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LNT1_TREDE
ID   LNT1_TREDE              Reviewed;         544 AA.
AC   P61037;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Apolipoprotein N-acyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_01148};
DE            Short=ALP N-acyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_01148};
DE            EC=2.3.1.269 {ECO:0000255|HAMAP-Rule:MF_01148};
GN   Name=lnt1 {ECO:0000255|HAMAP-Rule:MF_01148}; OrderedLocusNames=TDE_1708;
OS   Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS   / KCTC 15104).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX   PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA   Seshadri R., Myers G.S.A., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA   Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA   Ren Q., Brinkac L.M., Madupu R., Kolonay J.F., Durkin S.A., Daugherty S.C.,
RA   Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G.,
RA   Malek J.A., Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K.,
RA   Pal S., Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E.,
RA   Baca E., Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT   "Comparison of the genome of the oral pathogen Treponema denticola with
RT   other spirochete genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
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}.
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DR   EMBL; AE017226; AAS12223.1; -; Genomic_DNA.
DR   RefSeq; NP_972312.1; NC_002967.9.
DR   RefSeq; WP_002679415.1; NC_002967.9.
DR   AlphaFoldDB; P61037; -.
DR   SMR; P61037; -.
DR   STRING; 243275.TDE_1708; -.
DR   EnsemblBacteria; AAS12223; AAS12223; TDE_1708.
DR   GeneID; 2740880; -.
DR   KEGG; tde:TDE_1708; -.
DR   PATRIC; fig|243275.7.peg.1633; -.
DR   eggNOG; COG0815; Bacteria.
DR   HOGENOM; CLU_019563_1_1_12; -.
DR   OMA; FSWMLSD; -.
DR   OrthoDB; 1291198at2; -.
DR   UniPathway; UPA00666; -.
DR   Proteomes; UP000008212; 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   3: Inferred from homology;
KW   Acyltransferase; Cell inner membrane; Cell membrane; Membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..544
FT                   /note="Apolipoprotein N-acyltransferase 1"
FT                   /id="PRO_0000178103"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        57..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   TRANSMEM        514..534
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   DOMAIN          225..501
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   ACT_SITE        272
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   ACT_SITE        360
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
FT   ACT_SITE        412
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01148"
SQ   SEQUENCE   544 AA;  63551 MW;  78E68ECACD6BFB56 CRC64;
     MKNKFIFFTL NLLLAVLGAV LFALSHPNYL NLNGFPFFAY IALIPFFLLL KRTKLKFSFL
     WGAFSGALSY FIFNFWIIFF HPLAIYIIIA KYCILYSVLF FVLKIIDSYF SRYSFIFQTI
     AWVAFEYLNT LGFLGYSYGI MGYTQWNFPI LIRVSSIFGV WGISFLLVFF SACSASFLFE
     FYKEKDIKNV YQRYKLPMMI WVGTFFAFIL YGAFTKIDLS EAQRARIALV QPNRDPWLGN
     LEVYRNNYEE LKNLSEKALK NFPDIELVVW PETAFIPMIR WHYKYTSTYN PNSLLVRELL
     HFLDNQKVPF LIGNDDGVLD EKFSDNNFDN LEDKRLDYNA ALLFIPKKNV SPPEPQTYRK
     MHLVPFTEHF PYQKLFPRFY EFLKENDTHF WEKGKEANLL EFNNFKIGTP ICFEDTFGYI
     SKAFSKKGAN IIINLTNDAW ANSAVSQYQH LSMAVFRAVE NRLPVLRATS SGQTAFIDQN
     GNIQEMLPPF IKDILVADVT VLTEGHKTVY SYLGDFFGVL CTIVLILNLC FIIINKFIKR
     SEVK
 
 
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