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LNT_BORPE
ID   LNT_BORPE               Reviewed;         547 AA.
AC   P61034;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Putative apolipoprotein N-acyltransferase;
DE            Short=ALP N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_01148};
DE            EC=2.3.1.269 {ECO:0000255|HAMAP-Rule:MF_01148};
GN   Name=lnt {ECO:0000255|HAMAP-Rule:MF_01148}; OrderedLocusNames=BP1037;
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- FUNCTION: Catalyzes the phospholipid dependent N-acylation of the N-
CC       terminal cysteine of apolipoprotein, the last step in lipoprotein
CC       maturation. {ECO:0000255|HAMAP-Rule:MF_01148}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-
CC         cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) +
CC         N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein];
CC         Xref=Rhea:RHEA:48228, Rhea:RHEA-COMP:14681, Rhea:RHEA-COMP:14684,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:136912, ChEBI:CHEBI:140656,
CC         ChEBI:CHEBI:140657, ChEBI:CHEBI:140660; EC=2.3.1.269;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01148};
CC   -!- PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl
CC       transfer). {ECO:0000255|HAMAP-Rule:MF_01148}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01148}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01148}.
CC   -!- SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N-
CC       acyltransferase subfamily. {ECO:0000255|HAMAP-Rule:MF_01148,
CC       ECO:0000305}.
CC   -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BX640414; Type=Frameshift; Note=This may be a natural frameshift.; Evidence={ECO:0000305};
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DR   EMBL; BX640414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P61034; -.
DR   SMR; P61034; -.
DR   UniPathway; UPA00666; -.
DR   Proteomes; UP000002676; 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   InterPro; IPR045378; LNT_N.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   Pfam; PF20154; LNT_N; 1.
DR   SUPFAM; SSF56317; SSF56317; 1.
DR   TIGRFAMs; TIGR00546; lnt; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
PE   5: Uncertain;
KW   Acyltransferase; Cell inner membrane; Cell membrane; Membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..547
FT                   /note="Putative apolipoprotein N-acyltransferase"
FT                   /id="PRO_0000178048"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   DOMAIN          248..511
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   ACT_SITE        292
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   ACT_SITE        366
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   ACT_SITE        416
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
SQ   SEQUENCE   547 AA;  58475 MW;  5D2FA58F307034B2 CRC64;
     MSPAGKGPAW RQPAILAAAG AAHALSFAPD PLPAWSLAPV QVIALAVAAH ASLQAPSARR
     ALARGWLFAM FSFSLGLYWM YVSMHDYGGL AAPLAAAGVL ALSAFLALFP GLACAAARWL
     CPPHWDASPP ARARRTLYTA ATWAACWAAL EWLRAVVLTG FPWLNISYAH VDSPLAGWAP
     LLGVHGMALL AAFAAAALAG LWQSASGRID SRQALAAGVA LLLAGAGWLL GQFSWSRPEG
     KPLHLRLVQG NVEQSQKFDP ALLETGLRRH LELASLPPRP GEPKPDMIIL PETVLPVFQD
     QLPASVWDAW IEVARRADTR IAMGVPLHTQ PDGATGHRYT NSVIGFDAST PVEQLRTGTT
     AMRYDKQHLV PWGEYVPPGF RWFVDMLDIP LGDFDRGAAR QPSFDIAGQR IAFNICYEDL
     FGPELLPALQ DGPDGRPGAT IMANVSNLGW FGNTWALRQH LQIGRLRTME TARPMVAATN
     TGITAAIDAR GRVAAALPAD RAGVLPVAVQ GMTGLTPYAR FGDKPALALI GLLLIAAAAR
     GRRPRQP
 
 
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