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Database: UniProt
Entry: I0V7Z5_9PSEU
LinkDB: I0V7Z5_9PSEU
Original site: I0V7Z5_9PSEU 
ID   I0V7Z5_9PSEU            Unreviewed;       535 AA.
AC   I0V7Z5;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 55.
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=SacxiDRAFT_4058 {ECO:0000313|EMBL:EID56248.1};
OS   Saccharomonospora xinjiangensis XJ-54.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharomonospora.
OX   NCBI_TaxID=882086 {ECO:0000313|EMBL:EID56248.1, ECO:0000313|Proteomes:UP000004691};
RN   [1] {ECO:0000313|EMBL:EID56248.1, ECO:0000313|Proteomes:UP000004691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XJ-54 {ECO:0000313|EMBL:EID56248.1,
RC   ECO:0000313|Proteomes:UP000004691};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Brambilla E.-M.,
RA   Klenk H.-P., Woyke T.;
RT   "Improved High-Quality Draft sequence of Saccharomonospora xinjiangensis
RT   XJ-54.";
RL   Submitted (JAN-2012) 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|HAMAP-Rule:MF_01148}.
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DR   EMBL; JH636049; EID56248.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0V7Z5; -.
DR   STRING; 882086.SacxiDRAFT_4058; -.
DR   eggNOG; COG0815; Bacteria.
DR   HOGENOM; CLU_019563_0_1_11; -.
DR   UniPathway; UPA00666; -.
DR   Proteomes; UP000004691; 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:EID56248.1};
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        15..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   TRANSMEM        61..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   TRANSMEM        92..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   TRANSMEM        156..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   TRANSMEM        197..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   TRANSMEM        486..508
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   DOMAIN          228..476
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS50263"
FT   REGION          513..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   535 AA;  56482 MW;  50E306A77C1732B3 CRC64;
     MTAPRPSPLR RGGPLAARIA LAAGSGLLFA AAFAPRPLWW VAPLAIAGLG IALHGRRAWG
     AAGYGLVFGI AFNLVHLVWI QDFLGHEFGP APWLALTGVL SGFLALVCAA MPLVSRLPGA
     PVWQALVFLS QESARMRWPF NGFPWGRVGF SQPEGAYLSL ASLGGAPLVG FAVLVTGFGL
     AQLAVRLRQG GVRFTRAVVA PALAVVLPLV AGLATWPTVG TAAESGTRTV AVVQGNAPDV
     GIGLLGQRDT IRANHFAESE RLLERIRSGE VPRPDVVVWP ETATDVRGGD ARLDELADEF
     GVPLLVGALY QRPGSDLTAN ATLVWEPGEG ITGHYVKREL VPFAEYVPMR EIARWFTPFV
     DDTRDMLWGT EGAALDVAGA QLGTVICYEV AYDYVARDNV AAGAELLVTP TNNAWFGPGE
     MSYQQLAMSR VRAVEHGRAV VVAATSGISA IVAPDGSVTR STSLYTATSM VAEVPLRQET
     TLSDRLGAWT EYALVGAALA AMVAGFVLRS HSKRTTPRAD ATEGEQHGGG DTAHG
//
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