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APBE_CHLMU
ID   APBE_CHLMU              Reviewed;         316 AA.
AC   Q9PKW2;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   03-AUG-2022, entry version 96.
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=TC_0349;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF39210.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE002160; AAF39210.1; ALT_INIT; Genomic_DNA.
DR   PIR; E81713; E81713.
DR   RefSeq; WP_010230229.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PKW2; -.
DR   SMR; Q9PKW2; -.
DR   STRING; 243161.TC_0349; -.
DR   EnsemblBacteria; AAF39210; AAF39210; TC_0349.
DR   GeneID; 1245702; -.
DR   KEGG; cmu:TC_0349; -.
DR   eggNOG; COG1477; Bacteria.
DR   HOGENOM; CLU_044403_0_1_0; -.
DR   OrthoDB; 2021063at2; -.
DR   Proteomes; UP000000800; 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; Signal; Transferase.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           20..316
FT                   /note="FAD:protein FMN transferase"
FT                   /id="PRO_0000001745"
FT   BINDING         33
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P41780"
FT   BINDING         71
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P41780"
FT   BINDING         112..114
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P41780"
FT   BINDING         170
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P41780"
FT   BINDING         173
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O83774"
FT   BINDING         176
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O83774"
FT   BINDING         253
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P41780"
FT   BINDING         282
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O83774"
FT   BINDING         286
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   316 AA;  35726 MW;  A92ECA297C8CF322 CRC64;
     MGKFFTPYAL IIFVFLIQAC SSPSKTIFEG VRMTIPYRVV LGETLSFSQK KQAQKEIDQI
     FDHIDQIFNN WNPFSEISRI NRSETLEPIS LSPELFSFLC EIDRFHTFSD GRFDPTLGAL
     KNLWLLHLKS QTLPPQELLH SYKQNTGWHL LSLDKTNHTL KKLSPSVQLD LCGAVKGFAV
     DLLGIFCSQF CQNYYVEWGG EIKTSGKHPS GRSWAIASSA TPEILHLNNS SIATSGNQYQ
     RWYVNKKIYT HILDPLTGIP LEESSYPILA VSVIDENCAF ADAMATALTT FTSKQEALDW
     AKKKHLCVYI TDKNAS
 
 
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