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Database: UniProt
Entry: O51253
LinkDB: O51253
Original site: O51253 
ID   LNT_BORBU               Reviewed;         521 AA.
AC   O51253;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   01-MAY-2013, entry version 78.
DE   RecName: Full=Apolipoprotein N-acyltransferase;
DE            Short=ALP N-acyltransferase;
DE            EC=2.3.1.-;
GN   Name=lnt; OrderedLocusNames=BB_0237;
OS   Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM
OS   4680).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC   Borrelia burgdorferi group.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / B31 / CIP 102532 / DSM 4680;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K.,
RA   Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D.,
RA   Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A.,
RA   Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K.,
RA   Roberts K.M., Hatch B., Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia
RT   burgdorferi.";
RL   Nature 390:580-586(1997).
CC   -!- FUNCTION: Transfers the fatty acyl group on membrane lipoproteins
CC       (By similarity).
CC   -!- PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl
CC       transfer).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N-
CC       acyltransferase subfamily.
CC   -!- SIMILARITY: Contains 1 CN hydrolase domain.
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DR   EMBL; AE000783; AAC66631.1; -; Genomic_DNA.
DR   PIR; E70129; E70129.
DR   RefSeq; NP_212371.1; NC_001318.1.
DR   ProteinModelPortal; O51253; -.
DR   STRING; 224326.BB0237; -.
DR   EnsemblBacteria; AAC66631; AAC66631; BB_0237.
DR   GeneID; 1195074; -.
DR   KEGG; bbu:BB_0237; -.
DR   PATRIC; 20557090; VBIBorBur75917_0636.
DR   eggNOG; COG0815; -.
DR   KO; K03820; -.
DR   OMA; HAFGWIT; -.
DR   ProtClustDB; PRK00302; -.
DR   BioCyc; BBUR224326:BB_0237-MONOMER; -.
DR   UniPathway; UPA00666; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0016410; F:N-acyltransferase activity; IEA:HAMAP.
DR   GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:HAMAP.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
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   Pfam; PF00795; CN_hydrolase; 1.
DR   SUPFAM; SSF56317; Ntlse/CNhydtse; 1.
DR   TIGRFAMs; TIGR00546; lnt; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cell inner membrane; Cell membrane;
KW   Complete proteome; Membrane; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    521       Apolipoprotein N-acyltransferase.
FT                                /FTId=PRO_0000178046.
FT   TRANSMEM      5     22       Helical; (Potential).
FT   TRANSMEM     27     44       Helical; (Potential).
FT   TRANSMEM     56     78       Helical; (Potential).
FT   TRANSMEM     83    105       Helical; (Potential).
FT   TRANSMEM    117    139       Helical; (Potential).
FT   TRANSMEM    154    176       Helical; (Potential).
FT   TRANSMEM    183    202       Helical; (Potential).
FT   DOMAIN      218    514       CN hydrolase.
SQ   SEQUENCE   521 AA;  59737 MW;  9114FCE59B262A14 CRC64;
     MKTRCFCLAA FSGILTTLAI PNEIKETGYS ILGFVAYVPL FIALNKLEDK KALMGLTVFY
     FIIANSLQNF WLGFFHAFGW ITFIGVIIGY IPYSLTLGYF LYYSLKSFKN KTMSITMLFT
     FYDYSRSIGF LAYPWGLAAF TVNNFNNLIQ IADIFGVFFV SFAVYFLNSG IADFLIHKNK
     TNLLNIAFPT LLITASFTYG MIKKIELKNL LAKEIDSLNI AAIQLNTDPW LPGNDKKGIR
     DSIEITEQAL KENPKIEFVI WSEGVLTYPF SKEDQHFKSS DLHNELKNFI KEHKIPFAIG
     APSNLDKAIG IQQNSIYMVE PNLNITNIYS KIFLVPFAEK IPFYEYKFVR NFFLKNFRIL
     GQIEGNKIEI LKLKKFKFAP LICYDDAFPE LSRFYKTQGA NILVNFSNDS WSKTNSAEWQ
     HFVVAKFRSI ENGIKTIRAT NSGITATINE YGETIKKLET FKKGYLLSTV KLSPTFTTIY
     EKIGDSFIHI LVMMFLITTL RFQFMEDKNQ LLSSSVVKIK V
//
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