(data stored in ACNUC7421 zone)

HOGENOM: ESCOL5_1_PE2924

ID   ESCOL5_1_PE2924                      STANDARD;      PRT;   512 AA.
AC   ESCOL5_1_PE2924; C6EK38; C5W101;
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;Flags: Precursor;
DE   (ESCOL5_1.PE2924).
GN   Name=lnt; OrderedLocusNames=B21_00616, ECBD_2994, ECD_00625;
OS   ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG'.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=866768;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ESCOL5_1.PE2924.
CC       Escherichia coli BL21-Gold(DE3)pLysS AG chromosome, complete genome.
CC       pEp5, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:C6EK38_ECOBD
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; C6EK38; C5W101; -.
DR   EMBL; CP001665; ACT30005.1; -; Genomic_DNA.
DR   EMBL; CP001509; ACT42501.1; -; Genomic_DNA.
DR   EMBL; AM946981; CAQ31133.2; -; Genomic_DNA.
DR   ProteinModelPortal; C6EK38; -.
DR   STRING; C6EK38; -.
DR   EnsemblBacteria; EBESCT00000156891; EBESCP00000148600; EBESCG00000159501.
DR   EnsemblBacteria; EBESCT00000190523; EBESCP00000176310; EBESCG00000186963.
DR   EnsemblBacteria; EBESCT00000192117; EBESCP00000182270; EBESCG00000191245.
DR   GenomeReviews; AM946981_GR; B21_00616.
DR   GenomeReviews; CP001509_GR; ECD_00625.
DR   GenomeReviews; CP001665_GR; ECBD_2994.
DR   KEGG; ebd:ECBD_2994; -.
DR   GeneTree; EBGT00050000010323; -.
DR   OMA; IAPYICY; -.
DR   ProtClustDB; PRK00302; -.
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; ESCOL5_1.PE2924; -.
KW   apolipoprotein N-acyltransferase;
KW   Acyltransferase; Cell inner membrane; Cell membrane;
KW   Complete proteome; Lipoprotein; Membrane; Signal; Transferase;
KW   Transmembrane; Transmembrane helix.
SQ   SEQUENCE   512 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAFASLIERQ RIRLLLALLF GACGTLAFSP YDVWPAAIIS LMGLQALTFN RRPLQSAAIG
     FGWGFGLFGS GINWVYVSIA TFGGMPGPVN IFLVVLLAAY LSLYTGLFAG VLSRLWPKTT
     WLRVAIAAPA LWQVTEFLRG WVLTGFPWLQ FGYSQIDGPL KGLAPIMGVE AINFLLMMVS
     GLLALALVKR NWRPLVVAVV LFALPFPLRY IQWFTPQPEK TIQVSMVQGD IPQSLKWDEG
     QLLNTLKIYY NATAPLMGKS SLIIWPESAI TDLEINQQPF LKVLDGELRD KGSSLVTGIV
     DARLNKQNRY DTYNTIITLG KGAPYSYESA DRYNKNHLVP FGEFVPLESI LRPLAPFFDL
     PMSSFSRGPY IQPPLSVNGI ELTAAICYEI ILGEQVRDNF RPDTDYLLTI SNDAWFGKSI
     GPWQHFQMAR MRALELARPL LRSTNNGITA VIGPQGEIQA MIPQFTREVL TTNVTPTTGL
     TPYARTGNWP LWVLTALFGF AAVLMSLRAR KR
//

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