CULP4_MYCTU
ID CULP4_MYCTU Reviewed; 226 AA.
AC O06319; F2GIK6; I6YG67;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Phospholipase Culp4 {ECO:0000305};
DE EC=3.1.1.- {ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20103719};
DE AltName: Full=Cutinase-like protein 4 {ECO:0000303|PubMed:19225166};
DE Short=Culp4 {ECO:0000303|PubMed:19225166};
DE Flags: Precursor;
GN Name=cut4 {ECO:0000312|EMBL:CCP46274.1};
GN OrderedLocusNames=Rv3452 {ECO:0000312|EMBL:CCP46274.1};
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]
RP SUBCELLULAR LOCATION.
RX PubMed=17416658; DOI=10.1128/jb.01909-06;
RA Parker S.K., Curtin K.M., Vasil M.L.;
RT "Purification and characterization of mycobacterial phospholipase A: an
RT activity associated with mycobacterial cutinase.";
RL J. Bacteriol. 189:4153-4160(2007).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC STRAIN=H37Rv;
RX PubMed=19225166; DOI=10.1096/fj.08-114421;
RA West N.P., Chow F.M., Randall E.J., Wu J., Chen J., Ribeiro J.M.,
RA Britton W.J.;
RT "Cutinase-like proteins of Mycobacterium tuberculosis: characterization of
RT their variable enzymatic functions and active site identification.";
RL FASEB J. 23:1694-1704(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=20103719; DOI=10.1096/fj.09-144766;
RA Schue M., Maurin D., Dhouib R., Bakala N'Goma J.C., Delorme V., Lambeau G.,
RA Carriere F., Canaan S.;
RT "Two cutinase-like proteins secreted by Mycobacterium tuberculosis show
RT very different lipolytic activities reflecting their physiological
RT function.";
RL FASEB J. 24:1893-1903(2010).
RN [5]
RP IMMUNOGENICITY.
RX PubMed=29709002; DOI=10.1371/journal.pone.0196470;
RA Renier W., Bourdin A., Rubbo P.A., Peries M., Dedieu L., Bendriss S.,
RA Kremer L., Canaan S., Terru D., Godreuil S., Nagot N., Van de Perre P.,
RA Tuaillon E.;
RT "B cells response directed against Cut4 and CFP21 lipolytic enzymes in
RT active and latent tuberculosis infections.";
RL PLoS ONE 13:e0196470-e0196470(2018).
CC -!- FUNCTION: A2-type phospholipase, which is probably involved in the
CC degradation of macrophage membrane (PubMed:20103719). Hydrolyzes
CC dipalmitoylphosphatidylcholine (PubMed:20103719). Also shows moderate
CC esterase activity and hydrolyzes the p-nitrophenol-linked aliphatic
CC ester pNP-butyrate (C4) (PubMed:19225166, PubMed:20103719). Does not
CC exhibit cutinase activity (PubMed:19225166).
CC {ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20103719}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000269|PubMed:20103719};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000269|PubMed:20103719};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate +
CC H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477;
CC Evidence={ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20103719};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349;
CC Evidence={ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20103719};
CC -!- ACTIVITY REGULATION: Inhibited by high concentrations of paraoxon
CC (PubMed:19225166). Inhibited by tetrahydrolipstatin (THL), a specific
CC lipase inhibitor (PubMed:20103719). {ECO:0000269|PubMed:19225166,
CC ECO:0000269|PubMed:20103719}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20103719}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17416658}.
CC Secreted, cell wall {ECO:0000269|PubMed:17416658}.
CC -!- MISCELLANEOUS: Circulating B cells able to spontaneously generate
CC specific antibodies directed against Culp4 are detected during active
CC tuberculosis and in some latent-tuberculosis cases.
CC {ECO:0000269|PubMed:29709002}.
CC -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46274.1; -; Genomic_DNA.
DR RefSeq; NP_217969.1; NC_000962.3.
DR RefSeq; WP_003418339.1; NZ_NVQJ01000065.1.
DR AlphaFoldDB; O06319; -.
DR SMR; O06319; -.
DR STRING; 83332.Rv3452; -.
DR SwissLipids; SLP:000001447; -.
DR ESTHER; myctu-RV3452; Cutinase.
DR PaxDb; O06319; -.
DR GeneID; 45427442; -.
DR GeneID; 887610; -.
DR KEGG; mtu:Rv3452; -.
DR PATRIC; fig|83332.111.peg.3847; -.
DR TubercuList; Rv3452; -.
DR eggNOG; ENOG5030PZC; Bacteria.
DR InParanoid; O06319; -.
DR OMA; GAMVTHA; -.
DR PhylomeDB; O06319; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IDA:MTBBASE.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:MTBBASE.
DR GO; GO:0016042; P:lipid catabolic process; IDA:MTBBASE.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000675; Cutinase/axe.
DR PANTHER; PTHR33630; PTHR33630; 1.
DR Pfam; PF01083; Cutinase; 1.
DR SMART; SM01110; Cutinase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall; Disulfide bond; Hydrolase; Membrane;
KW Reference proteome; Secreted; Serine esterase; Signal.
FT SIGNAL 1..45
FT /evidence="ECO:0000255"
FT CHAIN 46..226
FT /note="Phospholipase Culp4"
FT /evidence="ECO:0000255"
FT /id="PRO_5010306774"
FT ACT_SITE 128
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O53581"
FT ACT_SITE 195
FT /evidence="ECO:0000250|UniProtKB:O53581"
FT ACT_SITE 207
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O53581"
FT SITE 129
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 47..117
FT /evidence="ECO:0000250|UniProtKB:O53581"
FT DISULFID 191..198
FT /evidence="ECO:0000250|UniProtKB:O53581"
SQ SEQUENCE 226 AA; 23113 MW; DA956ABFC1085AFE CRC64;
MIPRPQPHSG RWRAGAARRL TSLVAAAFAA ATLLLTPALA PPASAGCPDA EVVFARGTGE
PPGLGRVGQA FVSSLRQQTN KSIGTYGVNY PANGDFLAAA DGANDASDHI QQMASACRAT
RLVLGGYSQG AAVIDIVTAA PLPGLGFTQP LPPAADDHIA AIALFGNPSG RAGGLMSALT
PQFGSKTINL CNNGDPICSD GNRWRAHLGY VPGMTNQAAR FVASRI
