ID   PHNT_SALTY              Reviewed;         369 AA.
AC   P96063; Q7CR32;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Putative 2-aminoethylphosphonate import ATP-binding protein PhnT;
GN   Name=phnT; OrderedLocusNames=STM0428;
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].
RC   STRAIN=LT2;
RA   Metcalf W.W., Jiang W., Wanner B.L.;
RT   "Molecular genetic analysis of the Salmonella typhimurium LT2 phnXWRSTUV
RT   locus required for 2-aminoethylphosphonate transport and metabolism.";
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
RP   CLONING, AND INDUCTION.
RC   STRAIN=LT2;
RX   PubMed=7592415; DOI=10.1128/jb.177.22.6411-6421.1995;
RA   Jiang W., Metcalf W.W., Lee K.-S., Wanner B.L.;
RT   "Molecular cloning, mapping, and regulation of Pho regulon genes for
RT   phosphonate breakdown by the phosphonatase pathway of Salmonella
RT   typhimurium LT2.";
RL   J. Bacteriol. 177:6411-6421(1995).
CC   -!- FUNCTION: Probably part of the PhnSTUV complex (TC 3.A.1.11.5) involved
CC       in 2-aminoethylphosphonate import. Probably responsible for energy
CC       coupling to the transport system.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC       membrane protein {ECO:0000305}.
CC   -!- INDUCTION: Induced when inorganic phosphate is limiting; this is
CC       controlled by PhoB. {ECO:0000269|PubMed:7592415}.
CC   -!- MISCELLANEOUS: Maps to a phosphate-starvation-inducible locus
CC       previously known as psiC.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. 2-
CC       aminoethylphosphonate importer (TC 3.A.1.11.5) family. {ECO:0000305}.
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DR   EMBL; U69493; AAB39645.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL19382.1; -; Genomic_DNA.
DR   PIR; T46950; T46950.
DR   RefSeq; NP_459423.1; NC_003197.2.
DR   RefSeq; WP_000928801.1; NC_003197.2.
DR   AlphaFoldDB; P96063; -.
DR   SMR; P96063; -.
DR   STRING; 99287.STM0428; -.
DR   TCDB; 3.A.1.11.5; the atp-binding cassette (abc) superfamily.
DR   PaxDb; P96063; -.
DR   PRIDE; P96063; -.
DR   EnsemblBacteria; AAL19382; AAL19382; STM0428.
DR   GeneID; 1251947; -.
DR   KEGG; stm:STM0428; -.
DR   PATRIC; fig|99287.12.peg.457; -.
DR   HOGENOM; CLU_000604_1_1_6; -.
DR   OMA; HITAIHV; -.
DR   PhylomeDB; P96063; -.
DR   BioCyc; SENT99287:STM0428-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
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; IPR017662; AminoethylPonate_ABC_PhnT.
DR   InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013611; Transp-assoc_OB_typ2.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF08402; TOBE_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF50331; SSF50331; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR03258; PhnT; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Transport.
FT   CHAIN           1..369
FT                   /note="Putative 2-aminoethylphosphonate import ATP-binding
FT                   protein PhnT"
FT                   /id="PRO_0000286742"
FT   DOMAIN          19..250
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         51..58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   369 AA;  40082 MW;  CAFD8F415A60C564 CRC64;
     MLMKTTTVHA PASQGTSGIV LDSLRVAYHG NVVLKPLSLT IEPGEVLALI GPSGSGKTTV
     LRAVAGFVQP AGGRILIGDT DVTHLPPYKR GLAMVVQNYA LFPHLKVEDN VAFGLRAQKQ
     PKALINERVT QALKTVGMSD YAARYPHQLS GGQQQRVAIA RAIAVRPRVL LLDEPLSALD
     AQIRHNMVEE IARLHRELPE LTILYVTHDQ TEALTLADKI GIMKDGSLIA HGETRALYQH
     PPNRFAAEFL GRANILSAIA LGITEAPGLV DVSCGGAVIR AFSRGSHHGY NKLLCIRPQH
     LSLTPRSAYS NRFNATLQSV HWQGDLTHLL CDVAGETVRM VLTHVNPLPR VGDKLALWFE
     PDDAVLIEV