(data stored in SCRATCH zone)

SWISSPROT: Q13EL1_RHOPS

ID   Q13EL1_RHOPS            Unreviewed;       536 AA.
AC   Q13EL1;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 92.
DE   RecName: Full=Apolipoprotein N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_01148};
DE            Short=ALP N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_01148};
DE            EC=2.3.1.269 {ECO:0000256|HAMAP-Rule:MF_01148};
GN   Name=lnt {ECO:0000256|HAMAP-Rule:MF_01148};
GN   OrderedLocusNames=RPD_0238 {ECO:0000313|EMBL:ABE37478.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37478.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37478.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37478.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the phospholipid dependent N-acylation of the
CC       N-terminal cysteine of apolipoprotein, the last step in
CC       lipoprotein maturation. {ECO:0000256|HAMAP-Rule:MF_01148,
CC       ECO:0000256|SAAS:SAAS01145534}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a glycerophospholipid + N-terminal S-1,2-diacyl-sn-
CC         glyceryl-L-cysteinyl-[lipoprotein] = a 1-lyso-
CC         glycerophospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-
CC         cysteinyl-[lipoprotein]; Xref=Rhea:RHEA:48228, Rhea:RHEA-
CC         COMP:14681, Rhea:RHEA-COMP:14684, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:136912, ChEBI:CHEBI:140656, ChEBI:CHEBI:140657,
CC         ChEBI:CHEBI:140660; EC=2.3.1.269; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01148, ECO:0000256|SAAS:SAAS01145543};
CC   -!- PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl
CC       transfer). {ECO:0000256|HAMAP-Rule:MF_01148,
CC       ECO:0000256|SAAS:SAAS00957699}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01148}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01148}.
CC   -!- SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N-
CC       acyltransferase subfamily. {ECO:0000256|HAMAP-Rule:MF_01148}.
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DR   EMBL; CP000283; ABE37478.1; -; Genomic_DNA.
DR   RefSeq; WP_011500668.1; NC_007958.1.
DR   STRING; 316057.RPD_0238; -.
DR   EnsemblBacteria; ABE37478; ABE37478; RPD_0238.
DR   KEGG; rpd:RPD_0238; -.
DR   eggNOG; ENOG4105CE8; Bacteria.
DR   eggNOG; COG0815; LUCA.
DR   HOGENOM; HOG000264280; -.
DR   KO; K03820; -.
DR   OMA; PIGEFVP; -.
DR   OrthoDB; 1291198at2; -.
DR   BioCyc; RPAL316057:RPD_RS01205-MONOMER; -.
DR   UniPathway; UPA00666; -.
DR   Proteomes; UP000001818; Chromosome.
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   Pfam; PF00795; CN_hydrolase; 1.
DR   SUPFAM; SSF56317; SSF56317; 1.
DR   TIGRFAMs; TIGR00546; lnt; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13EL1.
DR   SWISS-2DPAGE; Q13EL1.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00957697, ECO:0000313|EMBL:ABE37478.1};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01148};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00957713};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Lipoprotein {ECO:0000313|EMBL:ABE37478.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00957701};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00957686, ECO:0000313|EMBL:ABE37478.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00957708};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00957712}.
FT   TRANSMEM     42     63       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   TRANSMEM     75     95       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   TRANSMEM    101    126       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   TRANSMEM    138    161       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   TRANSMEM    181    200       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   TRANSMEM    212    230       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   DOMAIN      248    501       CN hydrolase. {ECO:0000259|PROSITE:
FT                                PS50263}.
SQ   SEQUENCE   536 AA;  58230 MW;  F630AADD3B4624C9 CRC64;
     MKLPNLPSLV ASSIILAWGW KRAAIAFVAG ALSSLAMAPF NAWPILFVTF PVAVWLIDGA
     GAGRWRGVPA AALSGWWFGF GYFVPGLYWI GYAFLVDAQT FAWLLPVAIC GLPAYLALFT
     ALGFALARLL WARGAMRVLA LAVSLTIGEW LRGHLLTGFP WNAFGYALTE PLALAQSVSL
     IGIWGLTLLA VAIFASPATL FDDGADTRRR WLAPTAALGL LIAMAVYGSV RLQITPTQLV
     EGVRLRIMQP DVQQDRRFNY AAKAEVMQKY LTLSDRSTGP GSTGVRDATL LIWPESAFPF
     FLTREADAMA QIAELLPKGT ILLTGAVRPP EMPPGRRITR AYNSIYAIDH DGSILAVYDK
     LHLVPFGEFL PFQNLMEKIG FVQLTKVQGG FLPGVKRQNI DLPKAPPLLP LICYEAIFPD
     EIEIRGSRPG WILNLTNDGW FGVSTGPYQH LQQARMRAVE QGLPLVRAAN TGISAVIDPV
     GRIVGRLDLG VEGVLDASLP SQIAPTVYAR VGDVPAAVLV ALSMTLVLLR RRAPPR
//

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