(data stored in ACNUC7421 zone)

SWISSPROT: B7UKU0_ECO27

ID   B7UKU0_ECO27            Unreviewed;       513 AA.
AC   B7UKU0;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 66.
DE   RecName: Full=Apolipoprotein N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_01148};
DE            Short=ALP N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_01148};
DE            EC=2.3.1.269 {ECO:0000256|HAMAP-Rule:MF_01148};
GN   Name=lnt {ECO:0000256|HAMAP-Rule:MF_01148,
GN   ECO:0000313|EMBL:CAS08098.1};
GN   OrderedLocusNames=E2348C_0550 {ECO:0000313|EMBL:CAS08098.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS08098.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS08098.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Catalyzes the phospholipid dependent N-acylation of the
CC       N-terminal cysteine of apolipoprotein, the last step in
CC       lipoprotein maturation. {ECO:0000256|HAMAP-Rule:MF_01148,
CC       ECO:0000256|SAAS:SAAS01145534}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a glycerophospholipid + N-terminal S-1,2-diacyl-sn-
CC         glyceryl-L-cysteinyl-[lipoprotein] = a 1-lyso-
CC         glycerophospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-
CC         cysteinyl-[lipoprotein]; Xref=Rhea:RHEA:48228, Rhea:RHEA-
CC         COMP:14681, Rhea:RHEA-COMP:14684, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:136912, ChEBI:CHEBI:140656, ChEBI:CHEBI:140657,
CC         ChEBI:CHEBI:140660; EC=2.3.1.269; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01148, ECO:0000256|SAAS:SAAS01145543};
CC   -!- PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl
CC       transfer). {ECO:0000256|HAMAP-Rule:MF_01148,
CC       ECO:0000256|SAAS:SAAS00957699}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01148}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01148}.
CC   -!- SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N-
CC       acyltransferase subfamily. {ECO:0000256|HAMAP-Rule:MF_01148}.
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DR   EMBL; FM180568; CAS08098.1; -; Genomic_DNA.
DR   RefSeq; WP_000853029.1; NC_011601.1.
DR   EnsemblBacteria; CAS08098; CAS08098; E2348C_0550.
DR   KEGG; ecg:E2348C_0550; -.
DR   HOGENOM; HOG000264279; -.
DR   KO; K03820; -.
DR   OMA; PIGEFVP; -.
DR   BioCyc; ECOL574521:E2348C_RS02890-MONOMER; -.
DR   UniPathway; UPA00666; -.
DR   Proteomes; UP000008205; 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: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; -; 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   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; B7UKU0.
DR   SWISS-2DPAGE; B7UKU0.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00957697, ECO:0000313|EMBL:CAS08098.1};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01148};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00957713};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Lipoprotein {ECO:0000313|EMBL:CAS08098.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00957701};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00957686, ECO:0000313|EMBL:CAS08098.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00957708};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00957712}.
FT   TRANSMEM     12     28       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   TRANSMEM     57     79       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   TRANSMEM     91    112       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   TRANSMEM    162    188       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   TRANSMEM    195    214       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   TRANSMEM    489    507       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   DOMAIN      227    476       CN hydrolase. {ECO:0000259|PROSITE:
FT                                PS50263}.
SQ   SEQUENCE   513 AA;  57249 MW;  D91470B46B9967EA CRC64;
     MAFASLIERQ RIRLLLALLF GACGTLAFSP YDVWPAAIIS LMGLQALTFN RRPLQSAAIG
     FCWGFGLFGS GINWVYVSIA TFGGMPGPVN IFLVVLLAAY LSLYTGLFAG VLSRLWPKTT
     WLRVAIAAPA LWQVTEFLRG WVLTGFPWLQ FGYSQIDGPL KGLAPIMGVE AINFLLMMVS
     GLLALALVKR NWRPLVVAVV LFALPFPLRY IQWFTPQPEK TIQVSMVQGD IPQSLKWDGD
     QLLNTLKIYY NATAPLMGKS SLIIWPESAI TDLEINQQPF LKALDGELRD KGSSLVTGIV
     DARLNKQNRY DTYNTIITLG KGAPYSYESA DRYNKNHLVP FGEFVPLESI LRPLAPFFDL
     PMSSFSRGPY IQPPLSLNGI QLTAAICYEI ILGEQVRDNF RPDTDYLLTI SNDAWFGKSI
     GPWQHFQMAR MRALELARPL LRSTNNGITA VIGPQGEIQA MIPQFTREVL TTNVTPTTGL
     TPYARTGNWP LWVLTALFGF AAVLMSLRQR RKR
//

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