ID E1SFT4_PANVC Unreviewed; 507 AA.
AC E1SFT4;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 74.
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 ECO:0000313|EMBL:ADO08715.1};
GN OrderedLocusNames=Pvag_0503 {ECO:0000313|EMBL:ADO08715.1};
OS Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=712898 {ECO:0000313|EMBL:ADO08715.1, ECO:0000313|Proteomes:UP000006631};
RN [1] {ECO:0000313|EMBL:ADO08715.1, ECO:0000313|Proteomes:UP000006631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C9-1 {ECO:0000313|EMBL:ADO08715.1,
RC ECO:0000313|Proteomes:UP000006631};
RX PubMed=20952567; DOI=10.1128/JB.01122-10;
RA Smits T.H., Rezzonico F., Kamber T., Goesmann A., Ishimaru C.A.,
RA Stockwell V.O., Frey J.E., Duffy B.;
RT "The genome sequence of the biocontrol agent Pantoea vagans strain C9-1.";
RL J. Bacteriol. 192:6486-6487(2010).
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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01148}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01148}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002206; ADO08715.1; -; Genomic_DNA.
DR RefSeq; WP_013357110.1; NC_014562.1.
DR AlphaFoldDB; E1SFT4; -.
DR KEGG; pva:Pvag_0503; -.
DR eggNOG; COG0815; Bacteria.
DR HOGENOM; CLU_019563_3_0_6; -.
DR OMA; IPQSMKW; -.
DR OrthoDB; 9804277at2; -.
DR UniPathway; UPA00666; -.
DR Proteomes; UP000006631; Chromosome.
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}; Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01148};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01148}; Lipoprotein {ECO:0000313|EMBL:ADO08715.1};
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..28
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 89..112
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 163..187
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 194..211
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 485..503
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT DOMAIN 227..475
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
SQ SEQUENCE 507 AA; 56354 MW; 720E70FF0667477A CRC64;
MALASLYPRQ RVRLLLALIT GALGTLAFSP YDFWPAALLS LCGLQLLTLN RSSPQATAIG
FVWGVGLFGS GINWVYVSVA TFGGMPGPVN VFIVALLAAY LSIYPALFAG VLNRIWPRTT
LWRLALAAPA LWQMTEFLRG WVLTGFPWLQ FGYSQIDGPL KGLAPLAGVE TLTFLLMVIA
GLLAYALQQR NVRSLVAALL LLALPWPLRY IQWVQPMPER AVEVALVQGN IPQSMKWDPQ
QLLTTLRIYN GLSQPLMGKA PIIIWPESAI TDLESNQQPF LRSLDDELRE RGSSLVTGIV
DSRLEQNRYH DYNTVIVLGG KTPYNYFSGN RYQKNHLVPF GEFVPLADLL RPLAPFFDLP
MSAFSRGNYL QPQLSVAGYN LTSAICYEIV LGEQVRANFH PDTNFLLTVS NDAWFGHSIG
PWQHFQMARM RALELGRPLL RSTNNGVTAV VNASGDVEAM LPQFTRDVLT SKVTPTQGET
PYARAGIWPV WSLTLLAALI ALLRRRR
//