145.b3783.

    Structurei

    Secondary structure

    1
    419
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 75Combined sources
    Helixi11 – 199Combined sources
    Turni20 – 223Combined sources
    Helixi26 – 283Combined sources
    Helixi31 – 4414Combined sources
    Beta strandi49 – 579Combined sources
    Beta strandi59 – 613Combined sources
    Beta strandi63 – 664Combined sources
    Helixi68 – 703Combined sources
    Helixi75 – 773Combined sources
    Beta strandi79 – 813Combined sources
    Helixi83 – 886Combined sources
    Beta strandi96 – 1027Combined sources
    Beta strandi105 – 1073Combined sources
    Beta strandi110 – 11910Combined sources
    Helixi124 – 1274Combined sources
    Turni133 – 1353Combined sources
    Beta strandi138 – 1403Combined sources
    Beta strandi142 – 1443Combined sources
    Helixi156 – 16510Combined sources
    Beta strandi169 – 1713Combined sources
    Beta strandi173 – 1775Combined sources
    Beta strandi180 – 1834Combined sources
    Helixi184 – 19815Combined sources
    Beta strandi202 – 21110Combined sources
    Helixi213 – 2208Combined sources
    Beta strandi224 – 2307Combined sources
    Helixi236 – 25520Combined sources
    Beta strandi259 – 2657Combined sources
    Helixi267 – 27711Combined sources
    Beta strandi286 – 2883Combined sources
    Helixi291 – 30111Combined sources
    Beta strandi305 – 3106Combined sources
    Beta strandi312 – 3198Combined sources
    Beta strandi322 – 3243Combined sources
    Helixi326 – 33813Combined sources
    Beta strandi340 – 3456Combined sources
    Helixi347 – 3515Combined sources
    Turni360 – 3623Combined sources
    Beta strandi364 – 3674Combined sources
    Helixi368 – 3703Combined sources
    Helixi374 – 38714Combined sources
    Helixi392 – 40110Combined sources
    Turni402 – 4054Combined sources
    Helixi408 – 4147Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A62X-ray1.55A1-130[»]
    1A63NMR-A1-130[»]
    1A8VX-ray2.00A/B1-118[»]
    1PV4X-ray3.00A/B/C/D/E/F1-419[»]
    1PVOX-ray3.00A/B/C/D/E/F1-419[»]
    1XPOX-ray3.15A/B/C/D/E/F1-419[»]
    1XPRX-ray3.15A/B/C/D/E/F1-419[»]
    1XPUX-ray3.05A/B/C/D/E/F1-419[»]
    2A8VX-ray2.40A/B/C1-118[»]
    2HT1X-ray3.51A/B1-411[»]
    3ICEX-ray2.80A/B/C/D/E/F1-419[»]
    ProteinModelPortaliP0AG30.
    SMRiP0AG30. Positions 1-415.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AG30.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni61 – 666RNA-binding 1
    Regioni78 – 803RNA-binding 1
    Regioni108 – 1103RNA-binding 1
    Regioni284 – 2885RNA-binding 2

    Domaini

    Each subunit has two RNA-binding sites, one at the surface of the hexameric ring, and one at the center of the open ring structure, where RNA helicase activity is thought to take place.

    Sequence similaritiesi

    Belongs to the Rho family.Curated

    Phylogenomic databases

    eggNOGiENOG4105C4P. Bacteria.
    COG1158. LUCA.
    HOGENOMiHOG000076952.
    InParanoidiP0AG30.
    KOiK03628.
    OMAiFLRAPDY.
    OrthoDBiEOG6N681W.
    PhylomeDBiP0AG30.

    Family and domain databases

    Gene3Di2.40.50.140. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPiMF_01884. Rho.
    InterProiIPR003593. AAA+_ATPase.
    IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
    IPR011129. Cold_shock_prot.
    IPR012340. NA-bd_OB-fold.
    IPR027417. P-loop_NTPase.
    IPR011112. Rho_N.
    IPR011113. Rho_RNA-bd.
    IPR004665. Term_rho.
    [Graphical view]
    PfamiPF00006. ATP-synt_ab. 1 hit.
    PF07498. Rho_N. 1 hit.
    PF07497. Rho_RNA_bind. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    SM00357. CSP. 1 hit.
    SM00959. Rho_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF68912. SSF68912. 1 hit.
    TIGRFAMsiTIGR00767. rho. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0AG30-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNLTELKNTP VSELITLGEN MGLENLARMR KQDIIFAILK QHAKSGEDIF
    60 70 80 90 100
    GDGVLEILQD GFGFLRSADS SYLAGPDDIY VSPSQIRRFN LRTGDTISGK
    110 120 130 140 150
    IRPPKEGERY FALLKVNEVN FDKPENARNK ILFENLTPLH ANSRLRMERG
    160 170 180 190 200
    NGSTEDLTAR VLDLASPIGR GQRGLIVAPP KAGKTMLLQN IAQSIAYNHP
    210 220 230 240 250
    DCVLMVLLID ERPEEVTEMQ RLVKGEVVAS TFDEPASRHV QVAEMVIEKA
    260 270 280 290 300
    KRLVEHKKDV IILLDSITRL ARAYNTVVPA SGKVLTGGVD ANALHRPKRF
    310 320 330 340 350
    FGAARNVEEG GSLTIIATAL IDTGSKMDEV IYEEFKGTGN MELHLSRKIA
    360 370 380 390 400
    EKRVFPAIDY NRSGTRKEEL LTTQEELQKM WILRKIIHPM GEIDAMEFLI
    410
    NKLAMTKTND DFFEMMKRS
    Length:419
    Mass (Da):47,004
    Last modified:July 21, 1986 - v1
    Checksum:i5970A85334C43467
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti411 – 4199DFFEMMKRS → EVMTPTY in AAA68985 (PubMed:7828920).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J01673 Genomic DNA. Translation: AAA24532.1.
    M87049 Genomic DNA. Translation: AAA67583.1.
    U00096 Genomic DNA. Translation: AAC76788.1.
    AP009048 Genomic DNA. Translation: BAE77515.1.
    M12779 Genomic DNA. Translation: AAA24695.1.
    S75640 Genomic DNA. Translation: AAB20841.1.
    L34404 Genomic DNA. Translation: AAA68985.1.
    PIRiA03530. TWECR.
    RefSeqiNP_418230.1. NC_000913.3.
    WP_001054527.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76788; AAC76788; b3783.
    BAE77515; BAE77515; BAE77515.
    GeneIDi948297.
    KEGGiecj:JW3756.
    eco:b3783.
    PATRICi32123057. VBIEscCol129921_3898.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J01673 Genomic DNA. Translation: AAA24532.1.
    M87049 Genomic DNA. Translation: AAA67583.1.
    U00096 Genomic DNA. Translation: AAC76788.1.
    AP009048 Genomic DNA. Translation: BAE77515.1.
    M12779 Genomic DNA. Translation: AAA24695.1.
    S75640 Genomic DNA. Translation: AAB20841.1.
    L34404 Genomic DNA. Translation: AAA68985.1.
    PIRiA03530. TWECR.
    RefSeqiNP_418230.1. NC_000913.3.
    WP_001054527.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A62X-ray1.55A1-130[»]
    1A63NMR-A1-130[»]
    1A8VX-ray2.00A/B1-118[»]
    1PV4X-ray3.00A/B/C/D/E/F1-419[»]
    1PVOX-ray3.00A/B/C/D/E/F1-419[»]
    1XPOX-ray3.15A/B/C/D/E/F1-419[»]
    1XPRX-ray3.15A/B/C/D/E/F1-419[»]
    1XPUX-ray3.05A/B/C/D/E/F1-419[»]
    2A8VX-ray2.40A/B/C1-118[»]
    2HT1X-ray3.51A/B1-411[»]
    3ICEX-ray2.80A/B/C/D/E/F1-419[»]
    ProteinModelPortaliP0AG30.
    SMRiP0AG30. Positions 1-415.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-35363N.
    IntActiP0AG30. 64 interactions.
    MINTiMINT-1222551.
    STRINGi511145.b3783.

    Proteomic databases

    EPDiP0AG30.
    PaxDbiP0AG30.
    PRIDEiP0AG30.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76788; AAC76788; b3783.
    BAE77515; BAE77515; BAE77515.
    GeneIDi948297.
    KEGGiecj:JW3756.
    eco:b3783.
    PATRICi32123057. VBIEscCol129921_3898.

    Organism-specific databases

    EchoBASEiEB0838.
    EcoGeneiEG10845. rho.

    Phylogenomic databases

    eggNOGiENOG4105C4P. Bacteria.
    COG1158. LUCA.
    HOGENOMiHOG000076952.
    InParanoidiP0AG30.
    KOiK03628.
    OMAiFLRAPDY.
    OrthoDBiEOG6N681W.
    PhylomeDBiP0AG30.

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10845-MONOMER.
    ECOL316407:JW3756-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP0AG30.
    PROiP0AG30.

    Family and domain databases

    Gene3Di2.40.50.140. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPiMF_01884. Rho.
    InterProiIPR003593. AAA+_ATPase.
    IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
    IPR011129. Cold_shock_prot.
    IPR012340. NA-bd_OB-fold.
    IPR027417. P-loop_NTPase.
    IPR011112. Rho_N.
    IPR011113. Rho_RNA-bd.
    IPR004665. Term_rho.
    [Graphical view]
    PfamiPF00006. ATP-synt_ab. 1 hit.
    PF07498. Rho_N. 1 hit.
    PF07497. Rho_RNA_bind. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    SM00357. CSP. 1 hit.
    SM00959. Rho_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF68912. SSF68912. 1 hit.
    TIGRFAMsiTIGR00767. rho. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The nucleotide sequence of the rho gene of E. coli K-12."
      Pinkham J.L., Platt T.
      Nucleic Acids Res. 11:3531-3545(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes."
      Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.
      Science 257:771-778(1992) [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. "Autogenous regulation of the gene for transcription termination factor rho in Escherichia coli: localization and function of its attenuators."
      Matsumoto Y., Shigesada K., Hirano M., Imai M.
      J. Bacteriol. 166:945-958(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-196.
    6. "Cloning and expression of the rfe-rff gene cluster of Escherichia coli."
      Ohta M., Ina K., Kusuzaki K., Kido N., Arakawa Y., Kato N.
      Mol. Microbiol. 5:1853-1862(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 397-419.
    7. "The ts15 mutation of Escherichia coli alters the sequence of the C-terminal nine residues of Rho protein."
      Opperman T., Martinez A., Richardson J.P.
      Gene 152:133-134(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 405-419.
    8. "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 1-12.
      Strain: K12 / EMG2.
    9. "Mutations in an RNP1 consensus sequence of Rho protein reduce RNA binding affinity but facilitate helicase turnover."
      Brennan C.A., Platt T.
      J. Biol. Chem. 266:17296-17305(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING DOMAIN.
    10. "Site-directed alterations in the ATP-binding domain of rho protein affect its activities as a termination factor."
      Dombroski A.J., Brennan C.A., Spear P., Platt T.
      J. Biol. Chem. 263:18802-18809(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS.
    11. "Bicyclomycin and dihydrobicyclomycin inhibition kinetics of Escherichia coli rho-dependent transcription termination factor ATPase activity."
      Park H.G., Zhang X., Moon H.S., Zwiefka A., Cox K., Gaskell S.J., Widger W.R., Kohn H.
      Arch. Biochem. Biophys. 323:447-454(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-202.
    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. "1H, 15N and 13C resonance assignments and secondary structure determination of the RNA-binding domain of E.coli rho protein."
      Briercheck D.M., Allison T.J., Richardson J.P., Ellena J.F., Wood T.C., Rule S.G.
      J. Biomol. NMR 8:429-444(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-130.
    14. "The NMR structure of the RNA binding domain of E. coli rho factor suggests possible RNA-protein interactions."
      Briercheck D.M., Allison T.J., Wood T.C., Richardson J.P., Rule G.S.
      Nat. Struct. Biol. 5:393-399(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-130.
    15. "Crystal structure of the RNA-binding domain from transcription termination factor rho."
      Allison T.J., Wood T.C., Briercheck D.M., Rastinejad F., Richardson J.P., Rule G.S.
      Nat. Struct. Biol. 5:352-356(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 1-130, SUBUNIT.
    16. "The structural basis for terminator recognition by the Rho transcription termination factor."
      Bogden C.E., Fass D., Bergman N., Nichols M.D., Berger J.M.
      Mol. Cell 3:487-493(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-118 IN COMPLEX WITH POLY-C OLIGONUCLEOTIDE, INTERACTION WITH TARGET RNA, SUBUNIT.
    17. "Structure of the Rho transcription terminator: mechanism of mRNA recognition and helicase loading."
      Skordalakes E., Berger J.M.
      Cell 114:135-146(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH AMPPNP AND OLIGONUCLEOTIDE, SUBUNIT.
    18. "Structural mechanism of inhibition of the Rho transcription termination factor by the antibiotic bicyclomycin."
      Skordalakes E., Brogan A.P., Park B.S., Kohn H., Berger J.M.
      Structure 13:99-109(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) IN COMPLEX WITH INHIBITOR BICYCLOMYCIN; MAGNESIUM-ATP ANALOG AND OLIGO-U OLIGONUCLEOTIDE, SUBUNIT.
    19. "Running in reverse: the structural basis for translocation polarity in hexameric helicases."
      Thomsen N.D., Berger J.M.
      Cell 139:523-534(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH POLY-U OLIGONUCLEOTIDE; ADP; MAGNESIUM AND BERYLLIUM IONS, SUBUNIT.

    Entry informationi

    Entry nameiRHO_ECOLI
    AccessioniPrimary (citable) accession number: P0AG30
    Secondary accession number(s): P03002, Q2M891, Q48357
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: March 16, 2016
    This is version 107 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.