(data stored in SCRATCH zone)

SWISSPROT: Q0SKF4_RHOJR

ID   Q0SKF4_RHOJR            Unreviewed;       567 AA.
AC   Q0SKF4;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   07-JUN-2017, entry version 91.
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.- {ECO:0000256|HAMAP-Rule:MF_01148};
GN   Name=lnt {ECO:0000256|HAMAP-Rule:MF_01148};
GN   OrderedLocusNames=RHA1_ro00146 {ECO:0000313|EMBL:ABG91982.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG91982.1, ECO:0000313|Proteomes:UP000008710};
RN   [1] {ECO:0000313|Proteomes:UP000008710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M.,
RA   Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D.,
RA   Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M.,
RA   Schein J.E., Shin H., Smailus D., Siddiqui A.S., Marra M.A.,
RA   Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M.,
RA   Davies J.E., Mohn W.W., Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC   -!- FUNCTION: Transfers the fatty acyl group on membrane lipoproteins.
CC       {ECO:0000256|HAMAP-Rule:MF_01148}.
CC   -!- PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl
CC       transfer). {ECO:0000256|HAMAP-Rule:MF_01148,
CC       ECO:0000256|SAAS:SAAS00088954}.
CC   -!- SUBCELLULAR LOCATION: Cell 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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000431; ABG91982.1; -; Genomic_DNA.
DR   RefSeq; WP_011593465.1; NC_008268.1.
DR   ProteinModelPortal; Q0SKF4; -.
DR   STRING; 101510.RHA1_ro00146; -.
DR   PRIDE; Q0SKF4; -.
DR   EnsemblBacteria; ABG91982; ABG91982; RHA1_ro00146.
DR   GeneID; 4217585; -.
DR   KEGG; rha:RHA1_ro00146; -.
DR   PATRIC; fig|101510.16.peg.172; -.
DR   eggNOG; ENOG4107R05; Bacteria.
DR   eggNOG; COG0815; LUCA.
DR   HOGENOM; HOG000021324; -.
DR   KO; K03820; -.
DR   OMA; PIGEFVP; -.
DR   OrthoDB; POG091H05IH; -.
DR   BioCyc; RJOS101510:GJJ1-146-MONOMER; -.
DR   UniPathway; UPA00666; -.
DR   Proteomes; UP000008710; 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:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0016410; F:N-acyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:UniProtKB-HAMAP.
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   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; Q0SKF4.
DR   SWISS-2DPAGE; Q0SKF4.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00088951, ECO:0000313|EMBL:ABG91982.1};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00088945};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008710};
KW   Lipoprotein {ECO:0000313|EMBL:ABG91982.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00100885};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00088948, ECO:0000313|EMBL:ABG91982.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00088943};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00088952}.
FT   TRANSMEM     16     34       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   TRANSMEM     40     61       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   TRANSMEM     68     86       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   TRANSMEM     92    115       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   TRANSMEM    122    138       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   TRANSMEM    158    191       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   TRANSMEM    203    221       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   TRANSMEM    496    517       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   DOMAIN      234    525       CN hydrolase. {ECO:0000259|PROSITE:
FT                                PS50263}.
SQ   SEQUENCE   567 AA;  59366 MW;  A0649DC5B89CA933 CRC64;
     MSGSTTPRWT IGKLGVLVRS VLSVAAGFLV FAGFPPRPLW FLAPIGIALL TLILTGAGGA
     APRLRAGFGY GYLAGLGFLV PLLPWIGVFV GALPWLALAA VESLYIGLFG VLAVLVSRLR
     WAPLWIAACW SLTEWLRASV PFGGFPWGRL AFGQSEGWFL PLASIGGAPL LSFAVALTGA
     GLASVAVTVR ARASGATNWT RPLAGGLVAA LAATVVSLAL WPTPPGMDSG DRTITVAAIQ
     GSVPKLGLDF NDQRKRVLDN HVNRTLELAD DVASGAAPQP DLVVWPENAS DIDPLRNADA
     AADISRASEA IGAPILVGAV LVNSDRTTTN SVIVWDGDAG PQEQHDKKII QPFGEYLPYR
     GFFRHFSAYA DRAGNFVPGD GDGVVHADGI AVGVATCYEV AFDRAFEQSV RSGAELLAVP
     TNNATFGDTE MTYQQLAMSQ VRAVEHGRAV VVAATSGVSA IISPDGSTAA ETSLFVPAAL
     VSQVPLRTGT TLASRLGPIP EVLLCVGAVA AVAFAVVQRR RTVRTLIQRS TEKAPAVAGR
     EDPHGIGDRF RAERGTERTD SGDHSDV
//

If you have problems or comments...

PBIL Back to PBIL home page