PROW_ECOLI
ID PROW_ECOLI Reviewed; 354 AA.
AC P14176;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Glycine betaine/proline betaine transport system permease protein ProW {ECO:0000305};
GN Name=proW {ECO:0000303|PubMed:2649479}; OrderedLocusNames=b2678, JW2653;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2649479; DOI=10.1128/jb.171.4.1923-1931.1989;
RA Gowrishankar J.;
RT "Nucleotide sequence of the osmoregulatory proU operon of Escherichia
RT coli.";
RL J. Bacteriol. 171:1923-1931(1989).
RN [2]
RP ERRATUM OF PUBMED:2649479.
RA Gowrishankar J.;
RL J. Bacteriol. 172:1165-1165(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION IN GLYCINE BETAINE TRANSPORT.
RX PubMed=3305496; DOI=10.1016/s0021-9258(18)60890-7;
RA Barron A., Jung J.U., Villarejo W.;
RT "Purification and characterization of a glycine betaine binding protein
RT from Escherichia coli.";
RL J. Biol. Chem. 262:11841-11846(1987).
RN [7]
RP FUNCTION IN PROLINE BETAINE TRANSPORT.
RX PubMed=7898450; DOI=10.1007/bf00290728;
RA Haardt M., Kempf B., Faatz E., Bremer E.;
RT "The osmoprotectant proline betaine is a major substrate for the binding-
RT protein-dependent transport system ProU of Escherichia coli K-12.";
RL Mol. Gen. Genet. 246:783-786(1995).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [9]
RP FUNCTION IN GLYCINE BETAINE TRANSPORT, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=23249124; DOI=10.3109/09687688.2012.754060;
RA Gul N., Poolman B.;
RT "Functional reconstitution and osmoregulatory properties of the ProU ABC
RT transporter from Escherichia coli.";
RL Mol. Membr. Biol. 30:138-148(2013).
CC -!- FUNCTION: Part of the ProU ABC transporter complex involved in glycine
CC betaine and proline betaine uptake (PubMed:3305496, PubMed:7898450,
CC PubMed:23249124). Probably responsible for the translocation of the
CC substrate across the membrane (Probable). {ECO:0000269|PubMed:23249124,
CC ECO:0000269|PubMed:3305496, ECO:0000269|PubMed:7898450, ECO:0000305}.
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:0000269|PubMed:23249124}.
CC -!- INTERACTION:
CC P14176; P14175: proV; NbExp=2; IntAct=EBI-8794761, EBI-546797;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. CysTW subfamily. {ECO:0000305}.
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DR EMBL; M24856; AAA24428.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75725.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16543.1; -; Genomic_DNA.
DR PIR; JS0129; MMECPW.
DR RefSeq; NP_417164.1; NC_000913.3.
DR RefSeq; WP_000774988.1; NZ_LN832404.1.
DR AlphaFoldDB; P14176; -.
DR SMR; P14176; -.
DR BioGRID; 4259449; 33.
DR ComplexPortal; CPX-2126; Glycine/Proline betaine ABC transporter complex.
DR IntAct; P14176; 1.
DR STRING; 511145.b2678; -.
DR TCDB; 3.A.1.12.1; the atp-binding cassette (abc) superfamily.
DR PaxDb; P14176; -.
DR PRIDE; P14176; -.
DR EnsemblBacteria; AAC75725; AAC75725; b2678.
DR EnsemblBacteria; BAA16543; BAA16543; BAA16543.
DR GeneID; 947145; -.
DR KEGG; ecj:JW2653; -.
DR KEGG; eco:b2678; -.
DR PATRIC; fig|1411691.4.peg.4063; -.
DR EchoBASE; EB0765; -.
DR eggNOG; COG4176; Bacteria.
DR HOGENOM; CLU_028473_1_0_6; -.
DR InParanoid; P14176; -.
DR OMA; HFNIMDP; -.
DR PhylomeDB; P14176; -.
DR BioCyc; EcoCyc:PROW-MON; -.
DR BioCyc; MetaCyc:PROW-MON; -.
DR PRO; PR:P14176; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; ISM:EcoCyc.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:1990222; C:ProVWX complex; IPI:ComplexPortal.
DR GO; GO:0005275; F:amine transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015226; F:carnitine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0089718; P:amino acid import across plasma membrane; IDA:ComplexPortal.
DR GO; GO:1902603; P:carnitine transmembrane transport; IBA:GO_Central.
DR GO; GO:0071470; P:cellular response to osmotic stress; IDA:ComplexPortal.
DR GO; GO:0015871; P:choline transport; IBA:GO_Central.
DR GO; GO:0031460; P:glycine betaine transport; IDA:ComplexPortal.
DR GO; GO:1903804; P:glycine import across plasma membrane; IDA:ComplexPortal.
DR GO; GO:0006972; P:hyperosmotic response; IDA:EcoCyc.
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 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_0000060191"
FT TOPO_DOM 1..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..198
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..300
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT DOMAIN 145..324
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 354 AA; 37620 MW; D35F94A74E2779D1 CRC64;
MADQNNPWDT TPAADSAAQS ADAWGTPTTA PTDGGGADWL TSTPAPNVEH FNILDPFHKT
LIPLDSWVTE GIDWVVTHFR PVFQGVRVPV DYILNGFQQL LLGMPAPVAI IVFALIAWQI
SGVGMGVATL VSLIAIGAIG AWSQAMVTLA LVLTALLFCI VIGLPLGIWL ARSPRAAKII
RPLLDAMQTT PAFVYLVPIV MLFGIGNVPG VVVTIIFALP PIIRLTILGI NQVPADLIEA
SRSFGASPRQ MLFKVQLPLA MPTIMAGVNQ TLMLALSMVV IASMIAVGGL GQMVLRGIGR
LDMGLATVGG VGIVILAIIL DRLTQAVGRD SRSRGNRRWY TTGPVGLLTR PFIK
