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GDSL_MYCTU
ID   GDSL_MYCTU              Reviewed;         231 AA.
AC   O33363; F2GND3; I6Y810; Q7D9Q4;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=GDSL lipase Rv0518 {ECO:0000305};
DE            EC=3.1.1.- {ECO:0000269|PubMed:31125644};
DE   Flags: Precursor;
GN   OrderedLocusNames=Rv0518 {ECO:0000312|EMBL:CCP43255.1};
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2] {ECO:0007744|PubMed:21969609}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBCELLULAR LOCATION, INDUCTION, AND MUTAGENESIS OF SER-46;
RP   GLY-87; ASN-120; ASP-205 AND HIS-208.
RC   STRAIN=H37Rv;
RX   PubMed=31125644; DOI=10.1016/j.ijbiomac.2019.05.121;
RA   Kaur J., Kaur J.;
RT   "Rv0518, a nutritive stress inducible GDSL lipase of Mycobacterium
RT   tuberculosis, enhanced intracellular survival of bacteria by cell wall
RT   modulation.";
RL   Int. J. Biol. Macromol. 135:180-195(2019).
CC   -!- FUNCTION: GDSL lipase that catalyzes the hydrolysis of p-nitrophenyl
CC       (pNP) esters. pNP-decanoate (C10) is the preferred substrate. It can
CC       also use pNP-octanoate (C8), pNP-dodecanoate (C12) and pNP-
CC       tetradecanoate (C14). Has lower activity with pNP-butyrate (C4), pNP-
CC       palmitate (C16) and pNP-stearate (C18) (PubMed:31125644). Does not show
CC       phospholipase A1 activity (PubMed:31125644). Might help bacteria to
CC       utilize available lipids for its growth as well as provide resistance
CC       to various intracellular stresses by cell wall modulation resulting in
CC       enhanced intracellular survival (PubMed:31125644).
CC       {ECO:0000269|PubMed:31125644}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acid ester + H2O = a fatty acid + an aliphatic alcohol
CC         + H(+); Xref=Rhea:RHEA:59388, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:35748;
CC         Evidence={ECO:0000269|PubMed:31125644};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=decanoate ester + H2O = an aliphatic alcohol + decanoate +
CC         H(+); Xref=Rhea:RHEA:47360, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:87658;
CC         Evidence={ECO:0000269|PubMed:31125644};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) +
CC         octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657;
CC         Evidence={ECO:0000269|PubMed:31125644};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dodecanoate ester + H2O = an aliphatic alcohol + dodecanoate
CC         + H(+); Xref=Rhea:RHEA:47364, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:87659;
CC         Evidence={ECO:0000269|PubMed:31125644};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a tetradecanoate ester + H2O = an aliphatic alcohol + H(+) +
CC         tetradecanoate; Xref=Rhea:RHEA:47388, ChEBI:CHEBI:2571,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807,
CC         ChEBI:CHEBI:87691; Evidence={ECO:0000269|PubMed:31125644};
CC   -!- ACTIVITY REGULATION: Activity is inhibited by the serine modifier
CC       phenylmethylsulfonyl fluoride (PMSF). {ECO:0000269|PubMed:31125644}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=400 uM for pNP-decanoate {ECO:0000269|PubMed:31125644};
CC         Note=kcat is 14440 min(-1) with pNP-decanoate as substrate.
CC         {ECO:0000269|PubMed:31125644};
CC       pH dependence:
CC         Optimum pH is 9.0 (with pNP-decanoate as substrate).
CC         {ECO:0000269|PubMed:31125644};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius (with pNP-decanoate as
CC         substrate). {ECO:0000269|PubMed:31125644};
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000269|PubMed:31125644}. Secreted, extracellular space
CC       {ECO:0000269|PubMed:31125644}.
CC   -!- INDUCTION: Expression is up-regulated under nutrient starvation (in
CC       strain H37Ra). {ECO:0000269|PubMed:31125644}.
CC   -!- MISCELLANEOUS: Expression in M.smegmatis alters colony morphology and
CC       growth kinetics, provides resistance to SDS, lysozyme and anti-TB
CC       drugs, increases the total lipid content and trehalose dimycolates, and
CC       enhances infection ability and intracellular survival capability of
CC       M.smegmatis. {ECO:0000269|PubMed:31125644}.
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AL123456; CCP43255.1; -; Genomic_DNA.
DR   RefSeq; NP_215032.1; NC_000962.3.
DR   RefSeq; WP_003402818.1; NZ_NVQJ01000068.1.
DR   AlphaFoldDB; O33363; -.
DR   SMR; O33363; -.
DR   STRING; 83332.Rv0518; -.
DR   PaxDb; O33363; -.
DR   PRIDE; O33363; -.
DR   DNASU; 887321; -.
DR   GeneID; 887321; -.
DR   KEGG; mtu:Rv0518; -.
DR   PATRIC; fig|83332.111.peg.571; -.
DR   TubercuList; Rv0518; -.
DR   eggNOG; COG2755; Bacteria.
DR   OMA; SRNDQGV; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1110; -; 1.
DR   InterPro; IPR013830; SGNH_hydro.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   Pfam; PF13472; Lipase_GDSL_2; 1.
PE   1: Evidence at protein level;
KW   Cell wall; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Reference proteome; Secreted; Serine esterase; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..231
FT                   /note="GDSL lipase Rv0518"
FT                   /id="PRO_0000448306"
FT   ACT_SITE        46
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P41734"
FT   ACT_SITE        205
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P41734"
FT   ACT_SITE        208
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P41734"
FT   SITE            87
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P41734"
FT   SITE            120
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P41734"
FT   MUTAGEN         46
FT                   /note="S->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:31125644"
FT   MUTAGEN         87
FT                   /note="G->A: Retains 50-55% of activity."
FT                   /evidence="ECO:0000269|PubMed:31125644"
FT   MUTAGEN         120
FT                   /note="N->A: Retains 50-55% of activity."
FT                   /evidence="ECO:0000269|PubMed:31125644"
FT   MUTAGEN         205
FT                   /note="D->A: Retains 15-20% of activity."
FT                   /evidence="ECO:0000269|PubMed:31125644"
FT   MUTAGEN         208
FT                   /note="H->A: Retains 15-20% of activity."
FT                   /evidence="ECO:0000269|PubMed:31125644"
SQ   SEQUENCE   231 AA;  24636 MW;  7BF0F8B5E48785A9 CRC64;
     MSRPGTYVIG LTLLVGLVVG NPGCPRSYRP LTLDYRLNPV AVIGDSYTTG TDEGGLGSKS
     WTARTWQMLA ARGVRIAADV AAEGRAGYGV PGDHGNVFED LTARAVQPDD ALVVFFGSRN
     DQGMDPEDPE MLAEKVRDTF DLARHRAPSA SLLVIAPPWP TADVPGPMLR IRDVLGAQAR
     AAGAVFVDPI ADHWFVDRPE LIGADGVHPN DAGHEYLADK IAPLISMELV G
 
 
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