(data stored in ACNUC7421 zone)

HOGENOM: NEIM8_1_PE1508

ID   NEIM8_1_PE1508                       STANDARD;      PRT;   512 AA.
AC   NEIM8_1_PE1508; C9X0J9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   SubName: Full=Apolipoprotein N-acyltransferase (NEIM8_1.PE1508) (ALP
DE   N-acyltransferase); EC=2.3.1 -; .
GN   Name=lnt; OrderedLocusNames=NMV_1687;
OS   NEISSERIA MENINGITIDIS 8013.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=604162;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS NEIM8_1.PE1508.
CC       Neisseria meningitidis (serogroup C, strain 8013) chromosome, complete
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:C9X0J9_NEIM8
CC   -!- FUNCTION: Transfers the fatty acyl group on membrane lipoproteins
CC       (By similarity).
CC   -!- PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl
CC       transfer).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein (By similarity).
CC   -!- GENE_FAMILY: HOG000264279 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C9X0J9; -.
DR   EMBL; FM999788; CAX50500.1; -; Genomic_DNA.
DR   ProteinModelPortal; C9X0J9; -.
DR   EnsemblBacteria; EBNEIT00000016655; EBNEIP00000014524; EBNEIG00000016655.
DR   GenomeReviews; FM999788_GR; NMV_1687.
DR   GeneTree; EBGT00050000021680; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0016410; F:N-acyltransferase activity; IEA:HAMAP.
DR   GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:HAMAP.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   HAMAP; MF_01148; Lnt; 1; -.
DR   InterPro; IPR004563; Apolipo_AcylTrfase.
DR   InterPro; IPR003010; Ntlse/CNhydtse.
DR   Gene3D; G3DSA:3.60.110.10; Ntlse/CNhydtse; 1.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   SUPFAM; SSF56317; Ntlse/CNhydtse; 1.
DR   TIGRFAMs; TIGR00546; Lnt; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
DR   HOGENOMDNA; NEIM8_1.PE1508; -.
KW   CAX50500.1010727985old_1320000031;
KW   Apolipoprotein N-acyltransferase ;
KW   Acyltransferase; Cell inner membrane; Cell membrane;
KW   Complete proteome; Lipoprotein; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
SQ   SEQUENCE   512 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MVSKLDKYWQ HPALYWPLLI LFAAATPFTF APYYHFWLMP LIFGAFVRLI ELRPRFAVSS
     AYLFGLTAYT TQFYWIHTAL HDVSGLPDLY AVPLTFLLPA YLALYPALCF WLWKKFTLPR
     GIKIGLVLPI LWTLTEFARE RFLTGFGWGA IGYSQITPDS PLAGFAPLGG IHMVTLATAF
     LGVWLVLASD NTTRSGKRLL PIILIAALLA AGYTARQTDF TRPDGSRSTV ALLQGNIDQT
     LKWREDQVIP TIQKYYEQVG KTTADIVILP ETAIPVMRQN LPENILAKFA EQAQNNGSAL
     AVGISQYTSD GNGYENAVIN LTGYQENNQD GIPYYAKNHL VPFGEYKPLP FLTTPLYKMM
     DMPLSDFRKG GGKQSALLMK NQKIAFNICY EDGFGDELIA AAKDATLLAN ASNMAWYGKS
     NAMYQHLQQS QARAMELGRY MVRATNTGAT AIISPKGNII AQAQPDTETV LEGHIKGYVG
     ETPYMKTGSS WWLMGILTLA ALILFIFRNK EH
//

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