LNT_HELHP
ID LNT_HELHP Reviewed; 400 AA.
AC Q7VFP7;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 98.
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=HH_1628;
OS Helicobacter hepaticus (strain ATCC 51449 / 3B1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=235279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51449 / 3B1;
RX PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M.,
RA Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R.,
RA Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.,
RA Shen Z., Weber J., Frosch M., Fox J.G.;
RT "The complete genome sequence of the carcinogenic bacterium Helicobacter
RT hepaticus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(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}.
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DR EMBL; AE017125; AAP78225.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7VFP7; -.
DR SMR; Q7VFP7; -.
DR STRING; 235279.HH_1628; -.
DR EnsemblBacteria; AAP78225; AAP78225; HH_1628.
DR KEGG; hhe:HH_1628; -.
DR eggNOG; COG0815; Bacteria.
DR HOGENOM; CLU_050649_0_0_7; -.
DR OMA; HPFGFDW; -.
DR UniPathway; UPA00666; -.
DR Proteomes; UP000002495; 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 Pfam; PF00795; CN_hydrolase; 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..400
FT /note="Apolipoprotein N-acyltransferase"
FT /id="PRO_0000178069"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 67..87
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 123..143
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT DOMAIN 181..400
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 222
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 283
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 332
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
SQ SEQUENCE 400 AA; 45856 MW; 941A293EDC2265C4 CRC64;
MLPFYAQWVL ESYDKAISPL LVSLLGLFSI ASVLFVPKNR RFGVGFFIGM LWFYWISLGL
RYFDMSFLIP LVVIACGIFM GFVFYIGLWC ECLIVRFAFL LLLSYLTPFG FDWIVPESVF
AYSYIGVDKL SFALSILALW ILFKYKTWWK LGGVICLVFA LDFGLKDSKI QNLPPLKIKL
AQSAVSQDFD YRMREAKSIF SEHISDIQKA INEEYDVIIL PESAFYVPLD SQYFPYFDSL
LEMSHKIVII VGALREEIHT DGRASYFNST YKFDKGKVSF YDKVHLVPFG ETLPSFLLPL
VNTFFQGIGG FSAGKDFGYF DIAEIKFKNA ICYEGSNRGF YADYPQYVIV TSNNAWFVPS
IEPILQKNLM KYYARLYGSV IFHATNLSPA AIITPFVSSR
