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Protein

Carboxylesterase LipF

Gene

lipF

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes short-chain esters. Shows maximal activity with triacetin and p-nitrophenyl acetate.1 Publication

Catalytic activityi

A carboxylic ester + H2O = an alcohol + a carboxylate.1 Publication

Kineticsi

kcat is 581.2 sec(-1) for triacetin. kcat is 223.7 sec(-1) for tributyrin. kcat is 122.9 sec(-1) for tricaproin. kcat is 15.6 sec(-1) for tricaprylin. kcat is 501.8 sec(-1) for p-nitrophenyl acetate. kcat is 119.7 sec(-1) for p-nitrophenyl butyrate. kcat is 33.1 sec(-1) for p-nitrophenyl caproate.

  1. KM=0.13 mM for triacetin1 Publication
  2. KM=0.24 mM for tributyrin1 Publication
  3. KM=0.25 mM for tricaproin1 Publication
  4. KM=1.46 mM for tricaprylin1 Publication
  5. KM=0.16 mM for p-nitrophenyl acetate1 Publication
  6. KM=0.18 mM for p-nitrophenyl butyrate1 Publication
  7. KM=0.58 mM for p-nitrophenyl caproate1 Publication

    pH dependencei

    Optimum pH is 7.5.1 Publication

    Temperature dependencei

    Optimum temperature is 35 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei90 – 901Curated
    Active sitei189 – 1891Curated
    Active sitei219 – 2191Curated

    GO - Molecular functioni

    • carboxylic ester hydrolase activity Source: MTBBASE
    • phospholipase C activity Source: MTBBASE
    • triglyceride lipase activity Source: GO_Central

    GO - Biological processi

    • catabolic process Source: GO_Central
    • growth of symbiont in host cell Source: MTBBASE
    • response to acidic pH Source: MTBBASE
    • response to host immune response Source: MTBBASE
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Keywords - Biological processi

    Stress response

    Enzyme and pathway databases

    BioCyciMTBRV:RV3487C-MONOMER.

    Protein family/group databases

    ESTHERimyctu-Rv3487c. Hormone-sensitive_lipase_like_1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carboxylesterase LipF (EC:3.1.1.1)
    Gene namesi
    Name:lipF
    Ordered Locus Names:Rv3487c
    OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    Taxonomic identifieri83332 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    Proteomesi
    • UP000001584 Componenti: Chromosome

    Organism-specific databases

    TubercuListiRv3487c.

    Pathology & Biotechi

    Disruption phenotypei

    Mutants show reduced ability to grow in a mouse lung.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi90 – 901S → A: Loss of activity. 1 Publication
    Mutagenesisi189 – 1891E → A: Loss of activity. 1 Publication
    Mutagenesisi219 – 2191H → A: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 277277Carboxylesterase LipFPRO_0000419168Add
    BLAST

    Proteomic databases

    PaxDbiO06350.
    PRIDEiO06350.

    Expressioni

    Inductioni

    Induced by acidic pH.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi83332.Rv3487c.

    Structurei

    3D structure databases

    ProteinModelPortaliO06350.
    SMRiO06350. Positions 3-243.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi20 – 223Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion holeBy similarity

    Sequence similaritiesi

    Belongs to the 'GDXG' lipolytic enzyme family.Curated

    Phylogenomic databases

    HOGENOMiHOG000152319.
    InParanoidiO06350.
    OMAiKCADAPV.
    PhylomeDBiO06350.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR013094. AB_hydrolase_3.
    IPR033140. Lipase_GDXG_put_SER_AS.
    [Graphical view]
    PfamiPF07859. Abhydrolase_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS01174. LIPASE_GDXG_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O06350-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRAPGVRAAD GAGRVVLYLH GGAFVMCGPN SHSRIVNALS GFAESPVLIV
    60 70 80 90 100
    DYRLIPKHSL GMALDDCHDA YQWLRARGYR PEQIVLAGDS AGGYLALALA
    110 120 130 140 150
    QRLQCDDEKP AAIVAISPLL QLAKGPKQDH PNIGTDAMFP ARAFDALAAW
    160 170 180 190 200
    VRAAAAKNMV DGRPEDLYEP LDHIESSLPP TLIHVSGSEV LLHDAQLGAG
    210 220 230 240 250
    KLAAAGVCAE VRVWPGQAHL FQLATPLVPE ATRSLRQIGQ FIRDATADSS
    260 270
    LSPVHRSRYV AGSPRAASRG AFGQSPI
    Length:277
    Mass (Da):29,430
    Last modified:July 5, 2004 - v3
    Checksum:i79E38E7E4F8DE54D
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL123456 Genomic DNA. Translation: CCP46309.1.
    PIRiD70569.
    RefSeqiNP_218004.3. NC_000962.3.
    WP_003418946.1. NZ_KK339370.1.

    Genome annotation databases

    EnsemblBacteriaiCCP46309; CCP46309; Rv3487c.
    GeneIDi888430.
    KEGGimtu:Rv3487c.
    PATRICi18156368. VBIMycTub87468_3894.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL123456 Genomic DNA. Translation: CCP46309.1.
    PIRiD70569.
    RefSeqiNP_218004.3. NC_000962.3.
    WP_003418946.1. NZ_KK339370.1.

    3D structure databases

    ProteinModelPortaliO06350.
    SMRiO06350. Positions 3-243.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi83332.Rv3487c.

    Protein family/group databases

    ESTHERimyctu-Rv3487c. Hormone-sensitive_lipase_like_1.

    Proteomic databases

    PaxDbiO06350.
    PRIDEiO06350.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCCP46309; CCP46309; Rv3487c.
    GeneIDi888430.
    KEGGimtu:Rv3487c.
    PATRICi18156368. VBIMycTub87468_3894.

    Organism-specific databases

    TubercuListiRv3487c.

    Phylogenomic databases

    HOGENOMiHOG000152319.
    InParanoidiO06350.
    OMAiKCADAPV.
    PhylomeDBiO06350.

    Enzyme and pathway databases

    BioCyciMTBRV:RV3487C-MONOMER.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR013094. AB_hydrolase_3.
    IPR033140. Lipase_GDXG_put_SER_AS.
    [Graphical view]
    PfamiPF07859. Abhydrolase_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS01174. LIPASE_GDXG_SER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiLIPF_MYCTU
    AccessioniPrimary (citable) accession number: O06350
    Secondary accession number(s): F2GJ51, L0TCW1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2012
    Last sequence update: July 5, 2004
    Last modified: July 6, 2016
    This is version 102 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
      Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
    2. 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.