LYPGN_MYCTU
ID LYPGN_MYCTU Reviewed; 261 AA.
AC P9WG51; L0T858; P64837; P71669;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 07-JAN-2015, sequence version 2.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Lysoplasmalogenase {ECO:0000303|PubMed:35314194};
DE EC=3.3.2.2 {ECO:0000269|PubMed:35314194};
GN OrderedLocusNames=Rv1401; ORFNames=MTCY21B4.18;
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 PROTEIN SEQUENCE OF 2-24, AND SEQUENCE REVISION TO N-TERMINUS.
RC STRAIN=H37Rv;
RX PubMed=34915127; DOI=10.1016/j.ygeno.2021.12.001;
RA Shi J., Meng S., Wan L., Zhang Z., Jiang S., Zhu H., Dai E., Chang L.,
RA Gao H., Wan K., Zhang L., Zhao X., Liu H., Lyu Z., Zhang Y., Xu P.;
RT "Deep N-terminomics of Mycobacterium tuberculosis H37Rv extensively correct
RT annotated encoding genes.";
RL Genomics 114:292-304(2022).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP OVEREXPRESSION IN M.SMEGMATIS.
RC STRAIN=H37Rv;
RX PubMed=35314194; DOI=10.1016/j.jbc.2022.101849;
RA Jurkowitz M.S., Azad A.K., Monsma P.C., Keiser T.L., Kanyo J., Lam T.T.,
RA Bell C.E., Schlesinger L.S.;
RT "Mycobacterium tuberculosis encodes a YhhN family membrane protein with
RT lysoplasmalogenase activity that protects against toxic host lysolipids.";
RL J. Biol. Chem. 298:101849-101849(2022).
CC -!- FUNCTION: Specifically hydrolyzes the vinyl ether bond of
CC lysoplasmenylcholine (pLPC) and lysoplasmenylethanolamine (pLPE) to
CC release a fatty aldehyde and glycerophospho-choline or glycerophospho-
CC ethanolamine (PubMed:35314194). The cleavage activity is specific for
CC lysoplasmalogen substrates, and there is no activity on 1-alkenyl-sn-2-
CC acyl-glycerophospho-ethanolamine or 1-alkenyl-sn-2-acyl-glycerophospho-
CC choline (plasmalogen) substrates (PubMed:35314194). Confers a growth
CC advantage for mycobacteria in host macrophages, possibly by cleaving
CC toxic host pLPC into potentially energy-producing products
CC (PubMed:35314194). {ECO:0000269|PubMed:35314194}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + H2O = a 2,3-
CC saturated aldehyde + sn-glycerol 3-phosphocholine;
CC Xref=Rhea:RHEA:22544, ChEBI:CHEBI:15377, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:73359, ChEBI:CHEBI:77287; EC=3.3.2.2;
CC Evidence={ECO:0000269|PubMed:35314194};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22545;
CC Evidence={ECO:0000305|PubMed:35314194};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O = a
CC 2,3-saturated aldehyde + sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:16905, ChEBI:CHEBI:15377, ChEBI:CHEBI:73359,
CC ChEBI:CHEBI:77288, ChEBI:CHEBI:143890; EC=3.3.2.2;
CC Evidence={ECO:0000269|PubMed:35314194};
CC -!- ACTIVITY REGULATION: Competitively inhibited by lysophosphatidic acid.
CC {ECO:0000269|PubMed:35314194}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=76.9 uM for lysoplasmenylcholine {ECO:0000269|PubMed:35314194};
CC KM=89.4 uM for lysoplasmenylethanolamine
CC {ECO:0000269|PubMed:35314194};
CC Vmax=15.5 umol/min/mg enzyme with lysoplasmenylcholine as substrate
CC {ECO:0000269|PubMed:35314194};
CC Vmax=15.5 umol/min/mg enzyme with lysoplasmenylethanolamine as
CC substrate {ECO:0000269|PubMed:35314194};
CC pH dependence:
CC Optimum pH is 6.6-7.2. {ECO:0000269|PubMed:35314194};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:35314194};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- MISCELLANEOUS: Overexpression of this gene in M.smegmatis increases its
CC survival within infected human macrophages (PubMed:35314194).
CC Overexpression also protects the M.smegmatis spheroplasts, which are
CC cell wall-deficient mycobacterial forms, from membrane disruption/lysis
CC by pLPC, by rapidly catabolizing it and depleting it from the media
CC (PubMed:35314194). {ECO:0000269|PubMed:35314194}.
CC -!- SIMILARITY: Belongs to the TMEM86 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCP44160.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000269|PubMed:34915127};
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DR EMBL; AL123456; CCP44160.1; ALT_INIT; Genomic_DNA.
DR PIR; F70900; F70900.
DR RefSeq; NP_215917.1; NC_000962.3.
DR AlphaFoldDB; P9WG51; -.
DR STRING; 83332.Rv1401; -.
DR PaxDb; P9WG51; -.
DR DNASU; 886733; -.
DR GeneID; 886733; -.
DR KEGG; mtu:Rv1401; -.
DR PATRIC; fig|83332.12.peg.1566; -.
DR TubercuList; Rv1401; -.
DR eggNOG; COG3714; Bacteria.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047408; F:alkenylglycerophosphocholine hydrolase activity; IBA:GO_Central.
DR GO; GO:0047409; F:alkenylglycerophosphoethanolamine hydrolase activity; IBA:GO_Central.
DR InterPro; IPR012506; YhhN.
DR PANTHER; PTHR31885; PTHR31885; 1.
DR Pfam; PF07947; YhhN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Hydrolase; Lipid metabolism;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Virulence.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:34915127"
FT CHAIN 2..261
FT /note="Lysoplasmalogenase"
FT /id="PRO_0000201848"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 261 AA; 27391 MW; DFA3084579718A91 CRC64;
MGSIAGFSSA VLSKLGIPVP YAPRLLAGGW VVAGWAGLAY GVYLTVIALR LPPGSELTGH
AMLQPAFKAS MAVLLAAAAV AHPIGRERRW LVPALLLSAT GDWLLAIPWW TWAFVFGLGA
FLLAHLCFIG ALLPLARQAA PSRGRVAAVV AMCVASAGLL VWFWPHLGKD NLTIPVTVYI
VALSAMVCTA LLARLPTIWT AVGAVCFAAS DSMIGIGRFI LGNEALAVPI WWSYAAAEIL
ITAGFFFGRE VPDNAAAPTD S
