PROW_SALTY
ID PROW_SALTY Reviewed; 354 AA.
AC P17327;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Glycine betaine/proline betaine transport system permease protein ProW {ECO:0000250|UniProtKB:P14176};
GN Name=proW {ECO:0000303|PubMed:2691838}; OrderedLocusNames=STM2810;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51.
RC STRAIN=LT2;
RX PubMed=2691838; DOI=10.1111/j.1365-2958.1989.tb00253.x;
RA Stirling D.A., Hulton C.S.J., Waddell L., Park S.F., Stewart G.S.A.B.,
RA Booth I.R., Higgins C.F.;
RT "Molecular characterization of the proU loci of Salmonella typhimurium and
RT Escherichia coli encoding osmoregulated glycine betaine transport
RT systems.";
RL Mol. Microbiol. 3:1025-1038(1989).
RN [3]
RP INDUCTION.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=1423593; DOI=10.1016/0092-8674(92)90354-f;
RA Owen-Hughes T.A., Pavitt G.D., Santos D.S., Sidebotham J.M., Hulton C.S.,
RA Hinton J.C., Higgins C.F.;
RT "The chromatin-associated protein H-NS interacts with curved DNA to
RT influence DNA topology and gene expression.";
RL Cell 71:255-265(1992).
CC -!- FUNCTION: Part of the ProU ABC transporter complex involved in glycine
CC betaine and proline betaine uptake. Probably responsible for the
CC translocation of the substrate across the membrane.
CC {ECO:0000250|UniProtKB:P14176}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (ProV),
CC two transmembrane proteins (ProW) and a solute-binding protein (ProX).
CC {ECO:0000250|UniProtKB:P14176}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P14176}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Induced in response to increased extracellular osmolarity,
CC this is the second gene of the proU operon (proV-proW-proX).
CC Osmoregulation requires curved DNA downstream of the transcription
CC start site in proV, which is repressed when bound by H-NS. H-NS may act
CC indirectly to influence the local topology of the promoter
CC (PubMed:1423593). {ECO:0000305|PubMed:1423593}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. CysTW subfamily. {ECO:0000305}.
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DR EMBL; AE006468; AAL21695.1; -; Genomic_DNA.
DR EMBL; X52693; CAA36922.1; -; Genomic_DNA.
DR RefSeq; NP_461736.1; NC_003197.2.
DR RefSeq; WP_000775022.1; NC_003197.2.
DR AlphaFoldDB; P17327; -.
DR SMR; P17327; -.
DR STRING; 99287.STM2810; -.
DR PaxDb; P17327; -.
DR EnsemblBacteria; AAL21695; AAL21695; STM2810.
DR GeneID; 1254333; -.
DR KEGG; stm:STM2810; -.
DR PATRIC; fig|99287.12.peg.2968; -.
DR HOGENOM; CLU_028473_1_0_6; -.
DR OMA; HFNIMDP; -.
DR PhylomeDB; P17327; -.
DR BioCyc; SENT99287:STM2810-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005275; F:amine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015226; F:carnitine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR GO; GO:1902603; P:carnitine transmembrane transport; IBA:GO_Central.
DR GO; GO:0015871; P:choline transport; 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 2: Evidence at transcript level;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..354
FT /note="Glycine betaine/proline betaine transport system
FT permease protein ProW"
FT /id="PRO_0000060192"
FT TOPO_DOM 1..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P14176"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P14176"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P14176"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..198
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P14176"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P14176"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..300
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P14176"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P14176"
FT DOMAIN 145..324
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 31
FT /note="A -> R (in Ref. 2; CAA36922)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 37655 MW; 9DDDF0A349872A46 CRC64;
MADQTNPWDT AQVADTTTQT ADAWGTPAGV ATDGGSTDWL NSAPAPAPEH FSLLDPFHKT
LIPLDSWVTE GIDWVVTHFR PLFQGIRVPV DYILNGFQQL LLGMPAPVAI ILFALIAWQV
SGVGMGIATL ISLIAIGAIG AWSQAMITLA LVLTALLFCV VIGLPMGIWL ARSPRAAKIV
RPLLDAMQTT PAFVYLVPIV MLFGIGNVPG VVVTIIFALP PIVRLTILGI NQVPADLIEA
SRSFGASPRQ MLFKVQLPLA MPTIMAGVNQ TLMLALSMVV IASMIAVGGL GQMVLRGIGR
LDMGLATVGG VGIVILAIIL DRLTQAVGRD SRSRGNRRWY TTGPVGLITR PFVK
