ID LNT_SYNY3 Reviewed; 519 AA. AC P74055; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 138. 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=slr0819; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae; OC Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). 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 ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000022; BAA18131.1; -; Genomic_DNA. DR PIR; S75570; S75570. DR AlphaFoldDB; P74055; -. DR SMR; P74055; -. DR STRING; 1148.gene:10499003; -. DR PaxDb; 1148-1653215; -. DR EnsemblBacteria; BAA18131; BAA18131; BAA18131. DR KEGG; syn:slr0819; -. DR eggNOG; COG0815; Bacteria. DR InParanoid; P74055; -. DR PhylomeDB; P74055; -. DR UniPathway; UPA00666; -. DR Proteomes; UP000001425; Chromosome. 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; Carbon-nitrogen hydrolase; 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 NCBIfam; TIGR00546; lnt; 1. DR PANTHER; PTHR38686; APOLIPOPROTEIN N-ACYLTRANSFERASE; 1. DR PANTHER; PTHR38686:SF1; APOLIPOPROTEIN N-ACYLTRANSFERASE; 1. DR Pfam; PF00795; CN_hydrolase; 1. DR Pfam; PF20154; LNT_N; 1. DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 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..519 FT /note="Apolipoprotein N-acyltransferase" FT /id="PRO_0000178101" FT TRANSMEM 6..26 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148" FT TRANSMEM 47..67 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148" FT TRANSMEM 83..103 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148" FT TRANSMEM 126..146 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148" FT TRANSMEM 174..194 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148" FT TRANSMEM 206..226 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148" FT TRANSMEM 496..516 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148" FT DOMAIN 244..482 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 343 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148" FT ACT_SITE 394 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148" SQ SEQUENCE 519 AA; 58131 MW; A28C75F260EF8BA3 CRC64; MGLATAPLGW TYVAWFGQIP LWIWIFRANT TRLNFTQLKQ FLISRSLTAI AWGGGFYGVA LFWITGVHPL TWLGVPWLAS LAIAAFCWLA ITAWGVVLVF VWLLAMAVWE VTTARTKVNS TFKKYLFILW GTASWCGLET LWSHSILWWS PVAYTQSPSQ LHFLQWGAIG GPALLSAFIV AVNGFLALGL IDFLDGKTVN KNKQNWHYFL IAILIWLFCQ GGGWLLYQKP LADTPEEKIN VGIIQGNIPN QIKFNSEGWQ RAIAGYTEGY KKLTEQGAEI VLTPEGALPY LWETVVAKSG FYQAILQTQV PVWLGAYGTK GDGYTNSLLT VDGQGKLLGR YDKFKLVPLG EYIPLSNVFG QLIQRLSPLK EQLLPGDRPQ VLPTPFGPAA VVICYESAFP DLLRSQLLQG GEFILSSANN AHYSDTMAAQ HHALDVMRAI EGDRWLARAT NTGLSAIINP RGKTLWLSAM NQYEIHAAPI YRRRGLILYS RWGDWVVFLL LVVSAIAWLY QIVFPLNQR //