LNT_PSEAE
ID LNT_PSEAE Reviewed; 511 AA.
AC Q9ZI86;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
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 homolog;
GN Name=lnt {ECO:0000255|HAMAP-Rule:MF_01148}; Synonyms=cutE;
GN OrderedLocusNames=PA3984;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Qi H.-Y., Gupta S.D., Wu H.C., Rick P.D.;
RT "Identification of N-acyltransferase (lnt) gene from Pseudonomas
RT aeruginosa.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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,
CC ECO:0000305}.
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DR EMBL; AF038595; AAC97167.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07371.1; -; Genomic_DNA.
DR PIR; B83148; B83148.
DR RefSeq; NP_252673.1; NC_002516.2.
DR RefSeq; WP_003118259.1; NZ_QZGE01000001.1.
DR PDB; 5N6M; X-ray; 3.10 A; A=1-511.
DR PDBsum; 5N6M; -.
DR AlphaFoldDB; Q9ZI86; -.
DR SMR; Q9ZI86; -.
DR STRING; 287.DR97_3881; -.
DR PaxDb; Q9ZI86; -.
DR PRIDE; Q9ZI86; -.
DR EnsemblBacteria; AAG07371; AAG07371; PA3984.
DR GeneID; 878907; -.
DR KEGG; pae:PA3984; -.
DR PATRIC; fig|208964.12.peg.4176; -.
DR PseudoCAP; PA3984; -.
DR HOGENOM; CLU_019563_3_0_6; -.
DR InParanoid; Q9ZI86; -.
DR OMA; IPQSMKW; -.
DR PhylomeDB; Q9ZI86; -.
DR BioCyc; PAER208964:G1FZ6-4058-MON; -.
DR BRENDA; 2.3.1.269; 5087.
DR UniPathway; UPA00666; -.
DR PHI-base; PHI:3782; -.
DR Proteomes; UP000002438; 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; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..511
FT /note="Apolipoprotein N-acyltransferase"
FT /id="PRO_0000178084"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT DOMAIN 230..470
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 269
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 330
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 382
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:5N6M"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:5N6M"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:5N6M"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:5N6M"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:5N6M"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:5N6M"
FT HELIX 51..69
FT /evidence="ECO:0007829|PDB:5N6M"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:5N6M"
FT HELIX 85..99
FT /evidence="ECO:0007829|PDB:5N6M"
FT HELIX 101..113
FT /evidence="ECO:0007829|PDB:5N6M"
FT TURN 117..121
FT /evidence="ECO:0007829|PDB:5N6M"
FT HELIX 122..138
FT /evidence="ECO:0007829|PDB:5N6M"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:5N6M"
FT HELIX 150..154
FT /evidence="ECO:0007829|PDB:5N6M"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:5N6M"
FT HELIX 163..184
FT /evidence="ECO:0007829|PDB:5N6M"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:5N6M"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:5N6M"
FT HELIX 192..211
FT /evidence="ECO:0007829|PDB:5N6M"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:5N6M"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:5N6M"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:5N6M"
FT HELIX 245..256
FT /evidence="ECO:0007829|PDB:5N6M"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:5N6M"
FT TURN 276..279
FT /evidence="ECO:0007829|PDB:5N6M"
FT HELIX 280..292
FT /evidence="ECO:0007829|PDB:5N6M"
FT STRAND 296..306
FT /evidence="ECO:0007829|PDB:5N6M"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:5N6M"
FT STRAND 312..325
FT /evidence="ECO:0007829|PDB:5N6M"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:5N6M"
FT TURN 335..338
FT /evidence="ECO:0007829|PDB:5N6M"
FT HELIX 343..346
FT /evidence="ECO:0007829|PDB:5N6M"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:5N6M"
FT STRAND 375..381
FT /evidence="ECO:0007829|PDB:5N6M"
FT HELIX 382..386
FT /evidence="ECO:0007829|PDB:5N6M"
FT HELIX 388..395
FT /evidence="ECO:0007829|PDB:5N6M"
FT STRAND 399..405
FT /evidence="ECO:0007829|PDB:5N6M"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:5N6M"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:5N6M"
FT HELIX 415..430
FT /evidence="ECO:0007829|PDB:5N6M"
FT STRAND 434..441
FT /evidence="ECO:0007829|PDB:5N6M"
FT STRAND 443..446
FT /evidence="ECO:0007829|PDB:5N6M"
FT STRAND 452..456
FT /evidence="ECO:0007829|PDB:5N6M"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:5N6M"
FT STRAND 463..468
FT /evidence="ECO:0007829|PDB:5N6M"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:5N6M"
FT HELIX 476..479
FT /evidence="ECO:0007829|PDB:5N6M"
FT HELIX 483..502
FT /evidence="ECO:0007829|PDB:5N6M"
SQ SEQUENCE 511 AA; 56017 MW; 9DAE98422EBF8B35 CRC64;
MRWISRPGWP GHLLALAAGA LTPLALAPFD YWPLAILSIA LLYLGLRGLP GKSALWRGWW
YGFGAFGAGT SWIYVSIHDY GAASVPLASL LMLGFTAGVA FFFALPAWLW ARCLRRDNAP
LGDALAFAAL WLALELFRSW FLTGFPWLYA GYSQLQGPLA GLVPVGGVWL SSFVIALSAA
LLVNLPRLFP HGASLLLGLV LLLGPWAAGL YLKGHAWTHS AGEPLRVVAI QGNIAQELKW
DPNQVRAQLD LYRDLSLPQQ DVDLIVWPET AVPILQDMAS GYLGAMGQVA DEKNAALITG
VPVRERLADG KSRYFNGITV VGEGAGTYLK QKLVPFGEYV PLQDLLRGLI AFFDLPMSDF
ARGPADQPLL KAKGYQIAPY ICYEVVYPEF AAALAAQSQV LLTVSNDTWF GTSIGPLQHL
QMAQMRALES GRWMIRATNN GVTGLIDPYG RIVRQIPQFQ QGILRGEVIP MQGLTPYLQY
RVWPLAGLAG VLLLWALLGR QLRPQERRLF G
