ID I3IJ73_9BACT Unreviewed; 531 AA.
AC I3IJ73;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=KSU1_C0172 {ECO:0000313|EMBL:GAB61768.1};
OS Candidatus Jettenia caeni.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Brocadiaceae; Candidatus Jettenia.
OX NCBI_TaxID=247490 {ECO:0000313|EMBL:GAB61768.1, ECO:0000313|Proteomes:UP000002985};
RN [1] {ECO:0000313|EMBL:GAB61768.1, ECO:0000313|Proteomes:UP000002985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22673575; DOI=10.1016/j.febslet.2012.04.041;
RA Hira D., Toh H., Migita C.T., Okubo H., Nishiyama T., Hattori M.,
RA Furukawa K., Fujii T.;
RT "Anammox organism KSU-1 expresses a NirK-type copper-containing nitrite
RT reductase instead of a NirS-type with cytochrome cd1.";
RL FEBS Lett. 586:1658-1663(2012).
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:GAB61768.1}.
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DR EMBL; BAFH01000003; GAB61768.1; -; Genomic_DNA.
DR AlphaFoldDB; I3IJ73; -.
DR STRING; 247490.KSU1_C0172; -.
DR eggNOG; COG0815; Bacteria.
DR UniPathway; UPA00666; -.
DR Proteomes; UP000002985; 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:GAB61768.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01148};
KW Reference proteome {ECO:0000313|Proteomes:UP000002985};
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..43
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 50..69
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 107..133
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 153..176
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 188..214
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT DOMAIN 228..493
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
SQ SEQUENCE 531 AA; 60650 MW; 520FE3952671CB6B CRC64;
MHTTNFLKVF ILSFLTIILL CLSFPPADLG YLAWIAFVPW FILIRTEEKY VYLSALFTGA
AFFFIQLSWL RHVTIIAWVL LSLYCSAYFV LFTLCTRFII VKLRLPLVIV APCLWAALEF
IRSFFLSGFP WFFIGHTQYT YLPLIQISDI AGVYGVSFII ITVNACIADF IIYRFIKRNE
IIPFPDRKFL FFGLIGIFPF VLLAATVFYG LYWLKNYKPQ EGPVVCMVQG NIPQDLKFEP
TEEDQIDILK KYSGLSMSMK GKVIDLLVWP ETMAPGLLNI DPKLTGRKID MLSQITAMQL
AQDLNTNLLL GAIALILDGK EQRYFNSAYY YSKEGKFIDR YDKIHLVPFG EFTPLKEYFP
FLAGMVPYEI GLTHGQRRVL FRLDTGKNGC FTFGSSICYE DTVPSLIRKF KMDGADFMLN
ITNDGWFRNS AELDQHLAIM VFRAVENRIC MARAANTGIS SFVAPDGTIY AKLTDQKGRY
REISGTLTDS IKLIEKQNTI YTNCGDWFSI LCTTASGIML LLSPFKKTLS P
//
