LNT_MYCS2
ID LNT_MYCS2 Reviewed; 594 AA.
AC A0QZ13;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 2.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Apolipoprotein N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_01148};
DE Short=ALP N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_01148};
DE EC=2.3.1.269 {ECO:0000255|HAMAP-Rule:MF_01148};
DE AltName: Full=LntMs;
GN Name=lnt {ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000305|PubMed:19661058};
GN Synonyms=ppm2 {ECO:0000303|PubMed:12427759}; OrderedLocusNames=MSMEG_3860;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP STIMULATES PPM SYNTHASE, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, AND
RP EXPRESSION IN E.COLI.
RX PubMed=12427759; DOI=10.1074/jbc.m207922200;
RA Baulard A.R., Gurcha S.S., Engohang-Ndong J., Gouffi K., Locht C.,
RA Besra G.S.;
RT "In vivo interaction between the polyprenol phosphate mannose synthase Ppm1
RT and the integral membrane protein Ppm2 from Mycobacterium smegmatis
RT revealed by a bacterial two-hybrid system.";
RL J. Biol. Chem. 278:2242-2248(2003).
RN [3]
RP FUNCTION AS AN N-ACYLTRANSFERASE, AND DISRUPTION PHENOTYPE.
RX PubMed=19661058; DOI=10.1074/jbc.m109.022715;
RA Tschumi A., Nai C., Auchli Y., Hunziker P., Gehrig P., Keller P., Grau T.,
RA Sander P.;
RT "Identification of apolipoprotein N-acyltransferase (Lnt) in
RT mycobacteria.";
RL J. Biol. Chem. 284:27146-27156(2009).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=19944079; DOI=10.1016/j.bbrc.2009.11.120;
RA Bruelle J.K., Grau T., Tschumi A., Auchli Y., Burri R., Polsfuss S.,
RA Keller P.M., Hunziker P., Sander P.;
RT "Cloning, expression and characterization of Mycobacterium tuberculosis
RT lipoprotein LprF.";
RL Biochem. Biophys. Res. Commun. 391:679-684(2010).
CC -!- FUNCTION: Catalyzes the phospholipid dependent N-acylation of the N-
CC terminal cysteine of apolipoprotein, the last step in lipoprotein
CC maturation. Can transfer a number of fatty acids (C16 and C19, palmitic
CC and probably tuberculostearic acids respectively are shown)
CC (PubMed:19661058). Enhances the polyprenol monophosphomannose (PPM)
CC synthase activity of Ppm1 (AC A0QZ12) without itself having PPM
CC synthase catalytic activity (PubMed:12427759).
CC {ECO:0000269|PubMed:12427759, ECO:0000269|PubMed:19661058}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-
CC cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) +
CC N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein];
CC Xref=Rhea:RHEA:48228, Rhea:RHEA-COMP:14681, Rhea:RHEA-COMP:14684,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136912, ChEBI:CHEBI:140656,
CC ChEBI:CHEBI:140657, ChEBI:CHEBI:140660; EC=2.3.1.269;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01148};
CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl
CC transfer). {ECO:0000255|HAMAP-Rule:MF_01148}.
CC -!- SUBUNIT: Interacts with Ppm1 (AC A0QZ12) upon coexpression in E.coli,
CC which increases the PPM synthase activity of Ppm1.
CC {ECO:0000269|PubMed:12427759}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01148,
CC ECO:0000269|PubMed:12427759}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000269|PubMed:12427759}.
CC -!- DISRUPTION PHENOTYPE: Not essential. Loss of N-acylation of
CC apolipoproteins. {ECO:0000269|PubMed:19661058,
CC ECO:0000269|PubMed:19944079}.
CC -!- MISCELLANEOUS: In a number of other Mycobacteria, including M.bovis and
CC M.tuberculosis, this protein is the second domain in a 2 domain
CC protein. {ECO:0000305|PubMed:12427759}.
CC -!- SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N-
CC acyltransferase subfamily. {ECO:0000255|HAMAP-Rule:MF_01148}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK75562.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK75562.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_888151.1; NC_008596.1.
DR AlphaFoldDB; A0QZ13; -.
DR SMR; A0QZ13; -.
DR STRING; 246196.MSMEI_3770; -.
DR PRIDE; A0QZ13; -.
DR EnsemblBacteria; ABK75562; ABK75562; MSMEG_3860.
DR KEGG; msm:MSMEG_3860; -.
DR PATRIC; fig|246196.19.peg.3799; -.
DR eggNOG; COG0815; Bacteria.
DR UniPathway; UPA00666; -.
DR Proteomes; UP000000757; 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:0016410; F:N-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd07571; ALP_N-acyl_transferase; 1.
DR Gene3D; 3.60.110.10; -; 1.
DR HAMAP; MF_01148; Lnt; 1.
DR InterPro; IPR004563; Apolipo_AcylTrfase.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR045378; LNT_N.
DR Pfam; PF00795; CN_hydrolase; 1.
DR Pfam; PF20154; LNT_N; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR TIGRFAMs; TIGR00546; lnt; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cell membrane; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..594
FT /note="Apolipoprotein N-acyltransferase"
FT /id="PRO_0000434585"
FT TOPO_DOM 1..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 68..87
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:12427759"
FT TOPO_DOM 88..116
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 117..134
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:12427759"
FT TOPO_DOM 135..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 139..160
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:12427759"
FT TOPO_DOM 161..221
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 222..239
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:12427759"
FT TOPO_DOM 240..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 252..269
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:12427759"
FT TOPO_DOM 270..554
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:12427759"
FT TRANSMEM 555..572
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:12427759"
FT TOPO_DOM 573..594
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 287..543
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..25
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 340
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 405
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 455
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
SQ SEQUENCE 594 AA; 63346 MW; 7D3BA3C233D022BD CRC64;
MIPAVTDDDP LEDPLDDDVA PGLDDAEPEP EPRDEHDEPS RPATGSRIGG WVARRGSRFG
KGVLDRCAPL SAAIGGGLAL WLSFPPIGWW FTAFPGLALL GWVLTRTATT KAGGFGYGVL
FGLAFYVPLL PWISGLVGAV PWLALAFAES LFCGLFGLGA VVVVRLPGWP LWFATLWVAA
EWAKSTFPFG GFPWGASSYG QTNGPLLALA RIGGAPLVSF AVALIGFSLT LLTAQIVWWW
RHGHKPGVPA PAVMLPGVAI AASLLVTALV WPQVRQSGTG AGDDTAVTVA AVQGNVPRLG
LEFNAQRRAV LDNHVKETLR LADDVKAGRA AQPMFVIWPE NSSDIDPLLN ADASAQITTA
AEAIDAPILV GGVVRADGYT PDNPVANNTV IVWEPTDGPG ERHDKQIVQP FGEYLPWRGF
FKHLSSYADR AGYFVPGTGT GVVHAAGVPI GITTCWEVIF DRAARESVLN GAQVLAVPSN
NATFDEAMSA QQLAFGKLRA VEHDRYVVVA GTTGISAVIA PDGHEISRTE WFQPAYLDNQ
IRLKTDLTPA TKWGPIVQAV LVIAGVAVLL IAILHNGRFA PRMLRRRSAT TVKR
