LNT2_LEPIN
ID LNT2_LEPIN Reviewed; 595 AA.
AC Q8EYY4;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 25-MAY-2022, entry version 105.
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=LA_4078;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
RN [2]
RP SEQUENCE REVISION TO 595.
RA Zhong Y., Zheng H.-J., Wang S.-Y., Guo X.-K., Zhao G.-P.;
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN51276.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE010300; AAN51276.2; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_714258.2; NC_004342.2.
DR AlphaFoldDB; Q8EYY4; -.
DR EnsemblBacteria; AAN51276; AAN51276; LA_4078.
DR KEGG; lil:LA_4078; -.
DR PATRIC; fig|189518.3.peg.4041; -.
DR HOGENOM; CLU_019563_3_1_12; -.
DR InParanoid; Q8EYY4; -.
DR OMA; IPQSMKW; -.
DR UniPathway; UPA00666; -.
DR Proteomes; UP000001408; Chromosome I.
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 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..595
FT /note="Apolipoprotein N-acyltransferase 2"
FT /id="PRO_0000178075"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT TRANSMEM 167..187
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 569..589
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT DOMAIN 241..555
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 293
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 372
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT ACT_SITE 463
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
SQ SEQUENCE 595 AA; 69198 MW; 7E8DC64816209F65 CRC64;
MDTLHHRFQQ FQKTIWFNIF CYLWTGIFSF LAFAPVSLTH FVWIAPFGFF WLSLKYHGKY
KKLFFHGLLI GVVFYAISFH WIIHMAITFG NFPYVVAILI LLFAGLLFGL KFPIFMMSFS
FLSGKIGRHS VWVAGFCGLL SELIGPQLFP WYWGNLAAGN IILAQNAEIT GVYGISFLVF
IVSYTLFQSN PWHWKEIIHS KEKRKQYLRF ITLPALLLLT FIVSGIFLFK KWENVKPVKS
LNVLIVQPDA PLSFRDGREI KESIEALMAR IEKLTDEGAV RLGKKPDLIV LPEAGVPFFS
AHKTEITTKV RRMYWDRFDS LMFLLANRYK ANVFFNEIDA GFKGAPSPRN LRYYNNNVLY
DPNGDRRDSY QKKFLLMFGE YMPFDFLYEL SQQTGRFEPG LTHNLIRYYT PRYYTLAEKE
KSPKGRHLGW TDTETFNHEA VRSYYETTRT EVSETGKFLP LICYEVILPE FVREFRTAGN
PEFIVNLTND KWYGATTESD QHMELGRLRS IELRRWMVRS TNSGISANID HLGRFVGNKK
TGLMTAEALS ETIDVIDSPP TFYTQYGNLI PWLMLFLTGI YYLNLLIGIR RGKSA
