Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P0AD69

- FTSI_ECO57

UniProt

P0AD69 - FTSI_ECO57

Protein

Peptidoglycan synthase FtsI

Gene

ftsI

Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (20 Mar 1987)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

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

    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 intermediateBy similarity

    GO - Molecular functioni

    1. penicillin binding Source: InterPro
    2. peptidoglycan glycosyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

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

    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

    BioCyciECOL386585:GJFA-86-MONOMER.
    ECOO157:FTSI-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:Z0094, ECs0088
    OrganismiEscherichia coli O157:H7
    Taxonomic identifieri83334 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

    Subcellular locationi

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

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 577577Peptidoglycan synthase FtsIPRO_0000043363Add
    BLAST
    Propeptidei578 – 58811By similarityPRO_0000043364Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-1031936.
    STRINGi155864.Z0094.

    Structurei

    3D structure databases

    ProteinModelPortaliP0AD69.
    SMRiP0AD69. 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).By similarity

    Sequence similaritiesi

    Belongs to the transpeptidase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0768.
    HOGENOMiHOG000049554.
    KOiK03587.
    OMAiHPRYFNF.
    OrthoDBiEOG6N0HHV.

    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.

    P0AD69-1 [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
    AE005174 Genomic DNA. Translation: AAG54388.1.
    BA000007 Genomic DNA. Translation: BAB33511.1.
    PIRiH85490.
    H90639.
    RefSeqiNP_285780.1. NC_002655.2.
    NP_308115.1. NC_002695.1.

    Genome annotation databases

    EnsemblBacteriaiAAG54388; AAG54388; Z0094.
    BAB33511; BAB33511; BAB33511.
    GeneIDi913535.
    956770.
    KEGGiece:Z0094.
    ecs:ECs0088.
    PATRICi18349118. VBIEscCol44059_0089.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG54388.1 .
    BA000007 Genomic DNA. Translation: BAB33511.1 .
    PIRi H85490.
    H90639.
    RefSeqi NP_285780.1. NC_002655.2.
    NP_308115.1. NC_002695.1.

    3D structure databases

    ProteinModelPortali P0AD69.
    SMRi P0AD69. Positions 60-570.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-1031936.
    STRINGi 155864.Z0094.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG54388 ; AAG54388 ; Z0094 .
    BAB33511 ; BAB33511 ; BAB33511 .
    GeneIDi 913535.
    956770.
    KEGGi ece:Z0094.
    ecs:ECs0088.
    PATRICi 18349118. VBIEscCol44059_0089.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00219 .
    BioCyci ECOL386585:GJFA-86-MONOMER.
    ECOO157:FTSI-MONOMER.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
    2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
      Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
      , Kuhara S., Shiba T., Hattori M., Shinagawa H.
      DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

    Entry informationi

    Entry nameiFTSI_ECO57
    AccessioniPrimary (citable) accession number: P0AD69
    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 69 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3