ID   LNT_WIGBR               Reviewed;         499 AA.
AC   Q8D2A8;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 92.
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};
GN   Name=lnt {ECO:0000255|HAMAP-Rule:MF_01148}; OrderedLocusNames=WIGBR4460;
OS   Wigglesworthia glossinidia brevipalpis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Wigglesworthia.
OX   NCBI_TaxID=36870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12219091; DOI=10.1038/ng986;
RA   Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M.,
RA   Aksoy S.;
RT   "Genome sequence of the endocellular obligate symbiont of tsetse flies,
RT   Wigglesworthia glossinidia.";
RL   Nat. Genet. 32:402-407(2002).
CC   -!- FUNCTION: Catalyzes the phospholipid dependent N-acylation of the N-
CC       terminal cysteine of apolipoprotein, the last step in lipoprotein
CC       maturation. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01148};
CC   -!- PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl
CC       transfer). {ECO:0000255|HAMAP-Rule:MF_01148}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01148};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01148}.
CC   -!- SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N-
CC       acyltransferase subfamily. {ECO:0000255|HAMAP-Rule:MF_01148}.
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DR   EMBL; BA000021; BAC24592.1; -; Genomic_DNA.
DR   RefSeq; WP_011070250.1; NC_004344.2.
DR   AlphaFoldDB; Q8D2A8; -.
DR   SMR; Q8D2A8; -.
DR   STRING; 36870.25166402; -.
DR   EnsemblBacteria; BAC24592; BAC24592; BAC24592.
DR   KEGG; wbr:lnt; -.
DR   eggNOG; COG0815; Bacteria.
DR   HOGENOM; CLU_019563_3_0_6; -.
DR   OMA; IPQSMKW; -.
DR   OrthoDB; 1291198at2; -.
DR   UniPathway; UPA00666; -.
DR   Proteomes; UP000000562; 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   3: Inferred from homology;
KW   Acyltransferase; Cell membrane; Membrane; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..499
FT                   /note="Apolipoprotein N-acyltransferase"
FT                   /id="PRO_0000178111"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        476..496
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   DOMAIN          217..461
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   ACT_SITE        257
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   ACT_SITE        320
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   ACT_SITE        372
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
SQ   SEQUENCE   499 AA;  57258 MW;  6662D4F5180E7C7B CRC64;
     MIKIFTALFF GSLNVISFSP YNFWPASIIS IFGLLIITTN CKNLINSAKL GFLWGIGNFF
     NEIYWIYISI NKFFGINLFF SIIIILLLSS YLSLYPTIFV ILTKFFFPKI NFFLFCVGAP
     SAWMISEILR SKILTGFPWL EIGYSQINGP LKGLAPIIGV SGISYILIII SGMCVLSFYK
     KSYYPIIFII FIITLTYPLN FFKWYSVKEK STKIALIQGN ISQHTYIDNN QIQKNLEQYL
     KITKKIINSS NIIIWPESAI PCDEISCRNF LLKIDKELKL KKSYLITGII SLKKSNYYNS
     IITLGGNSPY LDNSKNKYYK YNLVPFGEKL PLKSILNPIF NKLGLSLIDL KKGDFFQNQL
     KIFDFNIVPS ICYEIIFGDR IRKNVKINTD FLLTISNDSW FGDSIGPWQH FNMARMRALE
     TGKNLLRASN NGITAIIGPN GELKSKLPQF VNDFLLEEVF STMGVTPYVK FGNIPLLFFS
     IICFIISFFI KIKLIFLKN