位置:首页 > 蛋白库 > PLSX_BACHK
PLSX_BACHK
ID   PLSX_BACHK              Reviewed;         330 AA.
AC   Q6HEW2;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019};
DE            EC=2.3.1.274 {ECO:0000255|HAMAP-Rule:MF_00019};
DE   AltName: Full=Acyl-ACP phosphotransacylase {ECO:0000255|HAMAP-Rule:MF_00019};
DE   AltName: Full=Acyl-[acyl-carrier-protein]--phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019};
DE   AltName: Full=Phosphate-acyl-ACP acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019};
GN   Name=plsX {ECO:0000255|HAMAP-Rule:MF_00019}; OrderedLocusNames=BT9727_3594;
OS   Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=281309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=97-27;
RX   PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA   Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
CC   -!- FUNCTION: Catalyzes the reversible formation of acyl-phosphate (acyl-
CC       PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme
CC       utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
CC       {ECO:0000255|HAMAP-Rule:MF_00019}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-
CC         [ACP]; Xref=Rhea:RHEA:42292, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC         COMP:14125, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:138651; EC=2.3.1.274; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00019};
CC   -!- PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000255|HAMAP-
CC       Rule:MF_00019}.
CC   -!- SUBUNIT: Homodimer. Probably interacts with PlsY. {ECO:0000255|HAMAP-
CC       Rule:MF_00019}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00019}.
CC       Note=Associated with the membrane possibly through PlsY.
CC       {ECO:0000255|HAMAP-Rule:MF_00019}.
CC   -!- SIMILARITY: Belongs to the PlsX family. {ECO:0000255|HAMAP-
CC       Rule:MF_00019}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017355; AAT60619.1; -; Genomic_DNA.
DR   RefSeq; WP_000684110.1; NC_005957.1.
DR   RefSeq; YP_037914.1; NC_005957.1.
DR   AlphaFoldDB; Q6HEW2; -.
DR   SMR; Q6HEW2; -.
DR   EnsemblBacteria; AAT60619; AAT60619; BT9727_3594.
DR   KEGG; btk:BT9727_3594; -.
DR   PATRIC; fig|281309.8.peg.3832; -.
DR   HOGENOM; CLU_039379_1_1_9; -.
DR   OMA; HGKSNAR; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000001301; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043811; F:phosphate:acyl-[acyl carrier protein] acyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_00019; PlsX; 1.
DR   InterPro; IPR003664; FA_synthesis.
DR   InterPro; IPR012281; Phospholipid_synth_PlsX-like.
DR   PANTHER; PTHR30100; PTHR30100; 1.
DR   Pfam; PF02504; FA_synthesis; 1.
DR   PIRSF; PIRSF002465; Phsphlp_syn_PlsX; 1.
DR   TIGRFAMs; TIGR00182; plsX; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lipid biosynthesis; Lipid metabolism; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Transferase.
FT   CHAIN           1..330
FT                   /note="Phosphate acyltransferase"
FT                   /id="PRO_0000189843"
SQ   SEQUENCE   330 AA;  35432 MW;  ADBEAD6F346884F5 CRC64;
     MKIAIDAMGG DHAPKAVVLG AMKAIKEYSD LHITLVGKEE EIRQYLTSEE RITILHTDEK
     IESTDEPVRA VRRKKQASMV LAAQQVKDGV ADACISAGST GALMAAGLFV VGRMEGIERP
     ALSPTMPTVD GEGFVMLDVG ANVDAKPIHL YQYAVMGSVY AEKVRGIKNP RVGLLNVGTE
     DGKGNELSKQ VFTMLKDAPI NFVGNVESRD LLQGVADVVV CDGFTGNVAL KSLEGTALAL
     FSMLKEQLMS SFTSKLAAAV LKPKLMVLKD KMDYSEYGGA ALFGLKAPVI KAHGSSNDQS
     IFSAIRQTRE MVAKEVIPTI SSVMEKEPLQ
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024