LNT1_LEPIN
ID LNT1_LEPIN Reviewed; 576 AA.
AC Q8F724;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Apolipoprotein N-acyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_01148};
DE Short=ALP N-acyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_01148};
DE EC=2.3.1.269 {ECO:0000255|HAMAP-Rule:MF_01148};
GN Name=lnt1 {ECO:0000255|HAMAP-Rule:MF_01148}; OrderedLocusNames=LA_1124;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAN48323.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE010300; AAN48323.2; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_711305.2; NC_004342.2.
DR RefSeq; WP_000499632.1; NC_004342.2.
DR AlphaFoldDB; Q8F724; -.
DR SMR; Q8F724; -.
DR EnsemblBacteria; AAN48323; AAN48323; LA_1124.
DR KEGG; lil:LA_1124; -.
DR PATRIC; fig|189518.3.peg.1116; -.
DR HOGENOM; CLU_019563_3_1_12; -.
DR InParanoid; Q8F724; -.
DR OMA; FSWMLSD; -.
DR UniPathway; UPA00666; -.
DR Proteomes; UP000001408; Chromosome I.
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 Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; SSF56317; 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..576
FT /note="Apolipoprotein N-acyltransferase 1"
FT /id="PRO_0000178074"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 128..148
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 204..224
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 549..569
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT DOMAIN 236..538
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 285
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 355
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 446
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
SQ SEQUENCE 576 AA; 66158 MW; C1B9F08BF163B248 CRC64;
MFYNFISKDS ILYRLILCFG IGIGTVFGLS PFSFFSAGVF ASISCIFLFF SLNRTSIWKA
FLWLLILSQI LNFTAFYWIP GAISRISGVN TFVSILFFFL YGLISHLKFF LFYTLFRFSK
IDSASKTYIL LIFPAAGTLS DMITFQIFPW YWGNLISGSI VFEQFASICG VYGLSFLLLF
ISSTFLILVN YYKYKNSKEF KTSIASLICI TFIYGFGLYR IGYINQSQNE LKPKNLSVLM
IQPDTSPGTK DLKADASYLS ATMSKVFSLA IPTFENSPSL IVIPESAIPF HGTIDSEENR
KEKIYSSTME GIILYLSKHT GADVLFNELN LDENKLRNQV SLFKNLDGKT ERYNKRRLLP
FGEYLPMEKN FPFLRSIFQE TSRYVPGEFP KLLIGNKIQN QRSFLPPEIS KLNEPKTYRY
EFSSIVEHTN KIRNLEYSYS ILPLLCYEAM FTELVLDYFQ NEQKPEVLIN ITNDSWFDSE
LEAYQHSGAV RLRAIETGLP LIRSAVSGIS EVWDARGIPM IVPIGFHETG TRAFSIRLDA
IESTIYTRFG NSFLWIFCIL ILISRLIFVS RIERKS
