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UREI_HELPJ
ID   UREI_HELPJ              Reviewed;         195 AA.
AC   P56874;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Acid-activated urea channel;
DE   AltName: Full=Urease accessory protein UreI;
GN   Name=ureI; OrderedLocusNames=jhp_0066;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a membrane complex with the urease UreA/UreB.
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       P56874; P56874: ureI; NbExp=2; IntAct=EBI-16027017, EBI-16027017;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AmiS/UreI family. {ECO:0000305}.
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DR   EMBL; AE001439; AAD05637.1; -; Genomic_DNA.
DR   PIR; F71979; F71979.
DR   RefSeq; WP_000901274.1; NZ_CP011330.1.
DR   PDB; 3UX4; X-ray; 3.26 A; A/B/C=1-195.
DR   PDB; 6NSJ; EM; 2.70 A; A/B/C/D/E/F=1-195.
DR   PDB; 6NSK; EM; 2.70 A; A/B/C/D/E/F=1-195.
DR   PDBsum; 3UX4; -.
DR   PDBsum; 6NSJ; -.
DR   PDBsum; 6NSK; -.
DR   AlphaFoldDB; P56874; -.
DR   SMR; P56874; -.
DR   DIP; DIP-60123N; -.
DR   STRING; 85963.jhp_0066; -.
DR   EnsemblBacteria; AAD05637; AAD05637; jhp_0066.
DR   GeneID; 66521328; -.
DR   KEGG; hpj:jhp_0066; -.
DR   PATRIC; fig|85963.30.peg.968; -.
DR   OMA; FTYLWVA; -.
DR   Proteomes; UP000000804; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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   3D-structure; Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..195
FT                   /note="Acid-activated urea channel"
FT                   /id="PRO_0000067681"
FT   TOPO_DOM        1
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        22..33
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        34..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        54..74
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        75..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        94..103
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        123..140
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        159..171
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        192..195
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   HELIX           2..19
FT                   /evidence="ECO:0007829|PDB:6NSJ"
FT   TURN            20..23
FT                   /evidence="ECO:0007829|PDB:6NSJ"
FT   HELIX           26..53
FT                   /evidence="ECO:0007829|PDB:6NSJ"
FT   STRAND          71..74
FT                   /evidence="ECO:0007829|PDB:6NSJ"
FT   HELIX           76..96
FT                   /evidence="ECO:0007829|PDB:6NSJ"
FT   HELIX           102..124
FT                   /evidence="ECO:0007829|PDB:6NSJ"
FT   STRAND          135..137
FT                   /evidence="ECO:0007829|PDB:3UX4"
FT   HELIX           138..160
FT                   /evidence="ECO:0007829|PDB:6NSJ"
FT   HELIX           169..180
FT                   /evidence="ECO:0007829|PDB:6NSJ"
FT   TURN            181..183
FT                   /evidence="ECO:0007829|PDB:6NSJ"
FT   HELIX           184..191
FT                   /evidence="ECO:0007829|PDB:6NSJ"
SQ   SEQUENCE   195 AA;  21692 MW;  296955CDCF7C54F8 CRC64;
     MLGLVLLYVG IVLISNGICG LTKVDPKSTA VMNFFVGGLS IVCNVVVITY SALHPTAPVE
     GAEDIVQVSH HLTSFYGPAT GLLFGFTYLY AAINHTFGLD WRPYSWYSLF VAINTVPAAI
     LSHYSDMLDD HKVLGITEGD WWAIIWLAWG VLWLTAFIEN ILKIPLGKFT PWLAIIEGIL
     TAWIPAWLLF IQHWV
 
 
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