LNT_ECOL6
ID LNT_ECOL6 Reviewed; 512 AA.
AC Q8FJY4;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
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, ECO:0000269|PubMed:28698362};
DE AltName: Full=Copper homeostasis protein CutE;
GN Name=lnt {ECO:0000255|HAMAP-Rule:MF_01148}; Synonyms=cutE;
GN OrderedLocusNames=c0742;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN [2] {ECO:0007744|PDB:5VRG, ECO:0007744|PDB:5VRH}
RP X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 2-512 OF WILD-TYPE AND MUTANT
RP SER-387, FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, SUBUNIT,
RP SUBCELLULAR LOCATION, TOPOLOGY, DISRUPTION PHENOTYPE, ACTIVE SITE, AND
RP MUTAGENESIS OF PHE-146; TRP-148; GLN-233; TRP-237; GLU-267; ASN-314;
RP LYS-335; GLU-343; PHE-365; CYS-387; TYR-388; GLU-389; TRP-415 AND PHE-416.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=28698362; DOI=10.1073/pnas.1707813114;
RA Noland C.L., Kattke M.D., Diao J., Gloor S.L., Pantua H., Reichelt M.,
RA Katakam A.K., Yan D., Kang J., Zilberleyb I., Xu M., Kapadia S.B.,
RA Murray J.M.;
RT "Structural insights into lipoprotein N-acylation by Escherichia coli
RT apolipoprotein N-acyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E6044-E6053(2017).
CC -!- FUNCTION: Catalyzes the phospholipid dependent N-acylation of the N-
CC terminal cysteine of apolipoprotein, the last step in lipoprotein
CC maturation. Utilizes a two-step reaction via a ping-pong mechanism. Lnt
CC undergoes covalent modification in the presence of phospholipids,
CC resulting in a thioester acyl-enzyme intermediate. It then transfers
CC the acyl chain to the amine group of the N-terminal diacylglyceryl-
CC modified cysteine of apolipoprotein, leading to the formation of mature
CC triacylated lipoprotein. {ECO:0000269|PubMed:28698362}.
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 ECO:0000269|PubMed:28698362};
CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl
CC transfer). {ECO:0000255|HAMAP-Rule:MF_01148}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:28698362}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01148, ECO:0000269|PubMed:28698362}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000269|PubMed:28698362}.
CC -!- DISRUPTION PHENOTYPE: Essential. Depletion results in increased outer
CC membrane permeability. {ECO:0000269|PubMed:28698362}.
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; AE014075; AAN79215.1; -; Genomic_DNA.
DR RefSeq; WP_000853028.1; NC_004431.1.
DR PDB; 5VRG; X-ray; 2.52 A; A=2-512.
DR PDB; 5VRH; X-ray; 2.14 A; A=2-512.
DR PDBsum; 5VRG; -.
DR PDBsum; 5VRH; -.
DR AlphaFoldDB; Q8FJY4; -.
DR SMR; Q8FJY4; -.
DR STRING; 199310.c0742; -.
DR PRIDE; Q8FJY4; -.
DR EnsemblBacteria; AAN79215; AAN79215; c0742.
DR KEGG; ecc:c0742; -.
DR eggNOG; COG0815; Bacteria.
DR HOGENOM; CLU_019563_3_0_6; -.
DR OMA; IPQSMKW; -.
DR BioCyc; ECOL199310:C0742-MON; -.
DR UniPathway; UPA00666; -.
DR Proteomes; UP000001410; 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 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cell inner membrane; Cell membrane;
KW Membrane; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..512
FT /note="Apolipoprotein N-acyltransferase"
FT /id="PRO_0000178064"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:28698362"
FT TRANSMEM 12..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..33
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:28698362"
FT TRANSMEM 34..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:28698362"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..90
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:28698362"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:28698362"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..167
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:28698362"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:28698362"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..486
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:28698362"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..512
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:28698362"
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 ECO:0000305|PubMed:28698362"
FT ACT_SITE 335
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148,
FT ECO:0000305|PubMed:28698362"
FT ACT_SITE 387
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148,
FT ECO:0000305|PubMed:28698362"
FT MUTAGEN 146
FT /note="F->A: Cannot rescue growth of a lnt mutant."
FT /evidence="ECO:0000269|PubMed:28698362"
FT MUTAGEN 148
FT /note="W->A: Cannot rescue growth of a lnt mutant."
FT /evidence="ECO:0000269|PubMed:28698362"
FT MUTAGEN 233
FT /note="Q->A: Cannot rescue growth of a lnt mutant."
FT /evidence="ECO:0000269|PubMed:28698362"
FT MUTAGEN 237
FT /note="W->A: Cannot rescue growth of a lnt mutant."
FT /evidence="ECO:0000269|PubMed:28698362"
FT MUTAGEN 267
FT /note="E->A: Cannot rescue growth of a lnt mutant."
FT /evidence="ECO:0000269|PubMed:28698362"
FT MUTAGEN 314
FT /note="N->A: Cannot rescue growth of a lnt mutant."
FT /evidence="ECO:0000269|PubMed:28698362"
FT MUTAGEN 335
FT /note="K->A: Cannot rescue growth of a lnt mutant."
FT /evidence="ECO:0000269|PubMed:28698362"
FT MUTAGEN 343
FT /note="E->A: Cannot rescue growth of a lnt mutant."
FT /evidence="ECO:0000269|PubMed:28698362"
FT MUTAGEN 365
FT /note="F->A: Cannot rescue growth of a lnt mutant."
FT /evidence="ECO:0000269|PubMed:28698362"
FT MUTAGEN 387
FT /note="C->A: Cannot rescue growth of a lnt mutant."
FT /evidence="ECO:0000269|PubMed:28698362"
FT MUTAGEN 388
FT /note="Y->A: Cannot rescue growth of a lnt mutant."
FT /evidence="ECO:0000269|PubMed:28698362"
FT MUTAGEN 389
FT /note="E->A: Cannot rescue growth of a lnt mutant."
FT /evidence="ECO:0000269|PubMed:28698362"
FT MUTAGEN 415
FT /note="W->A: Cannot rescue growth of a lnt mutant."
FT /evidence="ECO:0000269|PubMed:28698362"
FT MUTAGEN 416
FT /note="F->A: Cannot rescue growth of a lnt mutant."
FT /evidence="ECO:0000269|PubMed:28698362"
SQ SEQUENCE 512 AA; 57017 MW; A6B784709967EAD3 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 AAVLMSLRAR KH
