位置:首页 > 蛋白库 > ACPT_ECOLI
ACPT_ECOLI
ID   ACPT_ECOLI              Reviewed;         195 AA.
AC   P37623; Q2M7D8;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=4'-phosphopantetheinyl transferase AcpT;
DE            EC=2.7.8.7 {ECO:0000305|PubMed:10625633};
GN   Name=acpT {ECO:0000303|PubMed:10625633}; Synonyms=yhhU;
GN   OrderedLocusNames=b3475, JW3440;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA   Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT   from 76.0 to 81.5 minutes.";
RL   Nucleic Acids Res. 22:2576-2586(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION.
RX   PubMed=8939709; DOI=10.1016/s1074-5521(96)90181-7;
RA   Lambalot R.H., Gehring A.M., Flugel R.S., Zuber P., LaCelle M.,
RA   Marahiel M.A., Reid R., Khosla C., Walsh C.T.;
RT   "A new enzyme superfamily -- the phosphopantetheinyl transferases.";
RL   Chem. Biol. 3:923-936(1996).
RN   [5]
RP   FUNCTION.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=10625633; DOI=10.1074/jbc.275.2.959;
RA   Flugel R.S., Hwangbo Y., Lambalot R.H., Cronan J.E. Jr., Walsh C.T.;
RT   "Holo-(acyl carrier protein) synthase and phosphopantetheinyl transfer in
RT   Escherichia coli.";
RL   J. Biol. Chem. 275:959-968(2000).
CC   -!- FUNCTION: May be involved in an alternative pathway for
CC       phosphopantetheinyl transfer and holo-ACP synthesis in E.coli. The
CC       native apo-protein substrate is unknown. Is able to functionally
CC       replace AcpS in vivo but only when expressed at high levels.
CC       {ECO:0000269|PubMed:10625633, ECO:0000269|PubMed:8939709}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-
CC         [ACP]; Xref=Rhea:RHEA:12068, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC         COMP:9690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:64479; EC=2.7.8.7;
CC         Evidence={ECO:0000305|PubMed:10625633};
CC   -!- SIMILARITY: Belongs to the P-Pant transferase superfamily.
CC       Gsp/Sfp/HetI/AcpT family. {ECO:0000305}.
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; U00039; AAB18450.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76500.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77818.1; -; Genomic_DNA.
DR   PIR; S47694; S47694.
DR   RefSeq; NP_417932.1; NC_000913.3.
DR   RefSeq; WP_000285774.1; NZ_SSZK01000008.1.
DR   AlphaFoldDB; P37623; -.
DR   SMR; P37623; -.
DR   BioGRID; 4259300; 100.
DR   DIP; DIP-12355N; -.
DR   IntAct; P37623; 1.
DR   STRING; 511145.b3475; -.
DR   jPOST; P37623; -.
DR   PaxDb; P37623; -.
DR   PRIDE; P37623; -.
DR   EnsemblBacteria; AAC76500; AAC76500; b3475.
DR   EnsemblBacteria; BAE77818; BAE77818; BAE77818.
DR   GeneID; 947979; -.
DR   KEGG; ecj:JW3440; -.
DR   KEGG; eco:b3475; -.
DR   PATRIC; fig|1411691.4.peg.3250; -.
DR   EchoBASE; EB2135; -.
DR   eggNOG; COG2091; Bacteria.
DR   HOGENOM; CLU_119926_0_0_6; -.
DR   InParanoid; P37623; -.
DR   OMA; WQIVSID; -.
DR   PhylomeDB; P37623; -.
DR   BioCyc; EcoCyc:EG12221-MON; -.
DR   BioCyc; MetaCyc:EG12221-MON; -.
DR   PRO; PR:P37623; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IDA:EcoliWiki.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IGI:EcoliWiki.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IBA:GO_Central.
DR   GO; GO:0018070; P:peptidyl-serine phosphopantetheinylation; NAS:EcoliWiki.
DR   Gene3D; 3.90.470.20; -; 1.
DR   InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR   InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR   Pfam; PF01648; ACPS; 1.
DR   SUPFAM; SSF56214; SSF56214; 2.
PE   3: Inferred from homology;
KW   Reference proteome; Transferase.
FT   CHAIN           1..195
FT                   /note="4'-phosphopantetheinyl transferase AcpT"
FT                   /id="PRO_0000206081"
SQ   SEQUENCE   195 AA;  21768 MW;  29385FDA343B2AB7 CRC64;
     MYRIVLGKVS TLSAAPLPPG LREQAPQGPR RERWLAGRAL LSHTLSPLPE IIYGEQGKPA
     FAPEMPLWFN LSHSGDDIAL LLSDEGEVGC DIEVIRPRAN WRWLANAVFS LGEHAEMDAV
     HPDQQLEMFW RIWTRKEAIV KQRGGSAWQI VSVDSTYHSS LSVSHCQLEN LSLAICTPTP
     FTLTADSVQW IDSVN
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024