(data stored in ACNUC7421 zone)

HOGENOM: SHIF2_1_PE644

ID   SHIF2_1_PE644                        STANDARD;      PRT;   512 AA.
AC   SHIF2_1_PE644; D2A9Y8;
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; (SHIF2_1.PE644).
GN   OrderedLocusNames=SFxv_0691;
OS   SHIGELLA FLEXNERI 2002017.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=591020;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SHIF2_1.PE644.
CC       Shigella flexneri (serovar X, strain 2002017) chromosome, complete
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:D2A9Y8_SHIF2
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; D2A9Y8; -.
DR   EMBL; CP001383; ADA72993.1; -; Genomic_DNA.
DR   ProteinModelPortal; D2A9Y8; -.
DR   EnsemblBacteria; EBESCT00000204841; EBESCP00000190708; EBESCG00000200724.
DR   GenomeReviews; CP001383_GR; SFxv_0691.
DR   GeneTree; EBGT00050000010323; -.
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; SHIF2_1.PE644; -.
KW   ADA72993.1cccc7236820036002503210000011;
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;
     MDFASLIERQ RIRLLLALLF GACGTLAFSP YDVWPAAIIS LMGLQALTFN RRPLQSAAIG
     FCWGFGLFGS GINWVYVSIA TFGGMPGPVN IFLVVLLAAY LSLYTGLFAG VLSRLWPKTT
     WLRVAIATPA LWQVTEFLRG WVLTGFPWLQ FGYSQIDGPL KGLAPLMGVE AINFLLMMVS
     GLLALALVKR NWRPLVVAVV LFALPFPLRY IQWFTPQPEK TIQVSMVQGD IPQSLKWDEG
     QLLNTLKIYY NATAPLMGKS SLIIWPESAI TDLEINQQPF LKALDGELRD KGSSLVTGIV
     DARLNKQNRY DTYNTIITLG KGAPYSYESA DRYNKNHLVP FGEFVPLESI LRPLAPFFDL
     PMSSFSRGPY IQPPLSANGI ELTAAICYEI ILAEQVRDNF RPDTDYLLTI SNDAWFGKSI
     GPWQHFQMAR MRALELARPL LRSTNNGITA VIGPQGEIQA MIPQFAREVL TTNVTPTTGL
     TPYARTGNWP LWVLTALFGF AAVLMSLRQR RK
//

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