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APBE_ECO57
ID   APBE_ECO57              Reviewed;         351 AA.
AC   P0AB86; P33943; P33944; P76455;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=FAD:protein FMN transferase {ECO:0000250|UniProtKB:A5F5Y3};
DE            EC=2.7.1.180 {ECO:0000250|UniProtKB:A5F5Y3};
DE   AltName: Full=Flavin transferase {ECO:0000250|UniProtKB:A5F5Y3};
DE   Flags: Precursor;
GN   Name=apbE; OrderedLocusNames=Z3472, ECs3103;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Flavin transferase that catalyzes the transfer of the FMN
CC       moiety of FAD and its covalent binding to the hydroxyl group of a
CC       threonine residue in a target flavoprotein such as NqrB and NqrC, two
CC       subunits of the NQR complex. {ECO:0000250|UniProtKB:A5F5Y3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] +
CC         H(+); Xref=Rhea:RHEA:36847, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11061, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:74257, ChEBI:CHEBI:456215; EC=2.7.1.180;
CC         Evidence={ECO:0000250|UniProtKB:A5F5Y3};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:A5F5Y3};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P41780, ECO:0000255|PROSITE-ProRule:PRU00303};
CC       Lipid-anchor {ECO:0000250|UniProtKB:P41780, ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Periplasmic side {ECO:0000250|UniProtKB:P41780}.
CC   -!- SIMILARITY: Belongs to the ApbE family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG57349.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB36526.1; -; Genomic_DNA.
DR   PIR; A85861; A85861.
DR   PIR; G91016; G91016.
DR   RefSeq; NP_311130.1; NC_002695.1.
DR   RefSeq; WP_000406064.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AB86; -.
DR   SMR; P0AB86; -.
DR   STRING; 155864.EDL933_3380; -.
DR   DNASU; 957195; -.
DR   EnsemblBacteria; AAG57349; AAG57349; Z3472.
DR   EnsemblBacteria; BAB36526; BAB36526; ECs_3103.
DR   GeneID; 916810; -.
DR   KEGG; ece:Z3472; -.
DR   KEGG; ecs:ECs_3103; -.
DR   PATRIC; fig|386585.9.peg.3237; -.
DR   eggNOG; COG1477; Bacteria.
DR   HOGENOM; CLU_044403_0_0_6; -.
DR   OMA; MGTFWRV; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017013; P:protein flavinylation; IEA:InterPro.
DR   Gene3D; 3.10.520.10; -; 1.
DR   InterPro; IPR024932; ApbE.
DR   InterPro; IPR003374; ApbE-like_sf.
DR   PANTHER; PTHR30040; PTHR30040; 1.
DR   Pfam; PF02424; ApbE; 1.
DR   PIRSF; PIRSF006268; ApbE; 1.
DR   SUPFAM; SSF143631; SSF143631; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; FAD; Flavoprotein; Lipoprotein;
KW   Magnesium; Membrane; Metal-binding; Palmitate; Reference proteome; Signal;
KW   Transferase.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           20..351
FT                   /note="FAD:protein FMN transferase"
FT                   /id="PRO_0000042801"
FT   BINDING         42
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P41780"
FT   BINDING         79
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P41780"
FT   BINDING         120..122
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P41780"
FT   BINDING         182
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P41780"
FT   BINDING         185
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB85"
FT   BINDING         188
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P41780"
FT   BINDING         273
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P41780"
FT   BINDING         299
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O83774"
FT   BINDING         302
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB85"
FT   BINDING         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O83774"
FT   LIPID           20
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           20
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   351 AA;  38549 MW;  53D370B6BFF843D2 CRC64;
     MEISFTRVAL LAAALFFVGC DQKPQPAKTH ATEVTVLEGK TMGTFWRASI PGIDAKRSAE
     LKEKIQTQLD ADDQLLSTYK KDSALMRFND SQSLSPWPVS EAMADIVTTS LRIGAKTDGA
     MDITVGPLVN LWGFGPEQQP VQIPSQEQID AMKAKTGLQH LTVINQSHQQ YLQKDLPDLY
     VDLSTVGEGY AADHLARLME QEGISRYLVS VGGALNSRGM NGEGLPWRVA IQKPTDKENA
     VQAVVDINGH GISTSGSYRN YYELDGKRLS HVIDPQTGRP IEHNLVSVTV IAPTALEADA
     WDTGLMVLGP EKAKEVVRRE GLAVYMITKE GDSFKTWMSP QFKSFLVSEK N
 
 
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