ID LNT_HAEIN Reviewed; 522 AA. AC P44626; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 123. 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}; Synonyms=cutE; GN OrderedLocusNames=HI_0302; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC21967.1; -; Genomic_DNA. DR PIR; H64060; H64060. DR RefSeq; NP_438469.2; NC_000907.1. DR AlphaFoldDB; P44626; -. DR SMR; P44626; -. DR STRING; 71421.HI_0302; -. DR EnsemblBacteria; AAC21967; AAC21967; HI_0302. DR KEGG; hin:HI_0302; -. DR PATRIC; fig|71421.8.peg.319; -. DR eggNOG; COG0815; Bacteria. DR HOGENOM; CLU_019563_3_0_6; -. DR OrthoDB; 9804277at2; -. DR PhylomeDB; P44626; -. DR UniPathway; UPA00666; -. DR Proteomes; UP000000579; 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..522 FT /note="Apolipoprotein N-acyltransferase" FT /id="PRO_0000178068" FT TRANSMEM 17..37 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148" FT TRANSMEM 61..81 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148" FT TRANSMEM 98..118 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 164..184 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148" FT TRANSMEM 197..217 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148" FT TRANSMEM 495..515 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148" FT DOMAIN 236..483 FT /note="CN hydrolase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148" FT ACT_SITE 276 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148" FT ACT_SITE 342 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 522 AA; 58553 MW; 8D327E5C50053C8F CRC64; MKNLNRILLS IKFMNKYFTY LIAIISGLLG VFAFSPFDYW PLAYVSLLGL LYVAKNPKKS TALLSTFLWA MGFFCFGVSW LNVSIHQFGG ASLGVSYFLV GLLAAYLALY PMLFTYLVHH FKVQSAVIFA VIWTLTEFLR GWIFTGFPWL QFGYTQIDSP FYGIAPIFGV TGLTFFTVWA SAVIFNLVSS LFKTKNLKLV LANALLLIIV GGLSAYSSRI HFVKSVEDKA ISVTLAQGNI EQNLKWDPNY FYSTLAIYQK LITENLGKTD LIILPESALP TLENAITPFF EGLERAAKET KTEIMVGTVF QDTKSGKLLN SIMTAGNPDF PYQPNTQNRY NKHHLVPFGE YVPLESILRP LNSVFNLPMS AFQSGEAVQP SLIAKKRAFS PAICYEIIFG EQVRQNLKQD TDYLLTLSND AWFGDSIGPW QHLQMARMRA LELGKPLIRA TNTGISVFVD AQGKVLAQAP QFIETTLTYK IAPAEGKTPY SVLGNMPLYA LSLLFLLLHS MMAFIRRKMN IL //