APBE_TREPA
ID APBE_TREPA Reviewed; 362 AA.
AC O83774;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=TP_0796;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 23-362 IN COMPLEXES WITH ADP;
RP AMP; FAD AND MAGNESIUM, FUNCTION, COFACTOR, AND 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).
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 (By similarity). Displays
CC FAD pyrophosphatase activity in vitro, hydrolyzing FAD into FMN and AMP
CC (PubMed:23447540). {ECO:0000250|UniProtKB:A5F5Y3,
CC ECO:0000269|PubMed:23447540}.
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:0000269|PubMed:23447540};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:23447540};
CC Note=Magnesium. Can also use manganese. {ECO:0000269|PubMed:23447540};
CC -!- SUBUNIT: Monomer. {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}.
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DR EMBL; AE000520; AAC65759.1; -; Genomic_DNA.
DR PIR; C71281; C71281.
DR RefSeq; WP_010882241.1; NC_000919.1.
DR PDB; 4IFU; X-ray; 1.83 A; A=23-362.
DR PDB; 4IFW; X-ray; 2.30 A; A=23-362.
DR PDB; 4IFX; X-ray; 1.45 A; A=23-362.
DR PDB; 4IFZ; X-ray; 1.90 A; A=23-362.
DR PDB; 4IG1; X-ray; 1.43 A; A=23-362.
DR PDB; 4XDR; X-ray; 1.40 A; A=23-362.
DR PDB; 4XDT; X-ray; 1.45 A; A=23-362.
DR PDB; 4XDU; X-ray; 1.35 A; A=23-362.
DR PDBsum; 4IFU; -.
DR PDBsum; 4IFW; -.
DR PDBsum; 4IFX; -.
DR PDBsum; 4IFZ; -.
DR PDBsum; 4IG1; -.
DR PDBsum; 4XDR; -.
DR PDBsum; 4XDT; -.
DR PDBsum; 4XDU; -.
DR SMR; O83774; -.
DR STRING; 243276.TPANIC_0796; -.
DR EnsemblBacteria; AAC65759; AAC65759; TP_0796.
DR KEGG; tpa:TP_0796; -.
DR eggNOG; COG1477; Bacteria.
DR HOGENOM; CLU_044403_1_0_12; -.
DR OMA; MGTFWRV; -.
DR BRENDA; 2.7.1.180; 6429.
DR BRENDA; 3.6.1.18; 6429.
DR Proteomes; UP000000811; 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 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..22
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 23..362
FT /note="FAD:protein FMN transferase"
FT /id="PRO_0000001751"
FT BINDING 118..120
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23447540"
FT BINDING 181
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23447540"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:23447540"
FT BINDING 187
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23447540"
FT BINDING 278..280
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23447540"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:23447540"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:23447540"
FT LIPID 23
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 23
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:4XDU"
FT STRAND 41..49
FT /evidence="ECO:0007829|PDB:4XDU"
FT HELIX 53..74
FT /evidence="ECO:0007829|PDB:4XDU"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:4XDR"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:4XDU"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:4XDU"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:4XDU"
FT HELIX 99..114
FT /evidence="ECO:0007829|PDB:4XDU"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:4XDU"
FT HELIX 124..136
FT /evidence="ECO:0007829|PDB:4XDU"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:4XDU"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:4XDU"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:4XDU"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:4XDU"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:4XDU"
FT HELIX 186..200
FT /evidence="ECO:0007829|PDB:4XDU"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:4XDU"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:4XDU"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:4XDU"
FT STRAND 245..263
FT /evidence="ECO:0007829|PDB:4XDU"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:4XDU"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:4XDU"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:4XDU"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:4XDU"
FT STRAND 293..300
FT /evidence="ECO:0007829|PDB:4XDU"
FT HELIX 302..315
FT /evidence="ECO:0007829|PDB:4XDU"
FT HELIX 317..324
FT /evidence="ECO:0007829|PDB:4XDU"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:4XDU"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:4XDU"
FT TURN 345..347
FT /evidence="ECO:0007829|PDB:4XDU"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:4XDU"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:4XDU"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:4XDU"
SQ SEQUENCE 362 AA; 39064 MW; E64E2FAFD1A7041C CRC64;
MKSSCVYWRI GVLVCILCGV GSCGGRARVR EYSRAELVIG TLCRVRVYSK RPAAEVHAAL
EEVFTLLQQQ EMVLSANRDD SALAALNAQA GSAPVVVDRS LYALLERALF FAEKSGGAFN
PALGAXVKLW NIGFDRAAVP DPDALKEALT RCDFRQVHLR AGVSVGAPHT VQLAQAGMQL
DLGAIAKGFL ADKIVQLLTA HALDSALVDL GGNIFALGLK YGDVRSAAAQ RLEWNVGIRD
PHGTGQKPAL VVSVRDCSVV TSGAYERFFE RDGVRYHHII DPVTGFPAHT DVDSVSIFAP
RSTDADALAT ACFVLGYEKS CALLREFPGV DALFIFPDKR VRASAGIVDR VRVLDARFVL
ER
