PROP_ECOLI
ID PROP_ECOLI Reviewed; 500 AA.
AC P0C0L7; P30848; Q2M6J3;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Proline/betaine transporter;
DE AltName: Full=Proline porter II;
DE Short=PPII;
GN Name=proP; OrderedLocusNames=b4111, JW4072;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=8421314; DOI=10.1006/jmbi.1993.1030;
RA Culham D.E., Lasby B., Marangoni A.G., Milner J.L., Steer B.A.,
RA van Nues R.W., Wood J.M.;
RT "Isolation and sequencing of Escherichia coli gene proP reveals unusual
RT structural features of the osmoregulatory proline/betaine transporter,
RT ProP.";
RL J. Mol. Biol. 229:268-276(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
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 [4]
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 [5]
RP FUNCTION, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=3082857; DOI=10.1128/jb.166.1.331-333.1986;
RA Gowrishankar J.;
RT "proP-mediated proline transport also plays a role in Escherichia coli
RT osmoregulation.";
RL J. Bacteriol. 166:331-333(1986).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=10026245; DOI=10.1021/bi981279n;
RA Racher K.I., Voegele R.T., Marshall E.V., Culham D.E., Wood J.M., Jung H.,
RA Bacon M., Cairns M.T., Ferguson S.M., Liang W.J., Henderson P.J., White G.,
RA Hallett F.R.;
RT "Purification and reconstitution of an osmosensor: transporter ProP of
RT Escherichia coli senses and responds to osmotic shifts.";
RL Biochemistry 38:1676-1684(1999).
RN [7]
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 [8]
RP STRUCTURE BY NMR OF 464-498.
RX PubMed=14643666; DOI=10.1016/j.jmb.2003.10.020;
RA Zoetewey D.L., Tripet B.P., Kutateladze T.G., Overduin M.J., Wood J.M.,
RA Hodges R.S.;
RT "Solution structure of the C-terminal antiparallel coiled-coil domain from
RT Escherichia coli osmosensor ProP.";
RL J. Mol. Biol. 334:1063-1076(2003).
CC -!- FUNCTION: Proton symporter that senses osmotic shifts and responds by
CC importing osmolytes such as proline, glycine betaine, stachydrine,
CC pipecolic acid, ectoine and taurine. It is both an osmosensor and an
CC osmoregulator which is available to participate early in the bacterial
CC osmoregulatory response. {ECO:0000269|PubMed:10026245,
CC ECO:0000269|PubMed:3082857, ECO:0000269|PubMed:8421314}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=175 uM for proline {ECO:0000269|PubMed:10026245};
CC Vmax=83.6 nmol/min/mg enzyme with proline as substrate
CC {ECO:0000269|PubMed:10026245};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:10026245,
CC ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Induced by an increase in the osmolarity of the growth
CC medium. {ECO:0000269|PubMed:3082857}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Metabolite:H+
CC Symporter (MHS) family (TC 2.A.1.6) 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; M83089; AAB00919.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97010.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77072.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78113.1; -; Genomic_DNA.
DR PIR; S32331; S32331.
DR RefSeq; NP_418535.1; NC_000913.3.
DR RefSeq; WP_001298520.1; NZ_SSZK01000018.1.
DR PDB; 1R48; NMR; -; A/B=468-497.
DR PDBsum; 1R48; -.
DR AlphaFoldDB; P0C0L7; -.
DR BMRB; P0C0L7; -.
DR SMR; P0C0L7; -.
DR BioGRID; 4263085; 22.
DR STRING; 511145.b4111; -.
DR TCDB; 2.A.1.6.4; the major facilitator superfamily (mfs).
DR jPOST; P0C0L7; -.
DR PaxDb; P0C0L7; -.
DR PRIDE; P0C0L7; -.
DR EnsemblBacteria; AAC77072; AAC77072; b4111.
DR EnsemblBacteria; BAE78113; BAE78113; BAE78113.
DR GeneID; 948626; -.
DR KEGG; ecj:JW4072; -.
DR KEGG; eco:b4111; -.
DR PATRIC; fig|1411691.4.peg.2589; -.
DR EchoBASE; EB1569; -.
DR eggNOG; COG0477; Bacteria.
DR HOGENOM; CLU_001265_39_0_6; -.
DR InParanoid; P0C0L7; -.
DR OMA; FLVEMFP; -.
DR PhylomeDB; P0C0L7; -.
DR BioCyc; EcoCyc:PROP-MON; -.
DR BioCyc; MetaCyc:PROP-MON; -.
DR SABIO-RK; P0C0L7; -.
DR EvolutionaryTrace; P0C0L7; -.
DR PRO; PR:P0C0L7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:CAFA.
DR GO; GO:0005297; F:proline:proton symporter activity; IDA:EcoCyc.
DR GO; GO:0006865; P:amino acid transport; IDA:EcoliWiki.
DR GO; GO:0071474; P:cellular hyperosmotic response; IDA:EcoCyc.
DR GO; GO:0071475; P:cellular hyperosmotic salinity response; IDA:CAFA.
DR GO; GO:0031460; P:glycine betaine transport; IDA:EcoCyc.
DR GO; GO:0007231; P:osmosensory signaling pathway; IDA:CAFA.
DR GO; GO:1905647; P:proline import across plasma membrane; IDA:CAFA.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004736; MHS_symport.
DR InterPro; IPR015041; Osmo_CC.
DR InterPro; IPR036292; ProP_C.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF08946; Osmo_CC; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR SUPFAM; SSF103661; SSF103661; 1.
DR TIGRFAMs; TIGR00883; 2A0106; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Coiled coil; Membrane;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..500
FT /note="Proline/betaine transporter"
FT /id="PRO_0000050324"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..65
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..121
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..194
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..297
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..350
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..416
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 438..500
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT COILED 453..498
FT /evidence="ECO:0000255"
FT HELIX 469..494
FT /evidence="ECO:0007829|PDB:1R48"
SQ SEQUENCE 500 AA; 54846 MW; 60EDDBF61190DDFC CRC64;
MLKRKKVKPI TLRDVTIIDD GKLRKAITAA SLGNAMEWFD FGVYGFVAYA LGKVFFPGAD
PSVQMVAALA TFSVPFLIRP LGGLFFGMLG DKYGRQKILA ITIVIMSIST FCIGLIPSYD
TIGIWAPILL LICKMAQGFS VGGEYTGASI FVAEYSPDRK RGFMGSWLDF GSIAGFVLGA
GVVVLISTIV GEANFLDWGW RIPFFIALPL GIIGLYLRHA LEETPAFQQH VDKLEQGDRE
GLQDGPKVSF KEIATKYWRS LLTCIGLVIA TNVTYYMLLT YMPSYLSHNL HYSEDHGVLI
IIAIMIGMLF VQPVMGLLSD RFGRRPFVLL GSVALFVLAI PAFILINSNV IGLIFAGLLM
LAVILNCFTG VMASTLPAMF PTHIRYSALA AAFNISVLVA GLTPTLAAWL VESSQNLMMP
AYYLMVVAVV GLITGVTMKE TANRPLKGAT PAASDIQEAK EILVEHYDNI EQKIDDIDHE
IADLQAKRTR LVQQHPRIDE
