LNT_THEVB
ID LNT_THEVB Reviewed; 506 AA.
AC Q8DIC3;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=tll1667;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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; BA000039; BAC09219.1; -; Genomic_DNA.
DR RefSeq; NP_682457.1; NC_004113.1.
DR RefSeq; WP_011057504.1; NC_004113.1.
DR AlphaFoldDB; Q8DIC3; -.
DR SMR; Q8DIC3; -.
DR STRING; 197221.22295392; -.
DR EnsemblBacteria; BAC09219; BAC09219; BAC09219.
DR KEGG; tel:tll1667; -.
DR PATRIC; fig|197221.4.peg.1748; -.
DR eggNOG; COG0815; Bacteria.
DR OMA; IPQSMKW; -.
DR OrthoDB; 1291198at2; -.
DR UniPathway; UPA00666; -.
DR Proteomes; UP000000440; 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..506
FT /note="Apolipoprotein N-acyltransferase"
FT /id="PRO_0000178099"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 483..500
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT DOMAIN 238..473
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 279
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 336
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 385
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
SQ SEQUENCE 506 AA; 56226 MW; C0650611E3A194BA CRC64;
MWRLPPKSNA NAKVLSRWLL FVGLGIAGWG TQLALPPVSG WFLAFVGIVP LWWQCQVLAP
LWAAIAGLCW GWGFYGSSLV WVWDLHPLTW IGIDPVPSWL ISRGIWLCLS SWGAVLSGSW
ALLMARYGVR RSAPWQLLWG VTLWCALEAL WSHSPLWWIS LSLTQSPGGL VQLGRLAGPT
TITAVVMTVN GLVTLSLRQQ KWARVGLAMT LVAAIALNGV LSVRVMADRG EPLRVGLIQG
NIPTREKLTP EGIRRAWQVY LQGYHQLVSW GVDAVLTPEG ALPILWQPQQ MNPITEAVRE
AGVPLWLGTF METAGGSHQV LLSLDGNGEI DSHYGKVNLV PLGEYIPPWL GGVVQRLSTL
RSPLIPGDPE QVFTTPWGNA VVLICFESAF SHRSRWQLVH GGQFILSVAN DDPYHRQLMT
QHHGHDVLRA VEGDRWLVRC TNTGLSAVIA PTGETLWLSK ADEFVIYAAT IFRRQTETLY
TRYGDWLLPL LLGMLSLSVL RQRGWH
