LNT_CAMJE
ID LNT_CAMJE Reviewed; 441 AA.
AC Q9PNJ9; Q0P9F9;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=Cj1095;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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; AL111168; CAL35212.1; -; Genomic_DNA.
DR PIR; B81313; B81313.
DR RefSeq; WP_002852744.1; NC_002163.1.
DR RefSeq; YP_002344488.1; NC_002163.1.
DR AlphaFoldDB; Q9PNJ9; -.
DR SMR; Q9PNJ9; -.
DR STRING; 192222.Cj1095; -.
DR PaxDb; Q9PNJ9; -.
DR PRIDE; Q9PNJ9; -.
DR EnsemblBacteria; CAL35212; CAL35212; Cj1095.
DR GeneID; 905386; -.
DR KEGG; cje:Cj1095; -.
DR PATRIC; fig|192222.6.peg.1077; -.
DR eggNOG; COG0815; Bacteria.
DR HOGENOM; CLU_050649_0_0_7; -.
DR OMA; HPFGFDW; -.
DR UniPathway; UPA00666; -.
DR Proteomes; UP000000799; 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 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 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..441
FT /note="Apolipoprotein N-acyltransferase"
FT /id="PRO_0000178052"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 133..153
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 178..198
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT DOMAIN 215..441
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 256
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 310
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 359
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
SQ SEQUENCE 441 AA; 52109 MW; E5CA2CC32C1B64B0 CRC64;
MKLKLNFLPY FSFIPKKLNT NSIIFKIIKV FFIAILLSNS IYLSFFENIF TQTISPFLAI
WGLVLLLKSK TSKQYFWIGF FVGILWFWWI GLSSIYFNLN YLVPIIPIII GFIYGLLFRL
CYLLKFDFLR LCGIFCISFI HPLGFDWFNW GIFTVYGFFD PSYRGIICIF LIAYFIYEGY
ISRYYKIAIV LILFFSGFQY NEKQAQTLNL NYKLINTNIS QDQKFLQENL KSNSDILIQD
ILQAINEKKE LVILPETAFA FDLKNTKYEL MLKELSYKIT IITGAFHVEK EHTYNSTYIF
KKGNVYILNK HFLVPFGEEI PFFKDLTKKY FLKNIEEFSK GPIQSKYKLD NQIITNAICY
EATKEQNYQN SQIIIALSNN AWFNNSSEYK LQQLLMKFYA SKYGVSVYHA TNGKENIVIL
PKKLLSKDWK NLSKEIFNDK K
