(data stored in ACNUC7421 zone)

HOGENOM: SHIFL2_1_PE582

ID   SHIFL2_1_PE582                       STANDARD;      PRT;   512 AA.
AC   SHIFL2_1_PE582; Q820C8;
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   RecName: Full=Apolipoprotein N-acyltransferase; Short=ALP
DE   N-acyltransferase; EC=2.3.1 -;AltName: Full=Copper homeostasis protein
DE   CutE; (SHIFL2_1.PE582).
GN   Name=lnt; Synonyms=cutE; OrderedLocusNames=SF0625, S0647;
OS   SHIGELLA FLEXNERI 2A STR. 2457T.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=198215;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SHIFL2_1.PE582.
CC       Shigella flexneri 2a str. 2457T, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:LNT_SHIFL
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   -!- SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N-
CC       acyltransferase subfamily.
CC   -!- SIMILARITY: Contains 1 CN hydrolase domain.
CC   -!- GENE_FAMILY: HOG000264279 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q820C8; -.
DR   EMBL; AE005674; AAN42262.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16133.1; -; Genomic_DNA.
DR   RefSeq; NP_706555.1; NC_004337.1.
DR   RefSeq; NP_836327.1; NC_004741.1.
DR   ProteinModelPortal; Q820C8; -.
DR   EnsemblBacteria; EBESCT00000086625; EBESCP00000083447; EBESCG00000085670.
DR   EnsemblBacteria; EBESCT00000090236; EBESCP00000086872; EBESCG00000089280.
DR   GeneID; 1023577; -.
DR   GeneID; 1077076; -.
DR   GenomeReviews; AE005674_GR; SF0625.
DR   GenomeReviews; AE014073_GR; S0647.
DR   KEGG; sfl:SF0625; -.
DR   KEGG; sfx:S0647; -.
DR   GeneTree; EBGT00050000010323; -.
DR   OMA; SKEEINV; -.
DR   ProtClustDB; PRK00302; -.
DR   BioCyc; SFLE198214:AAN42262.1-MON; -.
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:InterPro.
DR   GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:InterPro.
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; SHIFL2_1.PE582; -.
KW   apolipoprotein N-acyltransferase;
KW   Acyltransferase; Cell inner membrane; Cell membrane;
KW   Complete proteome; Copper; 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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