(data stored in ACNUC7421 zone)

SWISSPROT: LNT_ECO57

ID   LNT_ECO57               Reviewed;         512 AA.
AC   Q8XBK2;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   05-JUL-2017, entry version 91.
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.- {ECO:0000255|HAMAP-Rule:MF_01148};
DE   AltName: Full=Copper homeostasis protein CutE;
GN   Name=lnt {ECO:0000255|HAMAP-Rule:MF_01148}; Synonyms=cutE;
GN   OrderedLocusNames=Z0806, ECs0695;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Transfers the fatty acyl group on membrane lipoproteins.
CC       {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}.
DR   EMBL; AE005174; AAG54990.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34118.1; -; Genomic_DNA.
DR   PIR; B85566; B85566.
DR   PIR; G90715; G90715.
DR   RefSeq; NP_308722.1; NC_002695.1.
DR   RefSeq; WP_000853048.1; NZ_MWVM01000011.1.
DR   ProteinModelPortal; Q8XBK2; -.
DR   STRING; 155864.Z0806; -.
DR   EnsemblBacteria; AAG54990; AAG54990; Z0806.
DR   EnsemblBacteria; BAB34118; BAB34118; BAB34118.
DR   GeneID; 917056; -.
DR   KEGG; ece:Z0806; -.
DR   KEGG; ecs:ECs0695; -.
DR   PATRIC; fig|386585.9.peg.809; -.
DR   eggNOG; ENOG4105CE8; Bacteria.
DR   eggNOG; COG0815; LUCA.
DR   HOGENOM; HOG000264279; -.
DR   KO; K03820; -.
DR   UniPathway; UPA00666; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0016410; F:N-acyltransferase activity; IEA:InterPro.
DR   GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:InterPro.
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   Pfam; PF00795; CN_hydrolase; 1.
DR   SUPFAM; SSF56317; SSF56317; 1.
DR   TIGRFAMs; TIGR00546; lnt; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8XBK2.
DR   SWISS-2DPAGE; Q8XBK2.
KW   Acyltransferase; Cell inner membrane; Cell membrane;
KW   Complete proteome; Copper; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    512       Apolipoprotein N-acyltransferase.
FT                                /FTId=PRO_0000178063.
FT   TRANSMEM     12     34       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01148}.
FT   TRANSMEM     54     76       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01148}.
FT   TRANSMEM     89    111       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01148}.
FT   TRANSMEM    166    188       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01148}.
FT   TRANSMEM    195    213       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01148}.
FT   TRANSMEM    489    507       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01148}.
FT   DOMAIN      227    476       CN hydrolase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00054}.
FT   REGION      425    431       Could contain a copper-binding motif.
FT   ACT_SITE    267    267       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00054}.
FT   ACT_SITE    335    335       {ECO:0000255|PROSITE-ProRule:PRU00054}.
FT   ACT_SITE    387    387       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00054}.
SQ   SEQUENCE   512 AA;  57094 MW;  5A592BA2BFADAF3C CRC64;
     MAFASLIERQ RIRLLLALLF GACGTLAFSP YDVWPAAIIS LMGLQALTFN RRPLQSAAIG
     FCWGFGLFGS GINWVYVSIA TFGGMPGPVN IFLVVLLAAY LSLYTGLFAG VLSRLWPKTT
     WLRVAIAAPA LWQVTEFLRG WVLTGFPWLQ FGYSQIDGPL KGLAPLMGVE AINFLLMMVS
     GLLALALVKR NWRPLVVAVV LFALPFPLRY IRWFTPQPEK TIQVSMVQGD IPQSLKWDEG
     QLLNTLKIYY NATAPLMGKS SLIIWPESAI TDLEINQQPF LKALDGELRD KGSSLVTGIV
     DARLNKQNRY DTYNTIITLG KGAPYSYESA DRYNKNHLVP FGEFVPLESI LRPLAPFFDL
     PMSSFSRGPY IQPPLSANGI ELTAAICYEI ILGEQVRDNF RPDTDYLLTI SNDAWFGKSI
     GPWQHFQMAR MRALELARPL LRSTNNGITA VIGPQGEIQA MIPQFTREVL TTNVTPTTGL
     TPYARTGNWP LWVLTALFGF AAVLMSLRQR RK
//

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