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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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
//