APBE_ECOLI
ID APBE_ECOLI Reviewed; 351 AA.
AC P0AB85; 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 116.
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; Synonyms=yojK, yojL; OrderedLocusNames=b2214, JW5368;
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 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RT "Automated multiplex sequencing of the E.coli genome.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
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 [4]
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 [5]
RP SUBUNIT.
RX PubMed=23447540; DOI=10.1074/jbc.m113.449975;
RA Deka R.K., Brautigam C.A., Liu W.Z., Tomchick D.R., Norgard M.V.;
RT "The TP0796 lipoprotein of Treponema pallidum is a bimetal-dependent FAD
RT pyrophosphatase with a potential role in flavin homeostasis.";
RL J. Biol. Chem. 288:11106-11121(2013).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 21-351 IN COMPLEX WITH CALCIUM.
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of a thiamine biosynthesis lipoprotein ApbE.";
RL Submitted (NOV-2006) to the PDB data bank.
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:23447540}.
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=AAA16404.1; Type=Frameshift; Note=Produces two separate ORFs.; Evidence={ECO:0000305};
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DR EMBL; U00008; AAA16405.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00008; AAA16404.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC75274.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15997.1; -; Genomic_DNA.
DR PIR; D64991; D64991.
DR RefSeq; NP_416718.1; NC_000913.3.
DR RefSeq; WP_000406064.1; NZ_SSZK01000030.1.
DR PDB; 2O18; X-ray; 2.20 A; A/B/C/D=21-351.
DR PDB; 4XGV; X-ray; 1.88 A; A/B/C/D=21-351.
DR PDB; 4XGW; X-ray; 1.75 A; A/B/C/D=21-351.
DR PDB; 4XGX; X-ray; 1.90 A; A/B=21-351.
DR PDBsum; 2O18; -.
DR PDBsum; 4XGV; -.
DR PDBsum; 4XGW; -.
DR PDBsum; 4XGX; -.
DR AlphaFoldDB; P0AB85; -.
DR SMR; P0AB85; -.
DR BioGRID; 4261922; 69.
DR STRING; 511145.b2214; -.
DR jPOST; P0AB85; -.
DR PaxDb; P0AB85; -.
DR PRIDE; P0AB85; -.
DR EnsemblBacteria; AAC75274; AAC75274; b2214.
DR EnsemblBacteria; BAA15997; BAA15997; BAA15997.
DR GeneID; 946711; -.
DR KEGG; ecj:JW5368; -.
DR KEGG; eco:b2214; -.
DR PATRIC; fig|1411691.4.peg.21; -.
DR EchoBASE; EB1998; -.
DR eggNOG; COG1477; Bacteria.
DR InParanoid; P0AB85; -.
DR OMA; MGTFWRV; -.
DR PhylomeDB; P0AB85; -.
DR BioCyc; EcoCyc:EG12073-MON; -.
DR BioCyc; MetaCyc:EG12073-MON; -.
DR BRENDA; 2.7.1.180; 2026.
DR BRENDA; 3.6.1.18; 2026.
DR EvolutionaryTrace; P0AB85; -.
DR PRO; PR:P0AB85; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0046658; C:anchored component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IDA:EcoCyc.
DR GO; GO:0016740; F:transferase activity; IDA:EcoCyc.
DR GO; GO:0017013; P:protein flavinylation; IDA:EcoCyc.
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..351
FT /note="FAD:protein FMN transferase"
FT /id="PRO_0000001748"
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:0000269|Ref.6, ECO:0000305"
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:0000269|Ref.6, ECO:0000305"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|Ref.6, ECO:0000305"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|Ref.6, ECO:0000305"
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 STRAND 34..41
FT /evidence="ECO:0007829|PDB:4XGW"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:4XGW"
FT HELIX 55..76
FT /evidence="ECO:0007829|PDB:4XGW"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:4XGW"
FT HELIX 84..90
FT /evidence="ECO:0007829|PDB:4XGW"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:4XGW"
FT HELIX 101..116
FT /evidence="ECO:0007829|PDB:4XGW"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:4XGW"
FT HELIX 126..132
FT /evidence="ECO:0007829|PDB:4XGW"
FT HELIX 146..153
FT /evidence="ECO:0007829|PDB:4XGW"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:4XGW"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:4XGW"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:4XGW"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:4XGW"
FT HELIX 187..201
FT /evidence="ECO:0007829|PDB:4XGW"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:4XGW"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:4XGW"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:4XGW"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:4XGW"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:4XGW"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:4XGW"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:4XGW"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:4XGW"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:4XGW"
FT STRAND 285..294
FT /evidence="ECO:0007829|PDB:4XGW"
FT HELIX 295..308
FT /evidence="ECO:0007829|PDB:4XGW"
FT HELIX 310..320
FT /evidence="ECO:0007829|PDB:4XGW"
FT STRAND 323..329
FT /evidence="ECO:0007829|PDB:4XGW"
FT STRAND 334..338
FT /evidence="ECO:0007829|PDB:4XGW"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:4XGW"
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
