LNT_BDEBA
ID LNT_BDEBA Reviewed; 547 AA.
AC P61032;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Apolipoprotein N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_01148};
DE Short=ALP N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_01148};
DE EC=2.3.1.269 {ECO:0000255|HAMAP-Rule:MF_01148};
GN Name=lnt {ECO:0000255|HAMAP-Rule:MF_01148}; OrderedLocusNames=Bd1278;
OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS HD100).
OC Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC Bdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=264462;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX PubMed=14752164; DOI=10.1126/science.1093027;
RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA Schuster S.C.;
RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT genomic perspective.";
RL Science 303:689-692(2004).
CC -!- FUNCTION: Catalyzes the phospholipid dependent N-acylation of the N-
CC terminal cysteine of apolipoprotein, the last step in lipoprotein
CC maturation. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01148};
CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl
CC transfer). {ECO:0000255|HAMAP-Rule:MF_01148}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01148}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01148}.
CC -!- SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N-
CC acyltransferase subfamily. {ECO:0000255|HAMAP-Rule:MF_01148}.
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DR EMBL; BX842649; CAE79175.1; -; Genomic_DNA.
DR RefSeq; WP_011163777.1; NC_005363.1.
DR AlphaFoldDB; P61032; -.
DR SMR; P61032; -.
DR STRING; 264462.Bd1278; -.
DR EnsemblBacteria; CAE79175; CAE79175; Bd1278.
DR KEGG; bba:Bd1278; -.
DR eggNOG; COG0815; Bacteria.
DR HOGENOM; CLU_019563_1_2_7; -.
DR OMA; IPQSMKW; -.
DR OrthoDB; 1291198at2; -.
DR UniPathway; UPA00666; -.
DR Proteomes; UP000008080; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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 Pfam; PF00795; CN_hydrolase; 1.
DR Pfam; PF20154; LNT_N; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR TIGRFAMs; TIGR00546; lnt; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..547
FT /note="Apolipoprotein N-acyltransferase"
FT /id="PRO_0000178044"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT DOMAIN 247..515
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 294
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 364
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 418
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
SQ SEQUENCE 547 AA; 62574 MW; 742F6C0530A63D83 CRC64;
MDSLTLYVTN TMMKRWFQFF KHKAYDFRWA ILSGILVGTS YIPFPPWALI FCYTPLWIYV
TEESSSVKKS FWAGWVTQFI LTLIGFHWIA YTAHEFGQLP WAVSYLALLL FCAFMHLYIP
VAVAAGTWLR LRFKLSGGQT LFTIALLHAL LERTWPVIFE WHLGYTLIWS KIPMYHLADL
VGFHGLSAVV LLFNAWMGYV WLKQSFVKKA LSHLSLLALT FAALVGWGFW HGKAWNKFDG
ETKATVVQAN IGNLEKIYAE QGRAYQEVIT RKFLDLSFAA MQKYPQTDIL IWPETAFPDY
LDQHLLDRKH AQILISGLQP LSRPLITGAY SKDPKADEKQ DTSTYNALFL VDPLGNNLDK
PYRKTELLAF GEYLPLSEQF PFLLKLLPFV SNFGRGHGPE VMKWDTPQGS VRWGGQICYE
GLYPSFTRGL AEKGADILVN VTNDSWFGKT FEPQQHLYMT LARAIEVRRP LVRSTNTGVS
TAVLANGDVL QKSPLHEEWS GQFVIKYLKN APLTFFVQWG HWDWIVILLV LGAVIGRGAL
NARSRRS
