ID A0A1I3K429_9ACTN Unreviewed; 512 AA.
AC A0A1I3K429;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Apolipoprotein N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_01148};
DE Short=ALP N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_01148};
DE EC=2.3.1.269 {ECO:0000256|HAMAP-Rule:MF_01148};
GN Name=lnt {ECO:0000256|HAMAP-Rule:MF_01148};
GN ORFNames=SAMN05216561_111130 {ECO:0000313|EMBL:SFI67261.1};
OS Nocardioides psychrotolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1005945 {ECO:0000313|EMBL:SFI67261.1, ECO:0000313|Proteomes:UP000198649};
RN [1] {ECO:0000313|EMBL:SFI67261.1, ECO:0000313|Proteomes:UP000198649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.11156 {ECO:0000313|EMBL:SFI67261.1,
RC ECO:0000313|Proteomes:UP000198649};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phospholipid dependent N-acylation of the N-
CC terminal cysteine of apolipoprotein, the last step in lipoprotein
CC maturation. {ECO:0000256|HAMAP-Rule:MF_01148}.
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:0000256|HAMAP-Rule:MF_01148};
CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl
CC transfer). {ECO:0000256|HAMAP-Rule:MF_01148}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01148};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01148}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N-
CC acyltransferase subfamily. {ECO:0000256|HAMAP-Rule:MF_01148}.
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DR EMBL; FOQG01000011; SFI67261.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3K429; -.
DR STRING; 1005945.SAMN05216561_111130; -.
DR UniPathway; UPA00666; -.
DR Proteomes; UP000198649; Unassembled WGS sequence.
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; Carbon-nitrogen hydrolase; 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 NCBIfam; TIGR00546; lnt; 1.
DR PANTHER; PTHR38686; APOLIPOPROTEIN N-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR38686:SF1; APOLIPOPROTEIN N-ACYLTRANSFERASE; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR Pfam; PF20154; LNT_N; 1.
DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_01148};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01148}; Lipoprotein {ECO:0000313|EMBL:SFI67261.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01148};
KW Reference proteome {ECO:0000313|Proteomes:UP000198649};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01148};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01148};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01148}.
FT TRANSMEM 6..35
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 47..65
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 77..96
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 103..122
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 142..168
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 175..192
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT DOMAIN 203..456
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
SQ SEQUENCE 512 AA; 54191 MW; A428BD39AF3BBC6E CRC64;
MLLRTSLALV AGLTLSLAFE PLALPIVMPF AVAAFFLSTR GLRARSAWIP GLGFGVAFYF
THISWMRDSI GPDAWVALAT IESLFYAVLG SVTAALHRRR LWALWMAPAW VTMEVVRSGW
PFSGMPWGRL AFGVVDTPAA PALPYVGSVG VSLLVALVSS LLAWVVVARG REQRVAGGAS
VAVLALTLLP ALTPYDVEET GQATVAAVQG NLPGPADNIL FDSQQVTDNH VQATIDLADQ
IAAGAQPEVD FVLWPENSTA SDPFGNAAVN AGIRSASAAI GVPILVGAIV DAGPDHVLNQ
GIVWDPVTGA GERYTKRHPV PYGEYIPLRD YLDGTFGKLA LIPRDMLSGS RKTPLEIAGI
SVADAICFDI AYDDGLYDQV SRGAELLTVQ TSNASFIFTD QIDQQFAMTR LRAIEAGRWL
VVASPNGISG VISPEGEVVA TADPRTQAVL VEQVGLSSDI TLAVRLGPWV GRSSAVLTGV
GLLLGLLAYR RSRHSPAPGG VLDENPEDEV LP
//
