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LNT_AGRFC
ID   LNT_AGRFC               Reviewed;         529 AA.
AC   Q8UID7;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=Atu0360;
GN   ORFNames=AGR_C_629;
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS   (strain C58)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176299;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743193; DOI=10.1126/science.1066804;
RA   Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA   Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA   Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA   Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA   Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA   Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA   Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA   Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA   Gordon M.P., Olson M.V., Nester E.W.;
RT   "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT   C58.";
RL   Science 294:2317-2323(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA   Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA   Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA   Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA   Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
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; AE007869; AAK86177.1; -; Genomic_DNA.
DR   PIR; AH2620; AH2620.
DR   PIR; H97402; H97402.
DR   RefSeq; NP_353392.1; NC_003062.2.
DR   RefSeq; WP_010970842.1; NC_003062.2.
DR   AlphaFoldDB; Q8UID7; -.
DR   SMR; Q8UID7; -.
DR   STRING; 176299.Atu0360; -.
DR   EnsemblBacteria; AAK86177; AAK86177; Atu0360.
DR   KEGG; atu:Atu0360; -.
DR   PATRIC; fig|176299.10.peg.351; -.
DR   eggNOG; COG0815; Bacteria.
DR   HOGENOM; CLU_019563_3_1_5; -.
DR   OMA; YVALVPW; -.
DR   PhylomeDB; Q8UID7; -.
DR   BioCyc; AGRO:ATU0360-MON; -.
DR   UniPathway; UPA00666; -.
DR   Proteomes; UP000000813; Chromosome circular.
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..529
FT                   /note="Apolipoprotein N-acyltransferase"
FT                   /id="PRO_0000178041"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        66..86
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        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        505..525
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   DOMAIN          242..491
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   ACT_SITE        286
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   ACT_SITE        350
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   ACT_SITE        403
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
SQ   SEQUENCE   529 AA;  56501 MW;  C459ECEF52E36D8D CRC64;
     MERLAGRVML AGGMSRAVMA IAAGAVGALA LPPFGFFAAL FFSFTLLVWL VDGCTGKPGG
     GLFSRILPAF GIGWCFGFGY FVAGLWWLGN ALLLEADEFA WALPLAILGL PALLALFYGF
     AVAAANLLWS DGLGRIAALA AAFGVSEWLR SFLATGFPWN AIGYGIMPIP IMMQSAHLLG
     LLSITTLAVF IFASPALIGT KKGMGPGLAL AGLLLAAHFG YGFYRLQTPA ETPADALTVR
     IVQPAIDQSR KMLNTDRAEI FAEHLRLSAL PPGEGKKRPD IIVWPETSVP FILTQNPDAL
     AEIASTLEDG QVLFTGAVRM EDQGAGRPPR YYNSVYAIDS QGEIIGATDK VHLTPFGEYV
     PFEGILREFG IDNVIALPGG FSAASSRTPL TLPSGKTFYP LICYEIIFPG EMTPGLQGAA
     AILNVTNDGW FGDTPGPYQH FLQARVRAVE TGVPVIRGAN TGISAVIDPY GRIIAGLDYG
     RVGILDATLS GGSNDAFTYD THRTYFWLIF SILMIVAVFP ALSFARRQN
 
 
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