ID   OSMV_SALTY              Reviewed;         382 AA.
AC   Q8ZPK4;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Osmoprotectant import ATP-binding protein OsmV;
DE            EC=7.6.2.-;
GN   Name=osmV; OrderedLocusNames=STM1491;
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. Probably responsible for energy coupling to the transport
CC       system. {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: Cell inner membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}.
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 ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; AE006468; AAL20410.1; -; Genomic_DNA.
DR   RefSeq; NP_460451.1; NC_003197.2.
DR   RefSeq; WP_000593086.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZPK4; -.
DR   SMR; Q8ZPK4; -.
DR   STRING; 99287.STM1491; -.
DR   TCDB; 3.A.1.12.14; the atp-binding cassette (abc) superfamily.
DR   PaxDb; Q8ZPK4; -.
DR   EnsemblBacteria; AAL20410; AAL20410; STM1491.
DR   GeneID; 1253009; -.
DR   KEGG; stm:STM1491; -.
DR   PATRIC; fig|99287.12.peg.1576; -.
DR   HOGENOM; CLU_000604_2_2_6; -.
DR   OMA; MYEFNRA; -.
DR   PhylomeDB; Q8ZPK4; -.
DR   BioCyc; SENT99287:STM1491-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0031460; P:glycine betaine transport; IEA:InterPro.
DR   Gene3D; 3.10.580.10; -; 1.
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; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR005892; Gly-betaine_transp_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF00571; CBS; 2.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00116; CBS; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54631; SSF54631; 1.
DR   TIGRFAMs; TIGR01186; proV; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; CBS domain; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Repeat; Translocase; Transport.
FT   CHAIN           1..382
FT                   /note="Osmoprotectant import ATP-binding protein OsmV"
FT                   /id="PRO_0000430043"
FT   DOMAIN          2..241
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          258..320
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          322..373
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   BINDING         39..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   382 AA;  42638 MW;  E237F4C6296AB97B CRC64;
     MIKLENLTKQ FVQKKGQPLK AVDNVNLNVP EGEMCVLLGP SGCGKTTTLK MINRLIAPSS
     GNILINGENT NDMDAVTLRR NIGYVIQQIG LFPNMTIEEN ITVVPRMLGW DKARCKQRAE
     ELMDMVALDA RKFLHRYPKE MSGGQQQRIG VIRALAADPP VLLMDEPFGA VDPINREVIQ
     NQFLDMQRKL KKTVMLVSHD IDEALKLGDR IAVFRQGRIV QCASPDELLA KPANEFVGSF
     VGQDRTLKRL LLVSAGDVTD QQPTITARPS TPLSEAFGIM DDHDIRAITV IDNDGKPLGF
     VKRREARNAS GICADITHPF RITGKAEDNL RIVLSRLYES NTSWMPIVDE DGRYNGEISQ
     DYIADYLSSG RTRRALNIHE NS