ID   THIZ_ALKHC              Reviewed;         249 AA.
AC   Q9K9G7;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Formylaminopyrimidine import ATP-binding protein ThiZ {ECO:0000305};
DE            Short=FAMP import ATP-binding protein {ECO:0000305};
DE            EC=7.6.2.- {ECO:0000305};
GN   Name=thiZ {ECO:0000303|PubMed:17618314};
GN   OrderedLocusNames=BH2680 {ECO:0000312|EMBL:BAB06399.1};
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).
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 such as the formylaminopyrimidine N-
CC       formyl-4-amino-5-aminomethyl-2-methylpyrimidine (FAMP). Is likely
CC       responsible for energy coupling to the transport system.
CC       {ECO:0000303|PubMed:17618314, ECO:0000305}.
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:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; BA000004; BAB06399.1; -; Genomic_DNA.
DR   PIR; H83984; H83984.
DR   RefSeq; WP_010898829.1; NC_002570.2.
DR   AlphaFoldDB; Q9K9G7; -.
DR   SMR; Q9K9G7; -.
DR   STRING; 272558.10175301; -.
DR   EnsemblBacteria; BAB06399; BAB06399; BAB06399.
DR   KEGG; bha:BH2680; -.
DR   eggNOG; COG1116; Bacteria.
DR   HOGENOM; CLU_000604_1_22_9; -.
DR   OrthoDB; 1832232at2; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000001258; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Reference proteome; Translocase; Transport.
FT   CHAIN           1..249
FT                   /note="Formylaminopyrimidine import ATP-binding protein
FT                   ThiZ"
FT                   /id="PRO_0000431517"
FT   DOMAIN          6..228
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         39..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   249 AA;  28258 MW;  20E1E7AD8606885B CRC64;
     MVKELLTFEE VSFAYSSSSP VIERLSFTVF ENEIVAILAK SGSGKSTLFR LITRLESPDQ
     GTIVCHAQGK IGYMPQQDLL LPWLTILENV SLPLEIQGKD KKEAKIIAAS FFNRFGLVGT
     ESLYPDALSG GMRQRAAFLR ATLTSETLLL LDEPFASLDS LTKTSMHHWL VSMWEKEKRT
     LLLVTHDIEE ALLLSDRLFI FTNQPLHGFT EVQVPPDLRR KMETTEKMEQ QRSSLKKDIR
     ALLIEESLR