(data stored in SCRATCH zone)

SWISSPROT: B8I9M2_METNO

ID   B8I9M2_METNO            Unreviewed;       556 AA.
AC   B8I9M2;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   07-JUN-2017, entry version 67.
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=Mnod_0231 {ECO:0000313|EMBL:ACL55275.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL55275.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL55275.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-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 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; CP001349; ACL55275.1; -; Genomic_DNA.
DR   RefSeq; WP_015926988.1; NC_011894.1.
DR   ProteinModelPortal; B8I9M2; -.
DR   STRING; 460265.Mnod_0231; -.
DR   EnsemblBacteria; ACL55275; ACL55275; Mnod_0231.
DR   KEGG; mno:Mnod_0231; -.
DR   eggNOG; ENOG4105CE8; Bacteria.
DR   eggNOG; COG0815; LUCA.
DR   HOGENOM; HOG000264280; -.
DR   KO; K03820; -.
DR   OMA; PIGEFVP; -.
DR   OrthoDB; POG091H05IH; -.
DR   UniPathway; UPA00666; -.
DR   Proteomes; UP000008207; 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; B8I9M2.
DR   SWISS-2DPAGE; B8I9M2.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00088951, ECO:0000313|EMBL:ACL55275.1};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01148};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00088945};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008207};
KW   Lipoprotein {ECO:0000313|EMBL:ACL55275.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00100885};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008207};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01148,
KW   ECO:0000256|SAAS:SAAS00088948, ECO:0000313|EMBL:ACL55275.1};
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     34     67       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   TRANSMEM     88    111       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   TRANSMEM    117    143       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   TRANSMEM    150    169       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   TRANSMEM    189    214       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   TRANSMEM    226    245       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   TRANSMEM    533    553       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01148}.
FT   DOMAIN      258    555       CN hydrolase. {ECO:0000259|PROSITE:
FT                                PS50263}.
SQ   SEQUENCE   556 AA;  58689 MW;  7F4E8CD6B193CAEF CRC64;
     MRPPDFDAPS FSAPSRLGAV ADRIALASGW QRLALAWLAG ACGALAMPPF GILPALAVAL
     VPAVWLLDGA ATGTGRLRRR LATAGSAAAI GWAWGFGYFV AGLWWLGAAF LVEADQFAVL
     MPLGVLGLPA VLGLFFGLGF ALARLLWSPG WARILALAAG LSAAEWLRGH LFTGFPWNTL
     GMALGQNLWL MQAASVFGLY GLTLLAVLIG AAPATLATGA TPRARWTPPL LALAVLALLA
     GAGAWRIPAG PMPDVPGVRL RLVQANIPQD ARFNPRNRDG ILERYLGLSD SATAPESRGL
     ADVTHLIWPE SSFPFLIQRD PKALAQITAA LPPGKHLVTG AARADEPLPG ERLHFYNGIL
     VIGAEGFVGL PYDKHHLVPF GEYLPGPVDR ILRAVGLRQF VAVPGGFTAA EGARRPFSVP
     GLPPVAASIC YEVIFPGEVV PQVGARPGLI LNLTNDGWFG DTPGPRQHFA QARLRAVEEG
     LPLVRAANTG ISAVADPYGR VTGFLPVGAE GVLDRKLPRN LGESTFYSRF RDLFFAALLL
     GSVLLAIGAR GRIARP
//

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