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P10408

- SECA_ECOLI

UniProt

P10408 - SECA_ECOLI

Protein

Protein translocase subunit SecA

Gene

secA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Required for protein export, interacts with the SecYEG preprotein conducting channel. SecA has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.1 Publication

    Cofactori

    Binds 1 zinc ion per subunit. Zinc is required for binding of the SecB chaperone to the extreme C-terminus of SecA.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi885 – 8851Zinc
    Metal bindingi887 – 8871Zinc
    Metal bindingi896 – 8961Zinc
    Metal bindingi897 – 8971Zinc

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi102 – 1098ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. identical protein binding Source: IntAct
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct
    5. protein-transmembrane transporting ATPase activity Source: EcoCyc

    GO - Biological processi

    1. chaperone-mediated protein folding Source: EcoCyc
    2. intracellular protein transmembrane transport Source: EcoliWiki
    3. protein import Source: InterPro
    4. protein targeting Source: EcoliWiki
    5. protein transport Source: EcoliWiki
    6. protein transport by the Sec complex Source: EcoCyc

    Keywords - Biological processi

    Protein transport, Translocation, Transport

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:SECA.
    ECOL316407:JW0096-MONOMER.

    Protein family/group databases

    TCDBi3.A.5.1.1. the general secretory pathway (sec) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein translocase subunit SecA
    Gene namesi
    Name:secA
    Synonyms:azi, pea, prlD
    Ordered Locus Names:b0098, JW0096
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10936. secA.

    Subcellular locationi

    GO - Cellular componenti

    1. cell envelope Sec protein transport complex Source: EcoCyc
    2. cytoplasm Source: EcoliWiki
    3. cytosol Source: EcoCyc
    4. integral component of plasma membrane Source: EcoCyc
    5. plasma membrane Source: EcoliWiki

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Essential. Leads to loss of translocation of lipoproteins Lpp and BRP.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 901901Protein translocase subunit SecAPRO_0000109585Add
    BLAST

    Proteomic databases

    PaxDbiP10408.
    PRIDEiP10408.

    Expressioni

    Inductioni

    Repressed under conditions of excess protein secretion capacity and derepressed when protein secretion becomes limiting. This is regulated by SecM.

    Gene expression databases

    GenevestigatoriP10408.

    Interactioni

    Subunit structurei

    Monomer and homodimer; probably dimeric in the cytoplasm. It is not yet clear whether the form that functions in protein insertion is monomeric or dimeric. Part of the essential protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF-YajC and YidC. Makes direct contact with SecY.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-543213,EBI-543213
    lamBP029433EBI-543213,EBI-371309
    secBP0AG864EBI-543213,EBI-555877
    secGP0AG992EBI-543213,EBI-6404248
    secYP0AGA24EBI-543213,EBI-761422
    ybgCP0A8Z32EBI-543213,EBI-543276

    Protein-protein interaction databases

    BioGridi849222. 1 interaction.
    DIPiDIP-10840N.
    IntActiP10408. 77 interactions.
    MINTiMINT-1224866.
    STRINGi511145.b0098.

    Structurei

    Secondary structure

    1
    901
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi14 – 3017
    Helixi32 – 376
    Helixi40 – 5516
    Helixi60 – 7920
    Helixi85 – 9511
    Beta strandi96 – 1016
    Helixi108 – 12013
    Beta strandi122 – 1243
    Beta strandi127 – 1326
    Helixi133 – 14917
    Beta strandi154 – 1563
    Helixi163 – 1719
    Beta strandi172 – 1787
    Helixi179 – 18911
    Helixi195 – 1973
    Beta strandi205 – 2095
    Helixi211 – 2144
    Turni215 – 2206
    Beta strandi222 – 2276
    Helixi234 – 2363
    Helixi237 – 2404
    Helixi241 – 2455
    Beta strandi250 – 2523
    Beta strandi278 – 2814
    Helixi282 – 2843
    Beta strandi286 – 2927
    Helixi301 – 3033
    Helixi304 – 31411
    Turni315 – 3173
    Beta strandi318 – 3203
    Turni323 – 3253
    Beta strandi326 – 3294
    Beta strandi332 – 3365
    Turni338 – 3403
    Beta strandi343 – 3464
    Turni350 – 3523
    Helixi353 – 3608
    Beta strandi370 – 3767
    Helixi377 – 3815
    Beta strandi384 – 3918
    Helixi398 – 4058
    Beta strandi408 – 4114
    Beta strandi426 – 4305
    Helixi431 – 44616
    Turni447 – 4493
    Beta strandi452 – 4587
    Helixi459 – 47113
    Beta strandi477 – 4793
    Helixi484 – 4929
    Turni493 – 4953
    Beta strandi496 – 4983
    Beta strandi500 – 5056
    Helixi519 – 5257
    Beta strandi526 – 5283
    Helixi533 – 55018
    Beta strandi553 – 5608
    Helixi565 – 5728
    Helixi577 – 5793
    Beta strandi582 – 5898
    Helixi590 – 5923
    Helixi593 – 5964
    Beta strandi597 – 5993
    Helixi601 – 6044
    Helixi605 – 6106
    Helixi621 – 66848
    Helixi673 – 68917
    Helixi698 – 7003
    Helixi703 – 71412
    Helixi720 – 7267
    Helixi728 – 7303
    Helixi732 – 75423
    Helixi756 – 78732
    Turni788 – 7903
    Beta strandi791 – 7933
    Beta strandi795 – 7973
    Turni799 – 8013
    Helixi802 – 82827
    Turni884 – 8874
    Beta strandi889 – 8913
    Helixi892 – 8965

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TM6NMR-A880-901[»]
    2FSFX-ray2.00A/B9-861[»]
    2FSGX-ray2.20A/B9-861[»]
    2FSHX-ray2.00A/B9-861[»]
    2FSIX-ray2.11A/B9-861[»]
    2VDANMR-A9-836[»]
    3BXZX-ray3.00A/B6-609[»]
    ProteinModelPortaliP10408.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10408.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the SecA family.Curated

    Phylogenomic databases

    eggNOGiCOG0653.
    HOGENOMiHOG000218168.
    KOiK03070.
    OMAiEAYEFQQ.
    OrthoDBiEOG654P48.
    PhylomeDBiP10408.

    Family and domain databases

    Gene3Di1.10.3060.10. 1 hit.
    3.40.50.300. 3 hits.
    3.90.1440.10. 1 hit.
    HAMAPiMF_01382. SecA.
    InterProiIPR027417. P-loop_NTPase.
    IPR004027. SEC_C_motif.
    IPR000185. SecA.
    IPR020937. SecA_CS.
    IPR011115. SecA_DEAD.
    IPR014018. SecA_motor_DEAD.
    IPR011130. SecA_preprotein_X-link_dom.
    IPR011116. SecA_Wing/Scaffold.
    [Graphical view]
    PfamiPF02810. SEC-C. 1 hit.
    PF07517. SecA_DEAD. 1 hit.
    PF01043. SecA_PP_bind. 1 hit.
    PF07516. SecA_SW. 1 hit.
    [Graphical view]
    PRINTSiPR00906. SECA.
    SMARTiSM00957. SecA_DEAD. 1 hit.
    SM00958. SecA_PP_bind. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 3 hits.
    SSF81767. SSF81767. 1 hit.
    SSF81886. SSF81886. 2 hits.
    TIGRFAMsiTIGR00963. secA. 1 hit.
    PROSITEiPS01312. SECA. 1 hit.
    PS51196. SECA_MOTOR_DEAD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P10408-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLIKLLTKVF GSRNDRTLRR MRKVVNIINA MEPEMEKLSD EELKGKTAEF    50
    RARLEKGEVL ENLIPEAFAV VREASKRVFG MRHFDVQLLG GMVLNERCIA 100
    EMRTGEGKTL TATLPAYLNA LTGKGVHVVT VNDYLAQRDA ENNRPLFEFL 150
    GLTVGINLPG MPAPAKREAY AADITYGTNN EYGFDYLRDN MAFSPEERVQ 200
    RKLHYALVDE VDSILIDEAR TPLIISGPAE DSSEMYKRVN KIIPHLIRQE 250
    KEDSETFQGE GHFSVDEKSR QVNLTERGLV LIEELLVKEG IMDEGESLYS 300
    PANIMLMHHV TAALRAHALF TRDVDYIVKD GEVIIVDEHT GRTMQGRRWS 350
    DGLHQAVEAK EGVQIQNENQ TLASITFQNY FRLYEKLAGM TGTADTEAFE 400
    FSSIYKLDTV VVPTNRPMIR KDLPDLVYMT EAEKIQAIIE DIKERTAKGQ 450
    PVLVGTISIE KSELVSNELT KAGIKHNVLN AKFHANEAAI VAQAGYPAAV 500
    TIATNMAGRG TDIVLGGSWQ AEVAALENPT AEQIEKIKAD WQVRHDAVLE 550
    AGGLHIIGTE RHESRRIDNQ LRGRSGRQGD AGSSRFYLSM EDALMRIFAS 600
    DRVSGMMRKL GMKPGEAIEH PWVTKAIANA QRKVESRNFD IRKQLLEYDD 650
    VANDQRRAIY SQRNELLDVS DVSETINSIR EDVFKATIDA YIPPQSLEEM 700
    WDIPGLQERL KNDFDLDLPI AEWLDKEPEL HEETLRERIL AQSIEVYQRK 750
    EEVVGAEMMR HFEKGVMLQT LDSLWKEHLA AMDYLRQGIH LRGYAQKDPK 800
    QEYKRESFSM FAAMLESLKY EVISTLSKVQ VRMPEEVEEL EQQRRMEAER 850
    LAQMQQLSHQ DDDSAAAAAL AAQTGERKVG RNDPCPCGSG KKYKQCHGRL 900
    Q 901
    Length:901
    Mass (Da):102,023
    Last modified:November 1, 1997 - v2
    Checksum:i683D66DD4305DBC2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti19 – 191R → G AA sequence (PubMed:2841285)Curated
    Sequence conflicti737 – 7382ER → DG in AAA24619. (PubMed:2841285)Curated
    Sequence conflicti737 – 7382ER → DG in CAA38875. (PubMed:1630901)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20791 Genomic DNA. Translation: AAA24619.1.
    M19211 Genomic DNA. Translation: AAA83851.1.
    X55034 Genomic DNA. Translation: CAA38875.1.
    U00096 Genomic DNA. Translation: AAC73209.1.
    AP009048 Genomic DNA. Translation: BAB96666.2.
    PIRiB64732. BVECCA.
    RefSeqiNP_414640.1. NC_000913.3.
    YP_488403.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73209; AAC73209; b0098.
    BAB96666; BAB96666; BAB96666.
    GeneIDi12932123.
    944821.
    KEGGiecj:Y75_p0097.
    eco:b0098.
    PATRICi32115301. VBIEscCol129921_0102.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20791 Genomic DNA. Translation: AAA24619.1 .
    M19211 Genomic DNA. Translation: AAA83851.1 .
    X55034 Genomic DNA. Translation: CAA38875.1 .
    U00096 Genomic DNA. Translation: AAC73209.1 .
    AP009048 Genomic DNA. Translation: BAB96666.2 .
    PIRi B64732. BVECCA.
    RefSeqi NP_414640.1. NC_000913.3.
    YP_488403.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TM6 NMR - A 880-901 [» ]
    2FSF X-ray 2.00 A/B 9-861 [» ]
    2FSG X-ray 2.20 A/B 9-861 [» ]
    2FSH X-ray 2.00 A/B 9-861 [» ]
    2FSI X-ray 2.11 A/B 9-861 [» ]
    2VDA NMR - A 9-836 [» ]
    3BXZ X-ray 3.00 A/B 6-609 [» ]
    ProteinModelPortali P10408.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 849222. 1 interaction.
    DIPi DIP-10840N.
    IntActi P10408. 77 interactions.
    MINTi MINT-1224866.
    STRINGi 511145.b0098.

    Protein family/group databases

    TCDBi 3.A.5.1.1. the general secretory pathway (sec) family.

    Proteomic databases

    PaxDbi P10408.
    PRIDEi P10408.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73209 ; AAC73209 ; b0098 .
    BAB96666 ; BAB96666 ; BAB96666 .
    GeneIDi 12932123.
    944821.
    KEGGi ecj:Y75_p0097.
    eco:b0098.
    PATRICi 32115301. VBIEscCol129921_0102.

    Organism-specific databases

    EchoBASEi EB0929.
    EcoGenei EG10936. secA.

    Phylogenomic databases

    eggNOGi COG0653.
    HOGENOMi HOG000218168.
    KOi K03070.
    OMAi EAYEFQQ.
    OrthoDBi EOG654P48.
    PhylomeDBi P10408.

    Enzyme and pathway databases

    BioCyci EcoCyc:SECA.
    ECOL316407:JW0096-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P10408.
    PROi P10408.

    Gene expression databases

    Genevestigatori P10408.

    Family and domain databases

    Gene3Di 1.10.3060.10. 1 hit.
    3.40.50.300. 3 hits.
    3.90.1440.10. 1 hit.
    HAMAPi MF_01382. SecA.
    InterProi IPR027417. P-loop_NTPase.
    IPR004027. SEC_C_motif.
    IPR000185. SecA.
    IPR020937. SecA_CS.
    IPR011115. SecA_DEAD.
    IPR014018. SecA_motor_DEAD.
    IPR011130. SecA_preprotein_X-link_dom.
    IPR011116. SecA_Wing/Scaffold.
    [Graphical view ]
    Pfami PF02810. SEC-C. 1 hit.
    PF07517. SecA_DEAD. 1 hit.
    PF01043. SecA_PP_bind. 1 hit.
    PF07516. SecA_SW. 1 hit.
    [Graphical view ]
    PRINTSi PR00906. SECA.
    SMARTi SM00957. SecA_DEAD. 1 hit.
    SM00958. SecA_PP_bind. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 3 hits.
    SSF81767. SSF81767. 1 hit.
    SSF81886. SSF81886. 2 hits.
    TIGRFAMsi TIGR00963. secA. 1 hit.
    PROSITEi PS01312. SECA. 1 hit.
    PS51196. SECA_MOTOR_DEAD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the secA gene and secA(Ts) mutations preventing protein export in Escherichia coli."
      Schmidt M., Rollo E., Grodberg J., Oliver D.
      J. Bacteriol. 170:3404-3414(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    2. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
      Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
      Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12.
    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], SEQUENCE REVISION TO 737-738.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Sequence analysis, transcriptional organization, and insertional mutagenesis of the envA gene of Escherichia coli."
      Beall B., Lutkenhaus J.
      J. Bacteriol. 169:5408-5415(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67.
      Strain: K12.
    6. "SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli."
      Lill R., Cunningham K., Brundage L.A., Ito K., Oliver D., Wickner W.
      EMBO J. 8:961-966(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: ATP HYDROLYSIS.
    7. Cited for: COFACTOR.
    8. "Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane."
      Or E., Navon A., Rapoport T.
      EMBO J. 21:4470-4479(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DIMER DISSOCIATION IN THE PRESENCE OF ACIDIC PHOSPHOLIPIDS, DETERGENTS, SYNTHETIC SIGNAL PEPTIDES.
    9. "Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase."
      Duong F.
      EMBO J. 22:4375-4384(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION OF MONOMER WITH SECYEG TRANSLOCATION COMPLEX.
    10. "Phospholipid-induced monomerization and signal-peptide-induced oligomerization of SecA."
      Benach J., Chou Y.T., Fak J.J., Itkin A., Nicolae D.D., Smith P.C., Wittrock G., Floyd D.L., Golsaz C.M., Gierasch L.M., Hunt J.F.
      J. Biol. Chem. 278:3628-3638(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACIDIC PHOSPHOLIPIDS, SYNTHETIC SIGNAL PEPTIDES, OLIGOMERIZATION STATE OF SECA.
    11. "Nucleotide binding induces changes in the oligomeric state and conformation of Sec A in a lipid environment: a small-angle neutron-scattering study."
      Bu Z., Wang L., Kendall D.A.
      J. Mol. Biol. 332:23-30(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE TURNOVER, OLIGOMERIZATION STATE OF SECA.
    12. "Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway."
      Froderberg L., Houben E.N., Baars L., Luirink J., de Gier J.W.
      J. Biol. Chem. 279:31026-31032(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN LIPOPROTEIN EXPORT, DISRUPTION PHENOTYPE.
    13. "Protein translocation is mediated by oligomers of the SecY complex with one SecY copy forming the channel."
      Osborne A.R., Rapoport T.A.
      Cell 129:97-110(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SECY.
    14. Cited for: CONTROL OF ATPASE ACTIVITY.
    15. "NMR structure of the C-terminal domain of SecA in the free state."
      Matousek W.M., Alexandrescu A.T.
      Biochim. Biophys. Acta 1702:163-171(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 880-901.
    16. "Structure of dimeric SecA, the Escherichia coli preprotein translocase motor."
      Papanikolau Y., Papadovasilaki M., Ravelli R.B.G., McCarthy A.A., Cusack S., Economou A., Petratos K.
      J. Mol. Biol. 366:1545-1557(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 9-861 AS A DIMERIC APOPROTEIN, AS A NUCLEOTIDE-BOUND DIMER.
    17. "Control of SecA and SecM translation by protein secretion."
      Nakatogawa H., Murakami A., Ito K.
      Curr. Opin. Microbiol. 7:145-150(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW OF PROTEIN SECRETION CONTROL OF SECA EXPRESSION.
    18. "Bacterial protein secretion through the translocase nanomachine."
      Papanikou E., Karamanou S., Economou A.
      Nat. Rev. Microbiol. 5:839-851(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW OF PROTEIN SECRETION.

    Entry informationi

    Entry nameiSECA_ECOLI
    AccessioniPrimary (citable) accession number: P10408
    Secondary accession number(s): P75642
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 147 of the entry and version 2 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