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Database: UniProt
Entry: A0A1Y5JXK7_9GAMM
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ID   A0A1Y5JXK7_9GAMM        Unreviewed;       517 AA.
AC   A0A1Y5JXK7;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
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   ORFNames=B5G52_19065 {ECO:0000313|EMBL:OUS68567.1};
OS   Pseudoalteromonas sp. A601.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1967839 {ECO:0000313|EMBL:OUS68567.1, ECO:0000313|Proteomes:UP000196208};
RN   [1] {ECO:0000313|EMBL:OUS68567.1, ECO:0000313|Proteomes:UP000196208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A601 {ECO:0000313|EMBL:OUS68567.1,
RC   ECO:0000313|Proteomes:UP000196208};
RA   Cheng Y., Li J.G., Liu H., Han W.J.;
RT   "Draft Genome of a Polysaccharide-Degrading Marine Bacterium
RT   Pseudoalteromonas sp. A601.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the phospholipid dependent N-acylation of the N-
CC       terminal cysteine of apolipoprotein, the last step in lipoprotein
CC       maturation. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01148};
CC   -!- PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl
CC       transfer). {ECO:0000256|HAMAP-Rule:MF_01148}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01148};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01148}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N-
CC       acyltransferase subfamily. {ECO:0000256|ARBA:ARBA00010065,
CC       ECO:0000256|HAMAP-Rule:MF_01148}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OUS68567.1}.
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DR   EMBL; MXQF01000037; OUS68567.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y5JXK7; -.
DR   OrthoDB; 9804277at2; -.
DR   UniPathway; UPA00666; -.
DR   Proteomes; UP000196208; Unassembled WGS sequence.
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; Carbon-nitrogen hydrolase; 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   NCBIfam; TIGR00546; lnt; 1.
DR   PANTHER; PTHR38686; APOLIPOPROTEIN N-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR38686:SF1; APOLIPOPROTEIN N-ACYLTRANSFERASE; 1.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   Pfam; PF20154; LNT_N; 1.
DR   SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW   Rule:MF_01148};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01148}; Lipoprotein {ECO:0000313|EMBL:OUS68567.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01148};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01148};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01148};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01148}.
FT   TRANSMEM        20..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   TRANSMEM        69..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   TRANSMEM        96..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   TRANSMEM        132..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   TRANSMEM        176..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   TRANSMEM        201..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   TRANSMEM        497..515
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   DOMAIN          233..484
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS50263"
SQ   SEQUENCE   517 AA;  57522 MW;  09CD168E74342565 CRC64;
     MKTILTNCLH LAKDKKAWLA LVAGLFLTLS YAPFGIWPLT FICLIVAIYT SHNQQYGKKP
     SKQAAKYGFL FGLGWFGAGI SWVHVSIATF GGMPLAASVL LMVLLCAYLA IYPALAFMFA
     TRFASGAHSY GLLLITGFAV TEYLRGVVLT GFPWLSFGYT QTDSPLNYLA PTLGEFGLTL
     ICIAIAFSFY QLLFNRSLKS TIATAAFIAL ISLIGNISQS PHYNDKTIST LLVQGNIKQH
     LRFEPSEFWT TMSKYQDMTR PHWNADLVVW PEAAVPEIEA LADSFLAGLD SAASFNETAL
     ITGIVDYQLD TKTIFNTLIV LGNKERDDEH GHYQYLGKNR YQKHQLLPIG EFVPFEDILR
     PIAPLFDLPM SSFTRGDEVQ NNLRANGLNI LPAICYEIAF ADLVRGNYHS ESDILFTVSN
     DAWFGASHGP HQHMQIARMR ALELQRPLIR VTNNGISGVY DPVSQTQISM PQFKAETLKV
     NVKLIEGDSI YSQYGNLPVW IVVVLMGFVG VVKRLKL
//
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