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P0AD68

- FTSI_ECOLI

UniProt

P0AD68 - FTSI_ECOLI

Protein

Peptidoglycan synthase FtsI

Gene

ftsI

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 91 (01 Oct 2014)
      Sequence version 1 (20 Mar 1987)
      Previous versions | rss
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    Functioni

    Cell wall formation. Essential for the formation of a septum of the murein sacculus. Synthesis of cross-linked peptidoglycan from the lipid intermediates.

    Catalytic activityi

    (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n)-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl diphosphate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei307 – 3071Acyl-ester intermediate

    GO - Molecular functioni

    1. penicillin binding Source: EcoliWiki
    2. peptidoglycan glycosyltransferase activity Source: EcoliWiki
    3. protein binding Source: IntAct

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell division Source: EcoliWiki
    3. peptidoglycan biosynthetic process Source: UniProtKB-UniPathway
    4. regulation of cell shape Source: UniProtKB-KW
    5. response to antibiotic Source: UniProtKB-KW
    6. response to drug Source: EcoliWiki

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Antibiotic resistance, Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10341-MONOMER.
    ECOL316407:JW0082-MONOMER.
    MetaCyc:EG10341-MONOMER.
    UniPathwayiUPA00219.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidoglycan synthase FtsI (EC:2.4.1.129)
    Alternative name(s):
    Penicillin-binding protein 3
    Short name:
    PBP-3
    Peptidoglycan glycosyltransferase 3
    Gene namesi
    Name:ftsI
    Synonyms:pbpB
    Ordered Locus Names:b0084, JW0082
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10341. ftsI.

    Subcellular locationi

    Cell inner membrane; Single-pass membrane protein; Periplasmic side
    Note: The bulk of the molecule, except for the N-terminal membrane anchor region, protrudes into the periplasmic space, where it acts on murein.

    GO - Cellular componenti

    1. cell division site Source: EcoliWiki
    2. integral component of plasma membrane Source: EcoliWiki
    3. intrinsic component of plasma membrane Source: EcoliWiki

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi307 – 3071S → A or T: Unable to bind penicillin. 1 Publication
    Mutagenesisi307 – 3071S → C: Still able to bind penicillin. 1 Publication
    Mutagenesisi361 – 3611N → S in PBPBR1; obtained after selection for increased resistance to cephalexin, causes a change in the shape of the cell: The polar caps are pointed. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 577577Peptidoglycan synthase FtsIPRO_0000017052Add
    BLAST
    Propeptidei578 – 58811PRO_0000017053Add
    BLAST

    Proteomic databases

    PaxDbiP0AD68.
    PRIDEiP0AD68.

    Expressioni

    Gene expression databases

    GenevestigatoriP0AD68.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    divIBQ8DQM03EBI-548564,EBI-6446264From a different organism.
    ftsLP0AEN44EBI-548564,EBI-1119082
    ftsNP291313EBI-548564,EBI-1134233
    ftsQP061365EBI-548564,EBI-1130157
    ftsWP0ABG47EBI-548564,EBI-1214767
    mtgAP460223EBI-548564,EBI-558469
    ymgFP580343EBI-548564,EBI-1214577

    Protein-protein interaction databases

    DIPiDIP-47950N.
    IntActiP0AD68. 18 interactions.
    MINTiMINT-1031950.
    STRINGi511145.b0084.

    Structurei

    3D structure databases

    ProteinModelPortaliP0AD68.
    SMRiP0AD68. Positions 60-570.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1818CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini40 – 577538PeriplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei19 – 3921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domaini

    Has an N-terminal penicillin insensitive transglycosylase domain (formation of linear glycan strands) and a C-terminal penicillin-sensitive transpeptidase domain (cross-linking of the peptide subunits).

    Sequence similaritiesi

    Belongs to the transpeptidase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0768.
    HOGENOMiHOG000049554.
    KOiK03587.
    OMAiHPRYFNF.
    OrthoDBiEOG6N0HHV.
    PhylomeDBiP0AD68.

    Family and domain databases

    Gene3Di3.40.710.10. 1 hit.
    InterProiIPR012338. Beta-lactam/transpept-like.
    IPR005311. PBP_dimer.
    IPR001460. PCN-bd_Tpept.
    [Graphical view]
    PfamiPF03717. PBP_dimer. 1 hit.
    PF00905. Transpeptidase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56519. SSF56519. 1 hit.
    SSF56601. SSF56601. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0AD68-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKAAAKTQKP KRQEEHANFI SWRFALLCGC ILLALAFLLG RVAWLQVISP    50
    DMLVKEGDMR SLRVQQVSTS RGMITDRSGR PLAVSVPVKA IWADPKEVHD 100
    AGGISVGDRW KALANALNIP LDQLSARINA NPKGRFIYLA RQVNPDMADY 150
    IKKLKLPGIH LREESRRYYP SGEVTAHLIG FTNVDSQGIE GVEKSFDKWL 200
    TGQPGERIVR KDRYGRVIED ISSTDSQAAH NLALSIDERL QALVYRELNN 250
    AVAFNKAESG SAVLVDVNTG EVLAMANSPS YNPNNLSGTP KEAMRNRTIT 300
    DVFEPGSTVK PMVVMTALQR GVVRENSVLN TIPYRINGHE IKDVARYSEL 350
    TLTGVLQKSS NVGVSKLALA MPSSALVDTY SRFGLGKATN LGLVGERSGL 400
    YPQKQRWSDI ERATFSFGYG LMVTPLQLAR VYATIGSYGI YRPLSITKVD 450
    PPVPGERVFP ESIVRTVVHM MESVALPGGG GVKAAIKGYR IAIKTGTAKK 500
    VGPDGRYINK YIAYTAGVAP ASQPRFALVV VINDPQAGKY YGGAVSAPVF 550
    GAIMGGVLRT MNIEPDALTT GDKNEFVINQ GEGTGGRS 588
    Length:588
    Mass (Da):63,877
    Last modified:March 20, 1987 - v1
    Checksum:iC89A403D5980B2CD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K00137 Genomic DNA. Translation: AAA24300.1.
    X55034 Genomic DNA. Translation: CAA38861.1.
    U00096 Genomic DNA. Translation: AAC73195.1.
    AP009048 Genomic DNA. Translation: BAB96652.1.
    S49802 Genomic DNA. Translation: AAB24312.1.
    S49875 Genomic DNA. Translation: AAB24310.1.
    X55814 Genomic DNA. Translation: CAA39333.1.
    PIRiA93123. ZPECP3.
    RefSeqiNP_414626.1. NC_000913.3.
    YP_488389.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73195; AAC73195; b0084.
    BAB96652; BAB96652; BAB96652.
    GeneIDi12932643.
    944799.
    KEGGiecj:Y75_p0083.
    eco:b0084.
    PATRICi32115273. VBIEscCol129921_0088.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K00137 Genomic DNA. Translation: AAA24300.1 .
    X55034 Genomic DNA. Translation: CAA38861.1 .
    U00096 Genomic DNA. Translation: AAC73195.1 .
    AP009048 Genomic DNA. Translation: BAB96652.1 .
    S49802 Genomic DNA. Translation: AAB24312.1 .
    S49875 Genomic DNA. Translation: AAB24310.1 .
    X55814 Genomic DNA. Translation: CAA39333.1 .
    PIRi A93123. ZPECP3.
    RefSeqi NP_414626.1. NC_000913.3.
    YP_488389.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P0AD68.
    SMRi P0AD68. Positions 60-570.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-47950N.
    IntActi P0AD68. 18 interactions.
    MINTi MINT-1031950.
    STRINGi 511145.b0084.

    Chemistry

    ChEMBLi CHEMBL2354204.

    Proteomic databases

    PaxDbi P0AD68.
    PRIDEi P0AD68.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73195 ; AAC73195 ; b0084 .
    BAB96652 ; BAB96652 ; BAB96652 .
    GeneIDi 12932643.
    944799.
    KEGGi ecj:Y75_p0083.
    eco:b0084.
    PATRICi 32115273. VBIEscCol129921_0088.

    Organism-specific databases

    EchoBASEi EB0337.
    EcoGenei EG10341. ftsI.

    Phylogenomic databases

    eggNOGi COG0768.
    HOGENOMi HOG000049554.
    KOi K03587.
    OMAi HPRYFNF.
    OrthoDBi EOG6N0HHV.
    PhylomeDBi P0AD68.

    Enzyme and pathway databases

    UniPathwayi UPA00219 .
    BioCyci EcoCyc:EG10341-MONOMER.
    ECOL316407:JW0082-MONOMER.
    MetaCyc:EG10341-MONOMER.

    Miscellaneous databases

    PROi P0AD68.

    Gene expression databases

    Genevestigatori P0AD68.

    Family and domain databases

    Gene3Di 3.40.710.10. 1 hit.
    InterProi IPR012338. Beta-lactam/transpept-like.
    IPR005311. PBP_dimer.
    IPR001460. PCN-bd_Tpept.
    [Graphical view ]
    Pfami PF03717. PBP_dimer. 1 hit.
    PF00905. Transpeptidase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56519. SSF56519. 1 hit.
    SSF56601. SSF56601. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "On the process of cellular division in Escherichia coli: nucleotide sequence of the gene for penicillin-binding protein 3."
      Nakamura M., Maruyama I.N., Soma M., Kato J., Suzuki H., Horota Y.
      Mol. Gen. Genet. 191:1-9(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    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].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Escherichia coli mraR gene involved in cell growth and division."
      Ueki M., Wachi M., Jung H.K., Ishino F., Matsuhashi M.
      J. Bacteriol. 174:7841-7843(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71.
      Strain: JE1011.
    6. "FtsL, an essential cytoplasmic membrane protein involved in cell division in Escherichia coli."
      Guzman L.-M., Barondess J.J., Beckwith J.
      J. Bacteriol. 174:7716-7728(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
    7. "Revised interpretation of the sequence containing the murE gene encoding the UDP-N-acetylmuramyl-tripeptide synthetase of Escherichia coli."
      Michaud C., Parquet C., Flouret B., Blanot D., van Heijenoort J.
      Biochem. J. 269:277-278(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 550-588.
    8. "Binding of penicillin to thiol-penicillin-binding protein 3 of Escherichia coli: identification of its active site."
      Houba-Herin N., Hara H., Inouye M., Hirota Y.
      Mol. Gen. Genet. 201:499-504(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SER-307.
    9. "Determination of the cleavage site involved in C-terminal processing of penicillin-binding protein 3 of Escherichia coli."
      Nagasawa H., Sakagami Y., Suzuki A., Suzuki H., Hara H., Hirota Y.
      J. Bacteriol. 171:5890-5893(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING.
    10. "An amino acid substitution in penicillin-binding protein 3 creates pointed polar caps in Escherichia coli."
      Taschner P.E.M., Ypenburg N., Spratt B.G., Woldringh C.L.
      J. Bacteriol. 170:4828-4837(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASN-361.
    11. "Membrane topology of penicillin-binding protein 3 of Escherichia coli."
      Bowler L.D., Spratt B.G.
      Mol. Microbiol. 3:1277-1286(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY.

    Entry informationi

    Entry nameiFTSI_ECOLI
    AccessioniPrimary (citable) accession number: P0AD68
    Secondary accession number(s): P04286
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 1987
    Last sequence update: March 20, 1987
    Last modified: October 1, 2014
    This is version 91 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

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3