ID I0ALV6_IGNAJ Unreviewed; 551 AA.
AC I0ALV6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
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:AFH49963.1};
GN OrderedLocusNames=IALB_2260 {ECO:0000313|EMBL:AFH49963.1};
OS Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 /
OS Mat9-16).
OC Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC Ignavibacteriaceae; Ignavibacterium.
OX NCBI_TaxID=945713 {ECO:0000313|EMBL:AFH49963.1, ECO:0000313|Proteomes:UP000007394};
RN [1] {ECO:0000313|EMBL:AFH49963.1, ECO:0000313|Proteomes:UP000007394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16
RC {ECO:0000313|Proteomes:UP000007394};
RX PubMed=22661972; DOI=10.3389/fmicb.2012.00185;
RA Liu Z., Frigaard N.-U., Vogl K., Iino T., Ohkuma M., Overmann J.,
RA Bryant D.A.;
RT "Complete genome of Ignavibacterium album, a metabolically versatile,
RT flagellated, facultative anaerobe from the phylum Chlorobi.";
RL Front. Microbiol. 3:185-185(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 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|HAMAP-Rule:MF_01148}.
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DR EMBL; CP003418; AFH49963.1; -; Genomic_DNA.
DR RefSeq; WP_014561112.1; NC_017464.1.
DR AlphaFoldDB; I0ALV6; -.
DR STRING; 945713.IALB_2260; -.
DR GeneID; 78243862; -.
DR KEGG; ial:IALB_2260; -.
DR eggNOG; COG0815; Bacteria.
DR HOGENOM; CLU_019563_1_2_10; -.
DR OrthoDB; 9804277at2; -.
DR UniPathway; UPA00666; -.
DR Proteomes; UP000007394; 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:AFH49963.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01148};
KW Reference proteome {ECO:0000313|Proteomes:UP000007394};
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 43..58
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 70..87
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 99..121
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 133..155
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 167..192
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 204..225
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT TRANSMEM 521..543
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01148"
FT DOMAIN 238..509
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
SQ SEQUENCE 551 AA; 63637 MW; 7AD378FBF3F6C48B CRC64;
MLKVFQRNKL SAEEKSFLRK DRLLLILSGI LTGISFTPFP FPFTLFLFIA FIPYFLVLEK
RKSLLEINRA SYLMFFTLSL ITIYWVGSWQ SKADPFLMIG GGVLIFFYPV VLLINSTLFY
LSQKIFSKEK SFWLFPIIWV TGEYLLTLTD LKFPWLILGH GLAKFTAFIQ IADVVGAFGL
SLIVLYINVL LFKAIKYYSS DRKLFFRYVT ISLLVFMFFF IYGIIKLNRK DEKNEKYLKV
GVVQPNLDPW DKWELGGLDD ILKNYIELSE ECTKLNAKII IWPETALPVY LLSGTYSDIV
DSIYSFLRKN NVYLLTGMPD YIVHYNNPPT DAKLSKSGNF YYSTYNSILL LNPNSYEIQR
YGKMQLVPLG EKVPFVDALP FLANWFKWGV GLSGWNVGKD TTVFKLKIDN DSVRVAGLVC
YESVFPDFVT HFVKKGAQFI TVVTNDSWYG NSSGPYQHKE FAALRAVENR RAVVRSANGG
ISCLINKFGI TEFETKMFTR TSFVVDVPLS DELTFYTKYP FIIPILSSAF SIWIIGINFL
LWLKRKFKFD K
//
