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Database: UniProt
Entry: S2WIZ0_9ACTN
LinkDB: S2WIZ0_9ACTN
Original site: S2WIZ0_9ACTN 
ID   S2WIZ0_9ACTN            Unreviewed;       507 AA.
AC   S2WIZ0;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
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=HMPREF9306_01311 {ECO:0000313|EMBL:EPD32612.1};
OS   Propionimicrobium lymphophilum ACS-093-V-SCH5.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Propionimicrobium.
OX   NCBI_TaxID=883161 {ECO:0000313|EMBL:EPD32612.1, ECO:0000313|Proteomes:UP000014417};
RN   [1] {ECO:0000313|EMBL:EPD32612.1, ECO:0000313|Proteomes:UP000014417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-093-V-SCH5 {ECO:0000313|EMBL:EPD32612.1,
RC   ECO:0000313|Proteomes:UP000014417};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA   Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Propionimicrobium lymphophilum ACS-093-V-SCH5.";
RL   Submitted (APR-2013) 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}.
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:EPD32612.1}.
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DR   EMBL; AGZR01000008; EPD32612.1; -; Genomic_DNA.
DR   AlphaFoldDB; S2WIZ0; -.
DR   STRING; 883161.HMPREF9306_01311; -.
DR   PATRIC; fig|883161.3.peg.1305; -.
DR   HOGENOM; CLU_019563_0_1_11; -.
DR   UniPathway; UPA00666; -.
DR   Proteomes; UP000014417; 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:EPD32612.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01148};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014417};
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        6..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   TRANSMEM        46..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   TRANSMEM        103..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   TRANSMEM        141..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT   DOMAIN          210..468
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS50263"
SQ   SEQUENCE   507 AA;  55218 MW;  366B94B363361E01 CRC64;
     MLVTALFGFC FGLIASLGFV PFGIWPMTIA GLAAFMVFTI RCSGRMSALA GYSFGIGLFG
     VTVSYVSVMG IWIGVALVAV LSLYTAIYGI VQNKIQRFKI WPLLVPAAWV AMEFCWSRFP
     LGGFGWVRLA FTSPDQPIGG LLWLLAASGI GYLIAFCASC LAAMVSKLVL GKHRSVLWLI
     PVSAIFVAGV IGQTFIPSKD GEQQVSVGMV QGDVAGSAGP RALGYARSVT NNHFSETVLL
     LAKARSENIP IDFILWPENS SDHDPTVDVK TEQMVQKTIE LGQSPLFMGA VMEGPGEDER
     QTTSLWYDAD GAIIGRHDKR NAVPFGEYTP FKDLVFKLVP MAKLVGRQTV EGSQPGVLDV
     LINEKPLKVG TIICFELAFD DTIYDLAKKD AQLIVVQSNN STYTGTFQPK QQFQITRVRA
     MELAQPIVVS TTSSFSGHID EHGRVIDRTE EATSASRIYK VPIGTVKTPA VYVGKVVDYL
     CLTVTLLSIG ATVVKRRPRH TKINFHD
//
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