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Database: UniProt
Entry: A0A1E5AFW2_9RHOB
LinkDB: A0A1E5AFW2_9RHOB
Original site: A0A1E5AFW2_9RHOB 
ID   A0A1E5AFW2_9RHOB        Unreviewed;       499 AA.
AC   A0A1E5AFW2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=AB838_08270 {ECO:0000313|EMBL:OED48954.1};
OS   Rhodobacteraceae bacterium (ex Bugula neritina AB1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1868286 {ECO:0000313|EMBL:OED48954.1, ECO:0000313|Proteomes:UP000094333};
RN   [1] {ECO:0000313|EMBL:OED48954.1, ECO:0000313|Proteomes:UP000094333}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB1-7 {ECO:0000313|EMBL:OED48954.1};
RX   PubMed=27681823; DOI=10.1038/srep34362;
RA   Miller I.J., Weyna T.R., Vanee N., Fong S., Lim-Fong G.E.;
RT   "Single sample resolution of rare microbial dark matter in a marine
RT   invertebrate metagenome.";
RL   Sci. Rep. 6:34362-34362(2016).
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:OED48954.1}.
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DR   EMBL; MDLF01000058; OED48954.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E5AFW2; -.
DR   STRING; 1868286.AB838_08270; -.
DR   UniPathway; UPA00666; -.
DR   Proteomes; UP000094333; 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:OED48954.1};
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        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   TRANSMEM        37..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   TRANSMEM        60..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   TRANSMEM        93..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   TRANSMEM        130..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   TRANSMEM        165..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   TRANSMEM        195..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   TRANSMEM        475..492
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   DOMAIN          225..466
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS50263"
SQ   SEQUENCE   499 AA;  53215 MW;  25512AC471242A20 CRC64;
     MISIGFRQAG RQLRLAPAAL AFGSGALASL ALAPWHLLPG LPVALAAAGW LVLKAASGRA
     AALAGWLFGL GYFAVGLSWI LEPFQIDPER HAWMAPFALV FLAAGLALFW GLAFGAAARF
     SRGALRIPML VASWALAEFA RAYILTGFPW AAFGQFWIDT PAENLLPWIG PHGLALLTLV
     AFLPLALLRT APAPALLPLG LIVAAALSVP APQQTAQTDK IVRIVQPNAP QDLKWHPDHR
     WRFLRRALAF SAEHPRPDLI VWPETAVPQM LNYAGDTLQI ISEGAGHVPV FLGIQREEGG
     AFYNSAVLLD ADGLPSATYD KAHLVPFGEY VPFGDFLARF GIHGFASRAG AGYAAGPGAQ
     LLDLPIGRAL PLICYEAVFP QDVNAAAARA DMLVQITNDA WFGTRSGPYQ HLVQARMRAL
     EQGLPMIRAA NTGVSAMIAP DGKLTDSLPL GEAGFIDAVL PAPLPPTLYS RTGDWPVFLL
     CLLIAGAGFV LSRGHARRS
//
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