ID A0A0F7KL86_9PROT Unreviewed; 497 AA.
AC A0A0F7KL86;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=AAW31_17560 {ECO:0000313|EMBL:AKH39734.1};
OS Nitrosomonas communis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=44574 {ECO:0000313|EMBL:AKH39734.1, ECO:0000313|Proteomes:UP000034156};
RN [1] {ECO:0000313|Proteomes:UP000034156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nm2 {ECO:0000313|Proteomes:UP000034156};
RA Kozlowski J.A., Kits K.D., Stein L.Y.;
RT "Draft genome of Nitrosomonas communis strain Nm2.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AKH39734.1, ECO:0000313|Proteomes:UP000034156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nm2 {ECO:0000313|EMBL:AKH39734.1,
RC ECO:0000313|Proteomes:UP000034156};
RX PubMed=26769932;
RA Kozlowski J.A., Kits K.D., Stein L.Y.;
RT "Genome Sequence of Nitrosomonas communis Strain Nm2, a Mesophilic Ammonia-
RT Oxidizing Bacterium Isolated from Mediterranean Soil.";
RL Genome Announc. 4:0-0(2016).
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|ARBA:ARBA00010065,
CC ECO:0000256|HAMAP-Rule:MF_01148}.
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DR EMBL; CP011451; AKH39734.1; -; Genomic_DNA.
DR RefSeq; WP_046851932.1; NZ_VNHT01000020.1.
DR AlphaFoldDB; A0A0F7KL86; -.
DR KEGG; nco:AAW31_17560; -.
DR PATRIC; fig|44574.3.peg.4222; -.
DR UniPathway; UPA00666; -.
DR Proteomes; UP000034156; Chromosome.
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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01148};
KW Reference proteome {ECO:0000313|Proteomes:UP000034156};
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..39
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 46..69
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 81..105
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 117..140
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 152..175
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 187..204
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 472..491
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT DOMAIN 219..460
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
SQ SEQUENCE 497 AA; 55531 MW; C72EA70A04EDEA9A CRC64;
MNLKIILSFL SGALTVLGFA PFYFFPIPLV TLALLIYFWR HNITPLTAAI LGFSFGMGMF
GTGVTWIYVS LHDFGNMPMP LAVLALILLC AYLSLFPALT GWISVRLRTA APAIWPWMIA
SLWILSEWLR GTLFTGFPWL AVGYSQAPSS PLIGFAPVVG VYGISLLLVL SAGWLSSWFE
QRRSWRCLFF LGGVWVIGLG LQGIEWTRPE GDAVTVSLLQ GNIPQDLKWR EDHVITTMDT
YAKLIQESNS QLIVTPEISI PLFHEDVPFD YLSELAAHAR ANEGDVLIGM AEAVSSDRNE
YYNTMFSLGV SPEQRYRKHH LVPFGEYIPL KLVFGWIIKV LNMPLSDFSR GSLDQQPLYL
AGQNVAINIC YEDVFGEEII MQLPEASLLV NVSNDAWFGR SIGPWQHLQI SQMRALETGR
YMLRATNTGV TAIIDQRGNL VQQLEMFTTA GLHGIAQGYS GATPYVRLGN SLVLGLAILL
LTTGWLSVFF YRKRKTL
//
