OSMY_SALTY
ID OSMY_SALTY Reviewed; 236 AA.
AC Q8ZPK1;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Osmoprotectant import permease protein OsmY;
GN Name=osmY; OrderedLocusNames=STM1494;
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 the translocation of the substrate
CC across the membrane. {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}; Multi-pass
CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
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 binding-protein-dependent transport system
CC permease family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE006468; AAL20413.1; -; Genomic_DNA.
DR RefSeq; NP_460454.1; NC_003197.2.
DR RefSeq; WP_000557304.1; NC_003197.2.
DR AlphaFoldDB; Q8ZPK1; -.
DR SMR; Q8ZPK1; -.
DR STRING; 99287.STM1494; -.
DR TCDB; 3.A.1.12.14; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q8ZPK1; -.
DR EnsemblBacteria; AAL20413; AAL20413; STM1494.
DR GeneID; 1253012; -.
DR KEGG; stm:STM1494; -.
DR PATRIC; fig|99287.12.peg.1579; -.
DR HOGENOM; CLU_046113_7_0_6; -.
DR OMA; MRYLFTH; -.
DR PhylomeDB; Q8ZPK1; -.
DR BioCyc; SENT99287:STM1494-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0031460; P:glycine betaine transport; IBA:GO_Central.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..236
FT /note="Osmoprotectant import permease protein OsmY"
FT /id="PRO_0000430045"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 43..224
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 236 AA; 25411 MW; 4CAFB029989D7AD2 CRC64;
MHTLTLKRVL GFTIVILLLL ALFIWGIGLE TLKARQVDLL YLGQRHLMLV FTSMFFALLV
GIPSGILLSR PAAKGFAEYV MQIFNVGNTL PPLAVLALAM VIIGIGDTPA IVALFLASLL
PIVRNTYAGL CSVPASLIEA ANGIGMTKWQ RLRQVELPNA WPVMLSGIRI ATAINVGTAP
LAFLIGASSY GELIFPGIYL NDFPTLILGA TATALFALIL DTLLAWFGRR LSPHTV