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 03-AUG-2022, entry version 110.
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};
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., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA 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., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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}.
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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_SEKU01000009.1.
DR AlphaFoldDB; Q8XBK2; -.
DR SMR; Q8XBK2; -.
DR STRING; 155864.EDL933_0734; -.
DR EnsemblBacteria; AAG54990; AAG54990; Z0806.
DR EnsemblBacteria; BAB34118; BAB34118; ECs_0695.
DR GeneID; 917056; -.
DR KEGG; ece:Z0806; -.
DR KEGG; ecs:ECs_0695; -.
DR PATRIC; fig|386585.9.peg.809; -.
DR eggNOG; COG0815; Bacteria.
DR HOGENOM; CLU_019563_3_0_6; -.
DR OMA; IPQSMKW; -.
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: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 InterPro; IPR045378; LNT_N.
DR Pfam; PF00795; CN_hydrolase; 1.
DR Pfam; PF20154; LNT_N; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR TIGRFAMs; TIGR00546; lnt; 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..512
FT /note="Apolipoprotein N-acyltransferase"
FT /id="PRO_0000178063"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT DOMAIN 227..476
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 267
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 335
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 387
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
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
