ID   LNT_PASMU               Reviewed;         520 AA.
AC   Q9CM14;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
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};
GN   Name=lnt {ECO:0000255|HAMAP-Rule:MF_01148}; OrderedLocusNames=PM1032;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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 inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01148}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01148}.
CC   -!- SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N-
CC       acyltransferase subfamily. {ECO:0000255|HAMAP-Rule:MF_01148}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE004439; AAK03116.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9CM14; -.
DR   SMR; Q9CM14; -.
DR   STRING; 747.DR93_937; -.
DR   EnsemblBacteria; AAK03116; AAK03116; PM1032.
DR   KEGG; pmu:PM1032; -.
DR   HOGENOM; CLU_019563_3_0_6; -.
DR   OMA; YVALVPW; -.
DR   UniPathway; UPA00666; -.
DR   Proteomes; UP000000809; 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 inner membrane; Cell membrane; Membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..520
FT                   /note="Apolipoprotein N-acyltransferase"
FT                   /id="PRO_0000178079"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        484..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   DOMAIN          232..479
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   ACT_SITE        272
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   ACT_SITE        338
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   ACT_SITE        390
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
SQ   SEQUENCE   520 AA;  58733 MW;  6BDECCC33A51D167 CRC64;
     MLHYLKKMKK KIFTYFIAIF SGIIGVLAFS PFDYWGCAYL SLLGLIFVAK TAEKKTALWS
     AFLWGLAFFT FGINWVHVSI HQFGGASVVV SYVLVLVLAA YLALYPMLFA YLIQRFQISS
     LAMFPVIWTF TEFLRGWLFT GFPWLQFGYS QIDSPFAHLA PMFGVTGVTF FVMWVSAVIF
     NLLSVLLIKP RKWNVVIANL LLLTLVGGLS AYSSKAEYVR KIEDRDLLVT LAQGNIEQNL
     KWEPEYLYQT LDIYHKLISQ HLGKTDVIIL PESALPVLEN HIQPFFQGLQ AHAQQAGTEI
     VMGTIYQDKT ANKLLNSIIT LGNTDFPYSL ETTNRYSKHH LVPFGEYVPL ETLLRPLGSV
     FNLPMSAFQS GDEIQSPLVV KNRQLSAAIC YEIILGEQLR KNVKQDTDFI LTVSNDAWFG
     DSIGPWQHLQ MARMRALEFG KPVIRATNTG ISVFIDEQGK IVAQAPQFIE TTLTHKVAAT
     EGQTPYAVFG NTAIYGLSLL LLLMRGFGAL IRRRLFMPRL