ID   OSMX_SALTY              Reviewed;         300 AA.
AC   Q8ZPK2;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Osmoprotectant-binding protein OsmX;
DE   Flags: Precursor;
GN   Name=osmX; OrderedLocusNames=STM1493;
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 [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   [2]
RP   FUNCTION, SUBUNIT, INDUCTION, DISRUPTION PHENOTYPE, AND GENE NAME.
RC   STRAIN=LT2;
RX   PubMed=22609924; DOI=10.1128/jb.00495-12;
RA   Frossard S.M., Khan A.A., Warrick E.C., Gately J.M., Hanson A.D.,
RA   Oldham M.L., Sanders D.A., Csonka L.N.;
RT   "Identification of a third osmoprotectant transport system, the osmU
RT   system, in Salmonella enterica.";
RL   J. Bacteriol. 194:3861-3871(2012).
CC   -!- FUNCTION: Part of the OsmU ABC transporter complex, which is involved
CC       in the uptake of osmoprotectants such as choline-O-sulfate and glycine
CC       betaine. {ECO:0000269|PubMed:22609924}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (OsmV),
CC       two transmembrane proteins (OsmW and OsmY) and a solute-binding protein
CC       (OsmX). {ECO:0000305|PubMed:22609924}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- INDUCTION: Induced by osmotic stress. Part of the osmU operon, which
CC       consists of four genes (osmV, osmW, osmX and osmY).
CC       {ECO:0000269|PubMed:22609924}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the osmU operon eliminates the
CC       residual osmoprotection by glycine betaine in a mutant that is lacking
CC       the ProP and the ProU systems. OsmU deletion has no effect on the
CC       utilization of glycine betaine as an osmoprotectant when ProP or ProU
CC       are functional. {ECO:0000269|PubMed:22609924}.
CC   -!- SIMILARITY: Belongs to the OsmX family. {ECO:0000305}.
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DR   EMBL; AE006468; AAL20412.1; -; Genomic_DNA.
DR   RefSeq; NP_460453.1; NC_003197.2.
DR   RefSeq; WP_001211193.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZPK2; -.
DR   SMR; Q8ZPK2; -.
DR   STRING; 99287.STM1493; -.
DR   TCDB; 3.A.1.12.14; the atp-binding cassette (abc) superfamily.
DR   PaxDb; Q8ZPK2; -.
DR   EnsemblBacteria; AAL20412; AAL20412; STM1493.
DR   GeneID; 1253011; -.
DR   KEGG; stm:STM1493; -.
DR   PATRIC; fig|99287.12.peg.1578; -.
DR   HOGENOM; CLU_038355_1_0_6; -.
DR   OMA; APMNNTY; -.
DR   PhylomeDB; Q8ZPK2; -.
DR   BioCyc; SENT99287:STM1493-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   InterPro; IPR007210; ABC_Gly_betaine_transp_sub-bd.
DR   Pfam; PF04069; OpuAC; 1.
PE   1: Evidence at protein level;
KW   Periplasm; Reference proteome; Signal; Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..300
FT                   /note="Osmoprotectant-binding protein OsmX"
FT                   /id="PRO_0000430046"
SQ   SEQUENCE   300 AA;  33884 MW;  8B0CD02A292DA16B CRC64;
     MRFKKHLLGW LAATLLFSSQ TQAAPLVLAT KSFTEQHILS AMTVQYLQKK GFQVQPQTNI
     AAVISRNAMV NKQIDITWEY TGTSLIIFNR IDKRMSPQET YDTVKRLDAK LGLVWLKPAD
     MNNTYAFAMQ RKRAESENIT TISQMVAKIE QVRQNDPDHN WMLGLDLEFA GRSDGMKPLQ
     QAYQMQLDRP QIRQMDPGLV YNAVRDGLVD AGLVYTTDGR VKGFDLKVLE DDKGFFPSYA
     VTPVVRKEVL EANPGLDDAL NTLSGLLNND VISTLNAQVD IEHRTPQQVA HQFLQDKGLL