(data stored in SCRATCH zone)

SWISSPROT: C1AR33_RHOOB

ID   C1AR33_RHOOB            Unreviewed;       567 AA.
AC   C1AR33;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 61.
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=ppm2 {ECO:0000313|EMBL:BAH48510.1};
GN   Synonyms=lnt {ECO:0000256|HAMAP-Rule:MF_01148};
GN   OrderedLocusNames=ROP_02630 {ECO:0000313|EMBL:BAH48510.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48510.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48510.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48510.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; AP011115; BAH48510.1; -; Genomic_DNA.
DR   RefSeq; WP_012687517.1; NC_012522.1.
DR   ProteinModelPortal; C1AR33; -.
DR   STRING; 632772.ROP_02630; -.
DR   EnsemblBacteria; BAH48510; BAH48510; ROP_02630.
DR   KEGG; rop:ROP_02630; -.
DR   PATRIC; fig|632772.20.peg.303; -.
DR   eggNOG; ENOG4107R05; Bacteria.
DR   eggNOG; COG0815; LUCA.
DR   HOGENOM; HOG000021324; -.
DR   KO; K03820; -.
DR   OMA; PIGEFVP; -.
DR   OrthoDB; POG091H05IH; -.
DR   UniPathway; UPA00666; -.
DR   Proteomes; UP000002212; 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; C1AR33.
DR   SWISS-2DPAGE; C1AR33.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00088951, ECO:0000313|EMBL:BAH48510.1};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00088945};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   Lipoprotein {ECO:0000313|EMBL:BAH48510.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00100885};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00088948, ECO:0000313|EMBL:BAH48510.1};
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    187       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   TRANSMEM    199    221       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   DOMAIN      234    526       CN hydrolase. {ECO:0000259|PROSITE:
FT                                PS50263}.
SQ   SEQUENCE   567 AA;  59278 MW;  2188677BDE1DB58F CRC64;
     MSGSATARWT TGKRGVLLRS VLSVAAGFLV FAGFPPRPLW FLAPLGIALL TLILTGAGGA
     APRLRAGFGY AYLAGLGLLV PLLPWIGVFV GALPWLALAA VESLFIGLFG TLAVLVSRLR
     WAPLWIAACW SLTEWLRASV PFGGFPWGRL AFGQSEGWFL PLASIGGSPL LSFAVALTGA
     GLASVAVTVR ARASGAANWA RPLAGGLVAA LAATVASLAL WPTLPDMDSG DRTITVAAIQ
     GSVPKLGLDF NDQRKRVLDN HVNRTLELAD DVASGAAPQP ELVVWPENAS DIDPLRNADA
     GADISRASEA IGAPILVGAV LVNADRTTTN SVIVWDGNSG PQERHDKKII QPFGEYLPYR
     GFFRHFSSYA DRAGNFVPGD GDGVVHANGI AVGVATCYEV AFDRAFEQSV RSGAELLAVP
     TNNATFGDTE MTYQQLAMSK VRAVEHGRAV VVAATSGVSA IIGPDGSTVQ QTPLFVPAAL
     VSQVPLSTGT TLASRLGPIP EVLLCLAAVA AVAFAVVQRR RTDRTPISSS TEKAPAVAGR
     EDPHGIGDRF RAERGTERTD SGDHSDV
//

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