ID   PHNU_SALTY              Reviewed;         286 AA.
AC   P96064; Q7CR33;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Putative 2-aminoethylphosphonate transport system permease protein PhnU;
GN   Name=phnU; OrderedLocusNames=STM0427;
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 the
CC       translocation of the substrate across the membrane.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
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 binding-protein-dependent transport system
CC       permease family. {ECO:0000305}.
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DR   EMBL; U69493; AAB39646.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL19381.1; -; Genomic_DNA.
DR   PIR; T46951; T46951.
DR   RefSeq; NP_459422.1; NC_003197.2.
DR   RefSeq; WP_000052716.1; NC_003197.2.
DR   AlphaFoldDB; P96064; -.
DR   SMR; P96064; -.
DR   STRING; 99287.STM0427; -.
DR   TCDB; 3.A.1.11.5; the atp-binding cassette (abc) superfamily.
DR   PaxDb; P96064; -.
DR   EnsemblBacteria; AAL19381; AAL19381; STM0427.
DR   GeneID; 1251946; -.
DR   KEGG; stm:STM0427; -.
DR   PATRIC; fig|99287.12.peg.456; -.
DR   HOGENOM; CLU_016047_18_0_6; -.
DR   OMA; TPFVMRP; -.
DR   PhylomeDB; P96064; -.
DR   BioCyc; SENT99287:STM0427-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033223; P:2-aminoethylphosphonate transport; IEA:InterPro.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd06261; TM_PBP2; 1.
DR   Gene3D; 1.10.3720.10; -; 1.
DR   InterPro; IPR017636; AminoethylPonate_ABC_perm-PhnU.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   SUPFAM; SSF161098; SSF161098; 1.
DR   TIGRFAMs; TIGR03226; PhnU; 1.
DR   PROSITE; PS50928; ABC_TM1; 1.
PE   2: Evidence at transcript level;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..286
FT                   /note="Putative 2-aminoethylphosphonate transport system
FT                   permease protein PhnU"
FT                   /id="PRO_0000286746"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          68..275
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   286 AA;  30891 MW;  5AC95F5DE8EB1937 CRC64;
     MSLILPLEKP ALNLRPLLWL LLPLLVLATL FFWPLSLIVE QALRGANGEI GLETFRQVVD
     SKRFVGALLN TLQIAFFATA GCLLLGSVMS LILVFIPFPG SELIGRVVDT FIALPTFLIT
     LAFTFIYGSA GLLNGTLMSL FAFELPPVDF LYSMQGVILA EITVFTPLVM RPLMAALRQI
     DKSQLEAASI LGAHPLRVIG QVIFPAALPA LMAGGSLCLL LTTNEFGIVL FIGAKGVNTL
     PMMVYSKAIL ESDYTVACMI ALINIVLSLG LFSLYRLAAS RTGVRS