THIY_ALKHC
ID THIY_ALKHC Reviewed; 330 AA.
AC Q9K9G5;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Formylaminopyrimidine-binding protein {ECO:0000303|PubMed:17618314};
DE Short=FAMP-binding protein {ECO:0000303|PubMed:20873853};
DE Flags: Precursor;
GN Name=thiY {ECO:0000303|PubMed:17618314, ECO:0000303|PubMed:20873853};
GN OrderedLocusNames=BH2682 {ECO:0000312|EMBL:BAB06401.1};
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
RN [2]
RP FUNCTION, AND PATHWAY.
RX PubMed=17618314; DOI=10.1038/nchembio.2007.13;
RA Jenkins A.H., Schyns G., Potot S., Sun G., Begley T.P.;
RT "A new thiamin salvage pathway.";
RL Nat. Chem. Biol. 3:492-497(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 29-330 IN COMPLEX WITH FAMP, AND
RP FUNCTION.
RX PubMed=20873853; DOI=10.1021/bi101209t;
RA Bale S., Rajashankar K.R., Perry K., Begley T.P., Ealick S.E.;
RT "HMP binding protein ThiY and HMP-P synthase THI5 are structural
RT homologues.";
RL Biochemistry 49:8929-8936(2010).
CC -!- FUNCTION: Participates in a thiamine pyrimidine salvage pathway as part
CC of the ABC transporter complex ThiXYZ involved in the import of
CC thiamine degradation products. Binds the formylaminopyrimidine N-
CC formyl-4-amino-5-aminomethyl-2-methylpyrimidine (FAMP). Does not bind
CC thiamine. {ECO:0000269|PubMed:17618314, ECO:0000269|PubMed:20873853}.
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000303|PubMed:17618314}.
CC -!- SUBUNIT: The complex is likely composed of an ATP-binding protein
CC (ThiZ), a transmembrane protein (ThiX) and a solute-binding protein
CC (ThiY). {ECO:0000303|PubMed:17618314, ECO:0000303|PubMed:20873853,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303, ECO:0000303|PubMed:20873853}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000303|PubMed:20873853}.
CC -!- SIMILARITY: Belongs to the NMT1 family. {ECO:0000305}.
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DR EMBL; BA000004; BAB06401.1; -; Genomic_DNA.
DR PIR; B83985; B83985.
DR RefSeq; WP_010898831.1; NC_002570.2.
DR PDB; 3IX1; X-ray; 2.40 A; A/B=29-330.
DR PDBsum; 3IX1; -.
DR AlphaFoldDB; Q9K9G5; -.
DR SMR; Q9K9G5; -.
DR STRING; 272558.10175303; -.
DR EnsemblBacteria; BAB06401; BAB06401; BAB06401.
DR KEGG; bha:BH2682; -.
DR eggNOG; COG0715; Bacteria.
DR HOGENOM; CLU_028871_6_2_9; -.
DR OMA; MKGWKYA; -.
DR OrthoDB; 1635706at2; -.
DR UniPathway; UPA00060; -.
DR EvolutionaryTrace; Q9K9G5; -.
DR Proteomes; UP000001258; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR027939; NMT1/THI5.
DR InterPro; IPR015168; SsuA/THI5.
DR PANTHER; PTHR31528; PTHR31528; 1.
DR Pfam; PF09084; NMT1; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 19..330
FT /note="Formylaminopyrimidine-binding protein"
FT /id="PRO_0000431515"
FT BINDING 38..39
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20873853,
FT ECO:0007744|PDB:3IX1"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20873853,
FT ECO:0007744|PDB:3IX1"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20873853,
FT ECO:0007744|PDB:3IX1"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20873853,
FT ECO:0007744|PDB:3IX1"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20873853,
FT ECO:0007744|PDB:3IX1"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:3IX1"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:3IX1"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:3IX1"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:3IX1"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:3IX1"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:3IX1"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:3IX1"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:3IX1"
FT HELIX 91..99
FT /evidence="ECO:0007829|PDB:3IX1"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:3IX1"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:3IX1"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:3IX1"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:3IX1"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:3IX1"
FT HELIX 145..155
FT /evidence="ECO:0007829|PDB:3IX1"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:3IX1"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:3IX1"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:3IX1"
FT STRAND 179..188
FT /evidence="ECO:0007829|PDB:3IX1"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:3IX1"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:3IX1"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:3IX1"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:3IX1"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:3IX1"
FT HELIX 225..230
FT /evidence="ECO:0007829|PDB:3IX1"
FT HELIX 232..251
FT /evidence="ECO:0007829|PDB:3IX1"
FT HELIX 253..262
FT /evidence="ECO:0007829|PDB:3IX1"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:3IX1"
FT HELIX 273..287
FT /evidence="ECO:0007829|PDB:3IX1"
FT HELIX 299..311
FT /evidence="ECO:0007829|PDB:3IX1"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:3IX1"
SQ SEQUENCE 330 AA; 36346 MW; 9DD309C6726813F3 CRC64;
MKSFKIISLL LAILFLASCQ TNTASDDEAL ETVEVMLDWY PNAVHTFLYV AIENGYFAEE
GLDVDIVFPT NPTDPIQLTA SGAIPLALSY QPDVILARSK DLPVVSVASV VRSPLNHVMF
LAEQDFDSPA DLVGLTVGYP GIPVNEPILK TMVEAAGGDY EQVHLMDVGF ELGASIVSGR
ADAVVGTYIN HEYPVLKHEG HDISYFNPVD YGVPEYDELV LISNEAYVEE SGEVLAAFWR
AALKGYEWMV ENPDEALNVL LTNQDEANFP LIQEVEEESL SILLEKMENP NGPFGGQDAE
SWEEVISWLD AHDWLEQPVV AEDAFSSITD
