UREI_HELPY
ID UREI_HELPY Reviewed; 195 AA.
AC Q09068; Q8VN83; Q8VN86; Q8VN88; Q8VN89; Q9S0Q4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Acid-activated urea channel;
DE AltName: Full=Urease accessory protein UreI;
GN Name=ureI; OrderedLocusNames=HP_0071;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=85P;
RX PubMed=1313413; DOI=10.1128/jb.174.8.2466-2473.1992;
RA Cussac V., Ferrero R.L., Labigne A.;
RT "Expression of Helicobacter pylori urease genes in Escherichia coli grown
RT under nitrogen-limiting conditions.";
RL J. Bacteriol. 174:2466-2473(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HPK5;
RX PubMed=10844692; DOI=10.1046/j.1365-2958.2000.01918.x;
RA Akada J.K., Shirai M., Takeuchi H., Tsuda M., Nakazawa T.;
RT "Identification of the urease operon in Helicobacter pylori and its control
RT by mRNA decay in response to pH.";
RL Mol. Microbiol. 36:1071-1084(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LSU1037-1, LSU1037-5, LSU1062-1, LSU1062-3, LSU2003-1, LSU2003-7,
RC and NQ1712;
RX PubMed=11742075; DOI=10.1073/pnas.251396098;
RA Falush D., Kraft C., Taylor N.S., Correa P., Fox J.G., Achtman M.,
RA Suerbaum S.;
RT "Recombination and mutation during long-term gastric colonization by
RT Helicobacter pylori: estimates of clock rates, recombination size and
RT minimal age.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:15056-15061(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [5]
RP FUNCTION, AND ROLE IN VIRULENCE.
RX PubMed=9712811; DOI=10.1128/iai.66.9.4517-4521.1998;
RA Skouloubris S., Thiberge J.-M., Labigne A., De Reuse H.;
RT "The Helicobacter pylori UreI protein is not involved in urease activity
RT but is essential for bacterial survival in vivo.";
RL Infect. Immun. 66:4517-4521(1998).
RN [6]
RP CHARACTERIZATION, TOPOLOGY, AND MUTAGENESIS OF HIS-123.
RX PubMed=10642549; DOI=10.1126/science.287.5452.482;
RA Weeks D.L., Eskandari S., Scott D.R., Sachs G.;
RT "A H+-gated urea channel: the link between Helicobacter pylori urease and
RT gastric colonization.";
RL Science 287:482-485(2000).
RN [7]
RP FUNCTION, AND MUTAGENESIS.
RX PubMed=11442825; DOI=10.1046/j.1365-2958.2001.02466.x;
RA Weeks D.L., Sachs G.;
RT "Sites of pH regulation of the urea channel of Helicobacter pylori.";
RL Mol. Microbiol. 40:1249-1259(2001).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF HIS-71; HIS-123; HIS-131 AND HIS-193.
RX PubMed=11737644; DOI=10.1046/j.1365-2958.2001.02689.x;
RA Bury-Mone S., Skouloubris S., Labigne A., De Reuse H.;
RT "The Helicobacter pylori UreI protein: role in adaptation to acidity and
RT identification of residues essential for its activity and for acid
RT activation.";
RL Mol. Microbiol. 42:1021-1034(2001).
RN [9]
RP INTERACTION WITH UREASE.
RX PubMed=12388207; DOI=10.1152/ajpgi.00160.2002;
RA Voland P., Weeks D.L., Marcus E.A., Prinz C., Sachs G., Scott D.;
RT "Interactions among the seven Helicobacter pylori proteins encoded by the
RT urease gene cluster.";
RL Am. J. Physiol. 284:G96-G106(2003).
CC -!- FUNCTION: Functions as a specific, H(+)-activated urea channel that
CC increases the rate of urea entry into the cytoplasm, resulting in
CC activation of cytoplasmic urease at acidic medium pH. Is essential for
CC H.pylori gastric survival and colonization. Is necessary for the
CC adaptation of urease activity to the extracellular pH, as in the
CC presence of urea, UreI rapidly enhances the production of ammonia in
CC the extracellular medium when the pH of the medium was decreased to pH5
CC or below. {ECO:0000269|PubMed:11442825, ECO:0000269|PubMed:11737644,
CC ECO:0000269|PubMed:9712811}.
CC -!- SUBUNIT: Forms a membrane complex with the urease UreA/UreB.
CC -!- INTERACTION:
CC Q09068; O34810: HP_1409; NbExp=3; IntAct=EBI-7667832, EBI-7494226;
CC Q09068; O26033: HP_1503; NbExp=3; IntAct=EBI-7667832, EBI-7498734;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: UreI-mediated transport is urea-specific, passive, non-
CC saturable, non-electrogenic, and temperature independent.
CC -!- SIMILARITY: Belongs to the AmiS/UreI family. {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:1313413) thought to be an accessory
CC protein required for nickel incorporation at the urease active site or
CC for nickel transport. Actually, has been shown (PubMed:9712811) not to
CC be required for the assembly of a catalytically active urease.
CC {ECO:0000305|PubMed:1313413, ECO:0000305|PubMed:9712811}.
CC -!- CAUTION: In PubMed:11442825, mutational analysis indicated that His-
CC 123, His-131, and His-193 were important for acid activation of urea
CC uptake in the Xenopus oocytes model, but in H.pylori itself His-193
CC seems to be the only histidine that is crucial for UreI activation at
CC low pH. {ECO:0000305|PubMed:11737644}.
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DR EMBL; M84338; AAA25022.1; -; Genomic_DNA.
DR EMBL; AB032429; BAA84534.1; -; Genomic_DNA.
DR EMBL; AJ418323; CAD11209.1; -; Genomic_DNA.
DR EMBL; AJ418324; CAD11212.1; -; Genomic_DNA.
DR EMBL; AJ418325; CAD11215.1; -; Genomic_DNA.
DR EMBL; AJ418326; CAD11218.1; -; Genomic_DNA.
DR EMBL; AJ418327; CAD11221.1; -; Genomic_DNA.
DR EMBL; AJ418328; CAD11224.1; -; Genomic_DNA.
DR EMBL; AJ418331; CAD11233.1; -; Genomic_DNA.
DR EMBL; AE000511; AAD07134.1; -; Genomic_DNA.
DR PIR; G64528; A41834.
DR RefSeq; NP_206871.1; NC_000915.1.
DR RefSeq; WP_000901247.1; NC_018939.1.
DR AlphaFoldDB; Q09068; -.
DR SMR; Q09068; -.
DR DIP; DIP-3136N; -.
DR IntAct; Q09068; 15.
DR MINT; Q09068; -.
DR STRING; 85962.C694_00340; -.
DR TCDB; 1.A.29.1.3; the urea/amide channel (uac) family.
DR PaxDb; Q09068; -.
DR EnsemblBacteria; AAD07134; AAD07134; HP_0071.
DR KEGG; hpy:HP_0071; -.
DR PATRIC; fig|85962.47.peg.74; -.
DR eggNOG; ENOG50300RH; Bacteria.
DR OMA; FTYLWVA; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 1.25.40.600; -; 1.
DR InterPro; IPR003211; AmiSUreI_transpt.
DR InterPro; IPR038523; AmiSUreI_transpt_sf.
DR Pfam; PF02293; AmiS_UreI; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Virulence.
FT CHAIN 1..195
FT /note="Acid-activated urea channel"
FT /id="PRO_0000067680"
FT TOPO_DOM 1
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:10642549"
FT TRANSMEM 2..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 22..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:10642549"
FT TRANSMEM 34..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..74
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:10642549"
FT TRANSMEM 75..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:10642549"
FT TRANSMEM 104..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..140
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:10642549"
FT TRANSMEM 141..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:10642549"
FT TRANSMEM 172..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..195
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:10642549"
FT VARIANT 42
FT /note="I -> V (in strain: LSU1037-1, LSU1037-5, LSU1062-1,
FT LSU1062-3, LSU2003-1 and LSU2003-7)"
FT VARIANT 45
FT /note="I -> V (in strain: 85P, HPK5, LSU1037-1, LSU1037-5,
FT LSU1062-1, LSU1062-3, LSU2003-1 and LSU2003-7)"
FT VARIANT 47
FT /note="V -> A (in strain: LSU2003-1 and LSU2003-7)"
FT VARIANT 51
FT /note="S -> F (in strain: LSU2003-1 and LSU2003-7)"
FT VARIANT 53
FT /note="L -> V (in strain: LSU2003-7)"
FT VARIANT 54
FT /note="H -> N (in strain: 85P, HPK5 and NQ1712)"
FT VARIANT 66
FT /note="A -> V (in strain: LSU1037-1, LSU1037-5, LSU1062-1,
FT LSU1062-3, LSU2003-1, LSU2003-7 and NQ1712)"
FT VARIANT 74
FT /note="S -> N (in strain: 85P and HPK5)"
FT VARIANT 77
FT /note="G -> E (in strain: HPK5)"
FT VARIANT 94
FT /note="N -> S (in strain: HPK5)"
FT VARIANT 98
FT /note="G -> N (in strain: HPK5)"
FT VARIANT 116
FT /note="I -> V (in strain: LSU1037-1, LSU1037-5, LSU1062-1,
FT LSU1062-3, LSU2003-1 and LSU2003-7)"
FT VARIANT 171
FT /note="P -> L (in strain: LSU1037-1)"
FT MUTAGEN 71
FT /note="H->G: No loss of acid activation of urea uptake."
FT /evidence="ECO:0000269|PubMed:11737644"
FT MUTAGEN 123
FT /note="H->R,G: No loss of acid activation of urea uptake;
FT when expressed in H.pylori itself. Opposite result; when
FT expressed in the Xenopus oocytes model."
FT /evidence="ECO:0000269|PubMed:10642549,
FT ECO:0000269|PubMed:11737644"
FT MUTAGEN 131
FT /note="H->G: No loss of acid activation of urea uptake."
FT /evidence="ECO:0000269|PubMed:11737644"
FT MUTAGEN 193
FT /note="H->G: Loss of acid activation of urea uptake."
FT /evidence="ECO:0000269|PubMed:11737644"
SQ SEQUENCE 195 AA; 21706 MW; 6A8F3E621CB2B37C CRC64;
MLGLVLLYVG IVLISNGICG LTKVDPKSTA VMNFFVGGLS IICNIVVITY SALHPTAPVE
GAEDIAQVSH HLTSFYGPAT GLLFGFTYLY AAINHTFGLD WRPYSWYSLF VAINTIPAAI
LSHYSDMLDD HKVLGITEGD WWAIIWLAWG VLWLTAFIEN ILKIPLGKFT PWLAIIEGIL
TAWIPAWLLF IQHWV
