LNT_RALSO
ID LNT_RALSO Reviewed; 523 AA.
AC Q8Y210;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 100.
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=RSc0527;
GN ORFNames=RS04941;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(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 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; AL646052; CAD14055.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8Y210; -.
DR SMR; Q8Y210; -.
DR STRING; 267608.RSc0527; -.
DR EnsemblBacteria; CAD14055; CAD14055; RSc0527.
DR KEGG; rso:RSc0527; -.
DR eggNOG; COG0815; Bacteria.
DR HOGENOM; CLU_019563_3_0_4; -.
DR OMA; IPQSMKW; -.
DR UniPathway; UPA00666; -.
DR Proteomes; UP000001436; 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..523
FT /note="Apolipoprotein N-acyltransferase"
FT /id="PRO_0000178087"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 49..66
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT DOMAIN 246..487
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 284
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 345
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 395
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
SQ SEQUENCE 523 AA; 56513 MW; 32D185FC69739B45 CRC64;
MRALFSSPAA DTAGQQEALA VPLARLRFAA PLAALLGVMH TLAFAPNRWW WLQILSLAGL
AALVRQAPRL RDVAWVGYAF GLGWFLSGIW WLYISMHVYG DMPAWMAAAA VLLFSAYLAL
HPALAAWLWQ RLARGRQLSG AASALVFGAA WLVSEWLRGT EWTGFPWLNG GYAHTDGPLA
GYAPLVGVYG VVAIAATLAG LLCAAAERRL HWLAGLAGVA VLAAGWPLHT IAWTQPVGKP
ITVRLLQGNV PQDVKFQQTG IDHSLALYTK MVTEQPAQLV VTPETAFPIL LQDMPQEIAL
AIRTYVDTTG SSVLFGAANA DSAVDYTNSA FGVGPWFKGV YRYDKHHLVP FGEFIPFGFH
WFVHMMNMPL GDFRRGLPVQ PPMPVAGQRV APNICYEDLF GEEIAASLRQ AERPATMLAN
VTNLAWFGDT IALDQHLQIS RMRALESGRP MLRATNTGAT AVVRPDGSVQ ARLPVFTLGT
LQADVQGMQG LTPFVRTGNA PALGAGVLVL LAALARRRRA GAA
