ID   LNT_RICBR               Reviewed;         499 AA.
AC   Q1RH27;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=RBE_1256;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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}.
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DR   EMBL; CP000087; ABE05337.1; -; Genomic_DNA.
DR   RefSeq; WP_011477909.1; NC_007940.1.
DR   AlphaFoldDB; Q1RH27; -.
DR   SMR; Q1RH27; -.
DR   STRING; 336407.RBE_1256; -.
DR   EnsemblBacteria; ABE05337; ABE05337; RBE_1256.
DR   KEGG; rbe:RBE_1256; -.
DR   eggNOG; COG0815; Bacteria.
DR   HOGENOM; CLU_019563_3_1_5; -.
DR   OMA; IPQSMKW; -.
DR   OrthoDB; 1291198at2; -.
DR   UniPathway; UPA00666; -.
DR   Proteomes; UP000001951; 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; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..499
FT                   /note="Apolipoprotein N-acyltransferase"
FT                   /id="PRO_0000277923"
FT   TRANSMEM        9..29
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        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        466..486
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   DOMAIN          220..464
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   ACT_SITE        259
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   ACT_SITE        322
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;  57132 MW;  4770DD96084FA341 CRC64;
     MYKPKISCLL LGLLSGLVFA PTFLLPALLT LSYLCCLVQK SKDWQEAAKL GYIFGFGHFL
     SGIYWISIGV SVYISDFWWA IPFALFGLPI ILAFFVSASC VFSFFVRNNK YYHFIFCLYW
     VLFEWVRSWI FTGLPWNLIG YAFSFSDILI QSLNIIGIYG LSFIVIYIST SFYPFFTKQF
     DQLKVLLLTS SITLAVIITY GSVRLHNHPT NFTDIKVRLV QPSIPQTEKW SEEEFWHNLM
     LHINLSENSQ PIDLVIWSEA ALVVPYDIPV VKSELLGLLN SVDATLITGG ISDNKKRGED
     FELYTAMYAL EKNGNKLFEY HKSHLVPFGE YMPFKKILPF KKLTHGFVDY TEGNGGLVYL
     DKYNLKIKPL ICYESIFPDF VRTNNETADV IINVTNDAWY GKSSGPYQHF HISRSRAVEN
     GLPMVRVANN GISAIIDPLG RVIKKLDLNE INYIDGLIPK KLDSPTIFSK FGNITILLIV
     FFIFLVNYLL DKKLINSRD