LNT2_TREPA
ID LNT2_TREPA Reviewed; 559 AA.
AC O83432;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 23-FEB-2022, entry version 114.
DE RecName: Full=Apolipoprotein N-acyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_01148};
DE Short=ALP N-acyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_01148};
DE EC=2.3.1.269 {ECO:0000255|HAMAP-Rule:MF_01148};
GN Name=lnt2 {ECO:0000255|HAMAP-Rule:MF_01148}; OrderedLocusNames=TP_0417;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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; AE000520; AAC65404.1; -; Genomic_DNA.
DR PIR; G71327; G71327.
DR RefSeq; WP_010881865.1; NC_000919.1.
DR STRING; 243276.TPANIC_0417; -.
DR PRIDE; O83432; -.
DR EnsemblBacteria; AAC65404; AAC65404; TP_0417.
DR KEGG; tpa:TP_0417; -.
DR eggNOG; COG0815; Bacteria.
DR HOGENOM; CLU_019563_1_1_12; -.
DR OMA; YVALVPW; -.
DR UniPathway; UPA00666; -.
DR Proteomes; UP000000811; 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..559
FT /note="Apolipoprotein N-acyltransferase 2"
FT /id="PRO_0000178106"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT DOMAIN 221..507
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 288
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 358
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 416
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
SQ SEQUENCE 559 AA; 61262 MW; ADE09DF055713F7E CRC64;
MLCTAPLVSS AASAVLLAFA IPNEFWLAGS SVLGLGALVP LYVGFLLSPA KKHVACSYGL
FVALVHACSS FWLKNFQGFA LFTLGASTVG YFFYALPFGV AFACILRKQA PARACAFALV
WTLWEWVKST GILAYPWGTV PMTAHSLSHL IQIADITGVW GLSFLIPLAN ACVAESLHFF
IKKRDSVPVF RLWLLTGCLY CLCSLYGAYR IATLGAPRTT LALAIVQQNA DPWDTXSFEK
NLTTAIHLTE TALRTQTAPP LPTTPYRKEK TLTHASARAP VDMVVWSESS LRYPYEQYRH
VYNALPAARP FSAFLRTLGA PLLVGTPLRL SGNSTKGGYA NAVALLRPDG HVAQVYGKMQ
MVPFAEFIPW GHMTSVQRLA QMLAGFSESW TPGPGPRLFH VPCAAGGSVR FATPICYEDA
FPSLCAALHT QGSELLINLT NDSWSKTASA EWQHYVVSLF RAIELRTTLV RSTNSGYTVV
IGPEGKTRAA FPLFQATSAV LHVPVYPVVR TYYARMRDWV IVLCALIFFA EGVRMAVHTR
RHSTTQAESS LQQIRGEHV
