UHPC_ECOLI
ID UHPC_ECOLI Reviewed; 439 AA.
AC P09836; P76728; Q2M7Y0;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Membrane sensor protein UhpC {ECO:0000305};
GN Name=uhpC {ECO:0000303|PubMed:3038843}; OrderedLocusNames=b3667, JW3642;
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=3301805; DOI=10.1128/jb.169.8.3556-3563.1987;
RA Friedrich M.J., Kadner R.J.;
RT "Nucleotide sequence of the uhp region of Escherichia coli.";
RL J. Bacteriol. 169:3556-3563(1987).
RN [2]
RP SEQUENCE REVISION.
RA Kadner R.J.;
RL Submitted (AUG-1990) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1569007; DOI=10.1128/jb.174.9.2754-2762.1992;
RA Island M.D., Wei B.-Y., Kadner R.J.;
RT "Structure and function of the uhp genes for the sugar phosphate transport
RT system in Escherichia coli and Salmonella typhimurium.";
RL J. Bacteriol. 174:2754-2762(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [5]
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 [6]
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 [7]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=3038843; DOI=10.1128/jb.169.8.3546-3555.1987;
RA Weston L.A., Kadner R.J.;
RT "Identification of uhp polypeptides and evidence for their role in
RT exogenous induction of the sugar phosphate transport system of Escherichia
RT coli K-12.";
RL J. Bacteriol. 169:3546-3555(1987).
RN [8]
RP FUNCTION.
RX PubMed=8349544; DOI=10.1128/jb.175.16.5028-5034.1993;
RA Island M.D., Kadner R.J.;
RT "Interplay between the membrane-associated UhpB and UhpC regulatory
RT proteins.";
RL J. Bacteriol. 175:5028-5034(1993).
RN [9]
RP FUNCTION.
RX PubMed=11053370; DOI=10.1128/jb.182.22.6279-6286.2000;
RA Wright J.S., Olekhnovich I.N., Touchie G., Kadner R.J.;
RT "The histidine kinase domain of UhpB inhibits UhpA action at the
RT Escherichia coli uhpT promoter.";
RL J. Bacteriol. 182:6279-6286(2000).
RN [10]
RP FUNCTION.
RX PubMed=11739766; DOI=10.1099/00221287-147-12-3345;
RA Verhamme D.T., Arents J.C., Postma P.W., Crielaard W., Hellingwerf K.J.;
RT "Glucose-6-phosphate-dependent phosphoryl flow through the Uhp two-
RT component regulatory system.";
RL Microbiology 147:3345-3352(2001).
RN [11]
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).
CC -!- FUNCTION: Part of the UhpABC signaling cascade that controls the
CC expression of the hexose phosphate transporter UhpT. UhpC senses
CC external glucose-6-phosphate and interacts with the histidine kinase
CC UhpB, leading to the stimulation of the autokinase activity of UhpB.
CC {ECO:0000269|PubMed:11053370, ECO:0000269|PubMed:11739766,
CC ECO:0000269|PubMed:3038843, ECO:0000269|PubMed:8349544}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Organophosphate:Pi antiporter (OPA) (TC 2.A.1.4) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA24722.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA62019.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; M17102; AAA24722.1; ALT_INIT; Genomic_DNA.
DR EMBL; M89479; AAA24726.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62019.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76690.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77626.1; -; Genomic_DNA.
DR PIR; D65168; RGECUC.
DR RefSeq; NP_418123.2; NC_000913.3.
DR RefSeq; WP_000936566.1; NZ_STEB01000015.1.
DR AlphaFoldDB; P09836; -.
DR SMR; P09836; -.
DR BioGRID; 4262582; 27.
DR STRING; 511145.b3667; -.
DR TCDB; 2.A.1.4.4; the major facilitator superfamily (mfs).
DR PaxDb; P09836; -.
DR PRIDE; P09836; -.
DR EnsemblBacteria; AAC76690; AAC76690; b3667.
DR EnsemblBacteria; BAE77626; BAE77626; BAE77626.
DR GeneID; 948184; -.
DR KEGG; ecj:JW3642; -.
DR KEGG; eco:b3667; -.
DR PATRIC; fig|511145.12.peg.3789; -.
DR EchoBASE; EB1046; -.
DR eggNOG; COG2271; Bacteria.
DR HOGENOM; CLU_001265_31_0_6; -.
DR InParanoid; P09836; -.
DR OMA; NAWFQGW; -.
DR PhylomeDB; P09836; -.
DR BioCyc; EcoCyc:UHPC-MON; -.
DR PRO; PR:P09836; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:EcoliWiki.
DR GO; GO:0016020; C:membrane; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoliWiki.
DR GO; GO:0061513; F:glucose 6-phosphate:inorganic phosphate antiporter activity; IBA:GO_Central.
DR GO; GO:0015760; P:glucose-6-phosphate transport; IBA:GO_Central.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IMP:EcoCyc.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR021159; Sugar-P_transporter_CS.
DR InterPro; IPR000849; Sugar_P_transporter.
DR Pfam; PF07690; MFS_1; 1.
DR PIRSF; PIRSF002808; Hexose_phosphate_transp; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS00942; GLPT; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..439
FT /note="Membrane sensor protein UhpC"
FT /id="PRO_0000199881"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 26..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..66
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 96..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..121
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 122..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..289
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..322
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..349
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..410
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 432..439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
SQ SEQUENCE 439 AA; 48257 MW; D8097864B7877700 CRC64;
MLPFLKAPAD APLMTDKYEI DARYRYWRRH ILLTIWLGYA LFYFTRKSFN AAVPEILANG
VLSRSDIGLL ATLFYITYGV SKFVSGIVSD RSNARYFMGI GLIATGIINI LFGFSTSLWA
FAVLWVLNAF FQGWGSPVCA RLLTAWYSRT ERGGWWALWN TAHNVGGALI PIVMAAAALH
YGWRAGMMIA GCMAIVVGIF LCWRLRDRPQ ALGLPAVGEW RHDALEIAQQ QEGAGLTRKE
ILTKYVLLNP YIWLLSFCYV LVYVVRAAIN DWGNLYMSET LGVDLVTANT AVTMFELGGF
IGALVAGWGS DKLFNGNRGP MNLIFAAGIL LSVGSLWLMP FASYVMQATC FFTIGFFVFG
PQMLIGMAAA ECSHKEAAGA ATGFVGLFAY LGASLAGWPL AKVLDTWHWS GFFVVISIAA
GISALLLLPF LNAQTPREA
