LNT_RHIE6
ID LNT_RHIE6 Reviewed; 534 AA.
AC B3PZB2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 79.
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};
GN OrderedLocusNames=RHECIAT_CH0000412;
OS Rhizobium etli (strain CIAT 652).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=491916;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIAT 652;
RA Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA Palacios R., Davila G.;
RT "Genome diversity and DNA divergence of Rhizobium etli.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001074; ACE89406.1; -; Genomic_DNA.
DR RefSeq; WP_012482411.1; NC_010994.1.
DR AlphaFoldDB; B3PZB2; -.
DR SMR; B3PZB2; -.
DR EnsemblBacteria; ACE89406; ACE89406; RHECIAT_CH0000412.
DR GeneID; 45955782; -.
DR KEGG; rec:RHECIAT_CH0000412; -.
DR eggNOG; COG0815; Bacteria.
DR HOGENOM; CLU_019563_3_1_5; -.
DR OMA; IPQSMKW; -.
DR UniPathway; UPA00666; -.
DR Proteomes; UP000008817; 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..534
FT /note="Apolipoprotein N-acyltransferase"
FT /id="PRO_1000137481"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 127..147
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 TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT DOMAIN 246..496
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 291
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 408
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
SQ SEQUENCE 534 AA; 57592 MW; C1761346AE71D669 CRC64;
MERLADRVIL VWGFKRSLLA IGAGAFAVLA LPPFGFFAAM FLSFTLLVWL IDGAAASPES
GLIGRLWPAF AVGWLFGFGY FVAGLWWLGH ALLVDSEEFA WALPLAILGL PACLAIFYGL
AVALARIFWS DGMGRIAALA AGFGLMEWLR SVILTGFPWN AIGYGLMPVP LMMQSAHVIG
AMGVTALAVF VFSAPALFGT RQGARTGVAL AVLLFAAHLG YGAYALYLAP RPAPLPEDKR
PVVRLVQPDI DQAAKMDNDA DRNAIFETHL KLSAEAPRNG GRKPNIIVWP ETSIPFILTD
NQDALTRIAD TLDDDQILIA GAVRAEEMGP GTPVRYYNSI YVIDGRGQII AASDKVHLVP
FGEYLPLEEL LTELGIQNVV EVPGGFSAAA SRHLLALPGG LNLYPLICYE IIFPDEMTGD
IKDANALLNL TNDAWFGMTP GPYQHFLQAR VRAVETGLPL IRDANSGISA LVNAHGEIIA
GLDLGETGFI DATVDSLSEG FGSTYPRQTY FWLTEALLIL IALISREGFI FGLN
