APBE_SALTY
ID APBE_SALTY Reviewed; 350 AA.
AC P41780; O06948;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 120.
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 {ECO:0000303|PubMed:9473043}; OrderedLocusNames=STM2266;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=LT2;
RX PubMed=9473043; DOI=10.1128/jb.180.4.885-891.1998;
RA Beck B.J., Downs D.M.;
RT "The apbE gene encodes a lipoprotein involved in thiamine synthesis in
RT Salmonella typhimurium.";
RL J. Bacteriol. 180:885-891(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29595 / ST1;
RA Beck G., Blat Y., Eisenbach M.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 337-350.
RX PubMed=1904855; DOI=10.1128/jb.173.12.3663-3672.1991;
RA Hakura A., Morimoto K., Sofuni T., Nohmi T.;
RT "Cloning and characterization of the Salmonella typhimurium ada gene, which
RT encodes O6-methylguanine-DNA methyltransferase.";
RL J. Bacteriol. 173:3663-3672(1991).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=LT2;
RX PubMed=10572132; DOI=10.1128/jb.181.23.7285-7290.1999;
RA Beck B.J., Downs D.M.;
RT "A periplasmic location is essential for the role of the ApbE lipoprotein
RT in thiamine synthesis in Salmonella typhimurium.";
RL J. Bacteriol. 181:7285-7290(1999).
RN [6]
RP DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=12486045; DOI=10.1128/jb.185.1.98-106.2003;
RA Skovran E., Downs D.M.;
RT "Lack of the ApbC or ApbE protein results in a defect in Fe-S cluster
RT metabolism in Salmonella enterica serovar Typhimurium.";
RL J. Bacteriol. 185:98-106(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 21-350 IN COMPLEX WITH FAD,
RP SUBUNIT, AND MUTAGENESIS OF TYR-78.
RC STRAIN=LT2;
RX PubMed=21148731; DOI=10.1128/jb.00730-10;
RA Boyd J.M., Endrizzi J.A., Hamilton T.L., Christopherson M.R., Mulder D.W.,
RA Downs D.M., Peters J.W.;
RT "FAD binding by ApbE protein from Salmonella enterica: a new class of FAD-
RT binding proteins.";
RL J. Bacteriol. 193:887-895(2011).
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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21148731}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303, ECO:0000269|PubMed:10572132,
CC ECO:0000269|PubMed:9473043}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303, ECO:0000269|PubMed:9473043}; Periplasmic side
CC {ECO:0000269|PubMed:10572132}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are conditional thiamine
CC auxotrophs, and display phenotypic behaviors similar to those of
CC strains lacking isc (iron-sulfur [Fe-S] cluster biosynthesis) operon
CC functions. {ECO:0000269|PubMed:12486045, ECO:0000269|PubMed:9473043}.
CC -!- SIMILARITY: Belongs to the ApbE family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be involved in synthesis of the
CC pyrimidine moiety of thiamine and/or in metabolism of Fe-S clusters.
CC {ECO:0000303|PubMed:12486045, ECO:0000303|PubMed:21148731,
CC ECO:0000303|PubMed:9473043}.
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DR EMBL; AF035376; AAC46116.1; -; Genomic_DNA.
DR EMBL; U90324; AAB50407.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21168.1; -; Genomic_DNA.
DR EMBL; D90221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_461209.1; NC_003197.2.
DR RefSeq; WP_000784307.1; NC_003197.2.
DR PDB; 3PND; X-ray; 2.75 A; A/B/C/D=21-350.
DR PDBsum; 3PND; -.
DR AlphaFoldDB; P41780; -.
DR SMR; P41780; -.
DR STRING; 99287.STM2266; -.
DR PaxDb; P41780; -.
DR DNASU; 1253788; -.
DR EnsemblBacteria; AAL21168; AAL21168; STM2266.
DR GeneID; 1253788; -.
DR KEGG; stm:STM2266; -.
DR PATRIC; fig|99287.12.peg.2400; -.
DR HOGENOM; CLU_044403_0_0_6; -.
DR OMA; MGTFWRV; -.
DR PhylomeDB; P41780; -.
DR BioCyc; SENT99287:STM2266-MON; -.
DR Proteomes; UP000001014; 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; IBA:GO_Central.
DR GO; GO:0017013; P:protein flavinylation; IBA:GO_Central.
DR DisProt; DP02667; -.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; FAD; Flavoprotein;
KW Lipoprotein; Magnesium; Membrane; Metal-binding; Palmitate;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 20..350
FT /note="FAD:protein FMN transferase"
FT /id="PRO_0000001750"
FT BINDING 41
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:21148731"
FT BINDING 78
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:21148731"
FT BINDING 119..121
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:21148731"
FT BINDING 181
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:21148731"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0AB85"
FT BINDING 187
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:21148731"
FT BINDING 272
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:21148731"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O83774"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0AB85"
FT BINDING 302
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"
FT MUTAGEN 78
FT /note="Y->A: Unable to grow in minimal glucose medium;
FT requires thiamine for growth. Is defective in FAD binding."
FT /evidence="ECO:0000269|PubMed:21148731"
FT CONFLICT 215
FT /note="S -> N (in Ref. 2; AAB50407)"
FT /evidence="ECO:0000305"
FT CONFLICT 321..350
FT /note="LAVFMIMKEGEGFKTWMSPQFKTFLVSDKN -> WRYL (in Ref. 2;
FT AAB50407)"
FT /evidence="ECO:0000305"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:3PND"
FT STRAND 43..52
FT /evidence="ECO:0007829|PDB:3PND"
FT HELIX 54..75
FT /evidence="ECO:0007829|PDB:3PND"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:3PND"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:3PND"
FT HELIX 100..115
FT /evidence="ECO:0007829|PDB:3PND"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:3PND"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:3PND"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:3PND"
FT HELIX 145..152
FT /evidence="ECO:0007829|PDB:3PND"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:3PND"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:3PND"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:3PND"
FT HELIX 183..200
FT /evidence="ECO:0007829|PDB:3PND"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:3PND"
FT STRAND 213..219
FT /evidence="ECO:0007829|PDB:3PND"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:3PND"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:3PND"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:3PND"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:3PND"
FT HELIX 257..263
FT /evidence="ECO:0007829|PDB:3PND"
FT TURN 274..277
FT /evidence="ECO:0007829|PDB:3PND"
FT STRAND 283..293
FT /evidence="ECO:0007829|PDB:3PND"
FT HELIX 294..307
FT /evidence="ECO:0007829|PDB:3PND"
FT HELIX 309..319
FT /evidence="ECO:0007829|PDB:3PND"
FT STRAND 322..329
FT /evidence="ECO:0007829|PDB:3PND"
FT STRAND 332..337
FT /evidence="ECO:0007829|PDB:3PND"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:3PND"
SQ SEQUENCE 350 AA; 38149 MW; 40AA62CB4D04F913 CRC64;
MKMTFCRAVC LAAAFLLMGC DEAPETTTAS PAAQVLEGKT MGTLWRVSVV GIDAKRAAEL
QTKIQTQLDA DDWLLSTYKN DSALMRFNHS RSLAPWPVSE AMADIVTSAL RIGAKTDGAM
DITVGPLVNL WGFGPDRQPL HIPTPAQIDA AKAKTGLQHL QVIDRAGHQF LQKDLPDLYV
DLSTVGEGYA ADHLARLMEQ EGIARYLVSV GGALSSRGMN AQGQPWRVAI QKPTDRENAV
QAIVDINGHG ISTSGSYRNY YELDGKRVSH VIDPQTGRPI EHNLVSVTVI APTALEADGW
DTGLMVLGTQ KAQEVVRREG LAVFMIMKEG EGFKTWMSPQ FKTFLVSDKN
