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Conserved domains on  [gi|446464713|ref|WP_000542567|]
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MULTISPECIES: AmiS/UreI family transporter [Bacillus]

Protein Classification

AmiS/UreI family transporter( domain architecture ID 10194154)

AmiS/UreI family transporter similar to putative amide transporters (AmiS of the amidase gene cluster) and Helicobacter pylori acid-activated urea channel (UreI) that functions as a specific, H(+)-activated urea channel that increases the rate of urea entry into the cytoplasm, resulting in activation of cytoplasmic urease at acidic medium pH

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UreI_AmiS_like_2 cd13429
UreI/AmiS family, subgroup 2. Putative transporters related to proton-gated urea channel and ...
 3-166 2.42e-66

UreI/AmiS family, subgroup 2. Putative transporters related to proton-gated urea channel and putative amide transporters; This subfamily includes putative UreI proton-gated urea channels and putative amide transporters (AmiS of the amidase gene cluster). Helicobacter pylori UreI (HpUreI), a proton-gated inner membrane urea channel opens in acidic pH to allow urea influx to the cytoplasm. There urea is metabolized, producing NH3 and Co2, leading to buffering of the periplasm. This action is essential for the survival of H. pylori in the stomach, and has been identified as a mechanism that could be clinically targeted to prevent various illnesses associated with infection by H. pylori. UreI and the related amide channels (AmiS) appear to function as hexamers, and have 6 predicted transmembrane segments. UreI has also been shown have a lipid "plug" in the center of the hexamer. Urea enters at the periplasmic opening of UreI and must pass 2 constriction sites, one on each side of a conserved Glu (Glu 177, H. pylori numbering), to reach the cytoplasm. Urea/thiourea selectivity is diminished by mutation of a conserved Trp to Ala or Phe in constriction site 2 (cytoplasmic). Channel functionality is greatly diminished by mutation of a conserved Trp in constriction site 1 (periplasmic) and a conserved Tyr in constriction site 2, and to a lesser extent a conserved Phe in site 1. In the cytoplasm, urease hydrolyzes urea to form ammonia and carbamate, which decomposes to carbonic acid. UreI is fully open at pH 5.0 to facilitate urea influx, but closes at neutral pH, preventing over-alkalization. Glu 177 (H. pylori numbering) is present in urea channel proteins, but absent in the related amide channels, suggesting that it plays a role in urea specificity.


:

Pssm-ID: 259833  Cd Length: 165  Bit Score: 201.01  E-value: 2.42e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464713   3 YVGLLLSGAALFLNSLVILGKAEMKSAGVFNLFVGALQIIIPFYLIMISDQSNWTVYSYAATFLFGLTYLYVGVTFIKGM 82
Cdd:cd13429    1 NVGLLFVGAVLFINGLVLLGRVDGKSAGVFNLFVGALQVVTPTYLIFQSDGDPWTIFAASGIFLFGFTYLYVGITNLFGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464713  83 DSSGLGWFCIWVAIIALFYMVVSFVQFHDVVNALTWFMWALLWYLFFVLNTQKK-NINQYLGRIAFVQSWVTLTLPSLFY 161
Cdd:cd13429   81 DGSGLGWYSLWVAIIALVYAIVSFGQFADPVFGVIWLSWAYLWFLFFLLLGLGKeNLGPYTGWVAIVQSWITATVPALLI 160


                 ....*
gi 446464713 162 FMGVW 166
Cdd:cd13429  161 LTGSW 165
 
Name Accession Description Interval E-value
UreI_AmiS_like_2 cd13429
UreI/AmiS family, subgroup 2. Putative transporters related to proton-gated urea channel and ...
 3-166 2.42e-66

UreI/AmiS family, subgroup 2. Putative transporters related to proton-gated urea channel and putative amide transporters; This subfamily includes putative UreI proton-gated urea channels and putative amide transporters (AmiS of the amidase gene cluster). Helicobacter pylori UreI (HpUreI), a proton-gated inner membrane urea channel opens in acidic pH to allow urea influx to the cytoplasm. There urea is metabolized, producing NH3 and Co2, leading to buffering of the periplasm. This action is essential for the survival of H. pylori in the stomach, and has been identified as a mechanism that could be clinically targeted to prevent various illnesses associated with infection by H. pylori. UreI and the related amide channels (AmiS) appear to function as hexamers, and have 6 predicted transmembrane segments. UreI has also been shown have a lipid "plug" in the center of the hexamer. Urea enters at the periplasmic opening of UreI and must pass 2 constriction sites, one on each side of a conserved Glu (Glu 177, H. pylori numbering), to reach the cytoplasm. Urea/thiourea selectivity is diminished by mutation of a conserved Trp to Ala or Phe in constriction site 2 (cytoplasmic). Channel functionality is greatly diminished by mutation of a conserved Trp in constriction site 1 (periplasmic) and a conserved Tyr in constriction site 2, and to a lesser extent a conserved Phe in site 1. In the cytoplasm, urease hydrolyzes urea to form ammonia and carbamate, which decomposes to carbonic acid. UreI is fully open at pH 5.0 to facilitate urea influx, but closes at neutral pH, preventing over-alkalization. Glu 177 (H. pylori numbering) is present in urea channel proteins, but absent in the related amide channels, suggesting that it plays a role in urea specificity.


Pssm-ID: 259833  Cd Length: 165  Bit Score: 201.01  E-value: 2.42e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464713   3 YVGLLLSGAALFLNSLVILGKAEMKSAGVFNLFVGALQIIIPFYLIMISDQSNWTVYSYAATFLFGLTYLYVGVTFIKGM 82
Cdd:cd13429    1 NVGLLFVGAVLFINGLVLLGRVDGKSAGVFNLFVGALQVVTPTYLIFQSDGDPWTIFAASGIFLFGFTYLYVGITNLFGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464713  83 DSSGLGWFCIWVAIIALFYMVVSFVQFHDVVNALTWFMWALLWYLFFVLNTQKK-NINQYLGRIAFVQSWVTLTLPSLFY 161
Cdd:cd13429   81 DGSGLGWYSLWVAIIALVYAIVSFGQFADPVFGVIWLSWAYLWFLFFLLLGLGKeNLGPYTGWVAIVQSWITATVPALLI 160


                 ....*
gi 446464713 162 FMGVW 166
Cdd:cd13429  161 LTGSW 165
AmiS_UreI pfam02293
AmiS/UreI family transporter; This family includes UreI and proton gated urea channel as well ...
 1-165 8.09e-53

AmiS/UreI family transporter; This family includes UreI and proton gated urea channel as well as putative amide transporters.


Pssm-ID: 426706  Cd Length: 165  Bit Score: 166.60  E-value: 8.09e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464713    1 MGYVGLLLSGAALFLNSLVILGKAEMKSAGVFNLFVGALQIIIPFYLIMISDQSNWTVYSYAATFLFGLTYLYVGVTFIK 80
Cdd:pfam02293   1 MLGVGLLYVGAVLFLNGLWLLGKIDDRSAAVINLFVGGLQLIINLVLIFGAGADAASIYAAALGLLFGFTYLYVAINRLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464713   81 GMDSSGLGWFCIWVAIIALFYMVVSFVQFHDVVNALTWFMWALLWYLFFVLNTQKKNINQYLGRIAFVQSWVTLTLPSLF 160
Cdd:pfam02293  81 GLDGRGLGWFSLFVAINAVPYALISFTAAGDPWFGVIWLAWAVLWLLFFLLLALKKPIGKFTGWLAIVEGIVTAWIPGFL 160


                  ....*
gi 446464713  161 YFMGV 165
Cdd:pfam02293 161 LLTGV 165
 
Name Accession Description Interval E-value
UreI_AmiS_like_2 cd13429
UreI/AmiS family, subgroup 2. Putative transporters related to proton-gated urea channel and ...
 3-166 2.42e-66

UreI/AmiS family, subgroup 2. Putative transporters related to proton-gated urea channel and putative amide transporters; This subfamily includes putative UreI proton-gated urea channels and putative amide transporters (AmiS of the amidase gene cluster). Helicobacter pylori UreI (HpUreI), a proton-gated inner membrane urea channel opens in acidic pH to allow urea influx to the cytoplasm. There urea is metabolized, producing NH3 and Co2, leading to buffering of the periplasm. This action is essential for the survival of H. pylori in the stomach, and has been identified as a mechanism that could be clinically targeted to prevent various illnesses associated with infection by H. pylori. UreI and the related amide channels (AmiS) appear to function as hexamers, and have 6 predicted transmembrane segments. UreI has also been shown have a lipid "plug" in the center of the hexamer. Urea enters at the periplasmic opening of UreI and must pass 2 constriction sites, one on each side of a conserved Glu (Glu 177, H. pylori numbering), to reach the cytoplasm. Urea/thiourea selectivity is diminished by mutation of a conserved Trp to Ala or Phe in constriction site 2 (cytoplasmic). Channel functionality is greatly diminished by mutation of a conserved Trp in constriction site 1 (periplasmic) and a conserved Tyr in constriction site 2, and to a lesser extent a conserved Phe in site 1. In the cytoplasm, urease hydrolyzes urea to form ammonia and carbamate, which decomposes to carbonic acid. UreI is fully open at pH 5.0 to facilitate urea influx, but closes at neutral pH, preventing over-alkalization. Glu 177 (H. pylori numbering) is present in urea channel proteins, but absent in the related amide channels, suggesting that it plays a role in urea specificity.


Pssm-ID: 259833  Cd Length: 165  Bit Score: 201.01  E-value: 2.42e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464713   3 YVGLLLSGAALFLNSLVILGKAEMKSAGVFNLFVGALQIIIPFYLIMISDQSNWTVYSYAATFLFGLTYLYVGVTFIKGM 82
Cdd:cd13429    1 NVGLLFVGAVLFINGLVLLGRVDGKSAGVFNLFVGALQVVTPTYLIFQSDGDPWTIFAASGIFLFGFTYLYVGITNLFGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464713  83 DSSGLGWFCIWVAIIALFYMVVSFVQFHDVVNALTWFMWALLWYLFFVLNTQKK-NINQYLGRIAFVQSWVTLTLPSLFY 161
Cdd:cd13429   81 DGSGLGWYSLWVAIIALVYAIVSFGQFADPVFGVIWLSWAYLWFLFFLLLGLGKeNLGPYTGWVAIVQSWITATVPALLI 160


                 ....*
gi 446464713 162 FMGVW 166
Cdd:cd13429  161 LTGSW 165
AmiS_UreI pfam02293
AmiS/UreI family transporter; This family includes UreI and proton gated urea channel as well ...
 1-165 8.09e-53

AmiS/UreI family transporter; This family includes UreI and proton gated urea channel as well as putative amide transporters.


Pssm-ID: 426706  Cd Length: 165  Bit Score: 166.60  E-value: 8.09e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464713    1 MGYVGLLLSGAALFLNSLVILGKAEMKSAGVFNLFVGALQIIIPFYLIMISDQSNWTVYSYAATFLFGLTYLYVGVTFIK 80
Cdd:pfam02293   1 MLGVGLLYVGAVLFLNGLWLLGKIDDRSAAVINLFVGGLQLIINLVLIFGAGADAASIYAAALGLLFGFTYLYVAINRLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464713   81 GMDSSGLGWFCIWVAIIALFYMVVSFVQFHDVVNALTWFMWALLWYLFFVLNTQKKNINQYLGRIAFVQSWVTLTLPSLF 160
Cdd:pfam02293  81 GLDGRGLGWFSLFVAINAVPYALISFTAAGDPWFGVIWLAWAVLWLLFFLLLALKKPIGKFTGWLAIVEGIVTAWIPGFL 160


                  ....*
gi 446464713  161 YFMGV 165
Cdd:pfam02293 161 LLTGV 165
UreI_AmiS cd13428
UreI/Amis family, proton-gated urea channel and putative amide transporters; This subfamily ...
 4-166 2.74e-27

UreI/Amis family, proton-gated urea channel and putative amide transporters; This subfamily includes UreI proton-gated urea channels as well as putative amide transporters (AmiS of the amidase gene cluster). Helicobacter pylori UreI (HpUreI), a proton-gated inner membrane urea channel opens in acidic pH to allow urea influx to the cytoplasm. There urea is metabolized, producing NH3 and Co2, leading to buffering of the periplasm. This action is essential for the survival of H. pylori in the stomach, and has been identified as a mechanism that could be clinically targeted to prevent various illnesses associated with infection by H. pylori. UreI and the related amide channels (AmiS) appear to function as hexamers, and have 6 predicted transmembrane segments. UreI has also been shown have a lipid "plug" in the center of the hexamer. Urea enters at the periplasmic opening of UreI and must pass 2 constriction sites, one on each side of a conserved Glu (Glu 177, H. pylori numbering), to reach the cytoplasm. Urea/thiourea selectivity is diminished by mutation of a conserved Trp to Ala or Phe in constriction site 2 (cytoplasmic). Channel functionality is greatly diminished by mutation of a conserved Trp in constriction site 1 (periplasmic) and a conserved Tyr in constriction site 2, and to a lesser extent a conserved Phe in site 1. In the cytoplasm, urease hydrolyzes urea to form ammonia and carbamate, which decomposes to carbonic acid. UreI is fully open at pH 5.0 to facilitate urea influx, but closes at neutral pH, preventing over-alkalization. Glu 177 (H. pylori numbering) is present in urea channel proteins, but absent in the related amide channels, suggesting that it plays a role in urea specificity.


Pssm-ID: 259832  Cd Length: 162  Bit Score: 101.21  E-value: 2.74e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464713   4 VGLLLSGAALFLNSLVILGKAEMKSAGVFNLFVGALQIIIPFYLIMISDQSNWtVYSYAATFLFGLTYLYVGVTFIKGMD 83
Cdd:cd13428    2 VVLLFVGIVLISNGIGGLGKIDPKSTAVMNFFTGGLSLIINIVVLVQGNENTA-YYAAATGLLFAFTYLYVAINNIFGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464713  84 SSGLGWFCIWVAIIALFYMVVSFVQfHDVVNALTWFMWALLWYLFFVLNTQKKNINQYLGRIAFVQSWVTLTLPSLFYFM 163
Cdd:cd13428   81 GRPYGWYCLFVAINTLPCAYISFST-GDMRFAIIWLLWGILWFTGFIELVLKKTLGKFVPYLTIFEGIVTCWIPGFLMLI 159


                 ...
gi 446464713 164 GVW 166
Cdd:cd13428  160 GRW 162
UreI_AmiS_like cd13404
UreI/AmiS family, proton-gated urea channel and putative amide transporters; This family ...
 4-166 3.94e-26

UreI/AmiS family, proton-gated urea channel and putative amide transporters; This family includes UreI proton-gated urea channels as well as putative amide transporters (AmiS of the amidase gene cluster). Helicobacter pylori UreI (HpUreI), a proton-gated inner membrane urea channel opens in acidic pH to allow urea influx to the cytoplasm. There urea is metabolized, producing NH3 and CO2, leading to buffering of the periplasm. This action is essential for the survival of H. pylori in the stomach, and has been identified as a mechanism that could be clinically targeted to prevent various illnesses associated with infection by H. pylori. UreI and the related amide channels (AmiS) appear to function as hexamers, and have 6 predicted transmembrane segments. UreI has also been shown have a lipid "plug" in the center of the hexamer. Urea enters at the periplasmic opening of UreI and must pass 2 constriction sites, one on each side of a conserved Glu (Glu 177, H. pylori numbering), to reach the cytoplasm. Urea/thiourea selectivity is diminished by mutation of a conserved Trp to Ala or Phe in constriction site 2 (cytoplasmic). Channel functionality is greatly diminished by mutation of a conserved Trp in constriction site 1 (periplasmic) and a conserved Tyr in constriction site 2, and to a lesser extent a conserved Phe in site 1. In the cytoplasm, urease hydrolyzes urea to form ammonia and carbamate, which decomposes to carbonic acid. UreI is fully open at pH 5.0 to facilitate urea influx, but closes at neutral pH, preventing over-alkalization. Glu 177 (H. pylori numbering) is present in urea channel proteins, but absent in the related amide channels, suggesting that it plays a role in urea specificity.


Pssm-ID: 259831  Cd Length: 167  Bit Score: 98.36  E-value: 3.94e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464713   4 VGLLLSGAALFLNSLVILGKAEMKSAGVFNLFVGALQIIIPFYLIMISDQSNWTVYSYAATFLFGLTYLYVGVTFIKGMD 83
Cdd:cd13404    2 LGLLYVGAVLFVNGLMLLGKVPVKSASVLNLFVGALQCVVPTVMLIQAQGDSSSVLAAAGLLLFGFTYLYVAINNLAGFD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464713  84 SSGLGWFCIWVAIIALFYMVVSFVQF---HDVVNALTWFMWALLWYLFFVLNTQKKNINQYLGRIAFVQSWVTLTLPSLF 160
Cdd:cd13404   82 PRGIGWYSLFVACAAVPYAFLSFYSLtvsNGPWFGVIWLAWAVLWTLFFLVLGLKEPLSRFTGWLAILEGIPTCWIPAFL 161


                 ....*.
gi 446464713 161 YFMGVW 166
Cdd:cd13404  162 LLTGNF 167
UreI_AmiS_like_1 cd13747
UreI/Amis family, subgroup 1. Putative proton-gated urea channel and putative amide ...
 4-166 1.15e-23

UreI/Amis family, subgroup 1. Putative proton-gated urea channel and putative amide transporters; This subfamily includes putative UreI proton-gated urea channels and putative amide transporters (AmiS of the amidase gene cluster). Helicobacter pylori UreI (HpUreI), a proton-gated inner membrane urea channel opens in acidic pH to allow urea influx to the cytoplasm. There urea is metabolized, producing NH3 and Co2, leading to buffering of the periplasm. This action is essential for the survival of H. pylori in the stomach, and has been identified as a mechanism that could be clinically targeted to prevent various illnesses associated with infection by H. pylori. UreI and the related amide channels (AmiS) appear to function as hexamers, and have 6 predicted transmembrane segments. UreI has also been shown have a lipid "plug" in the center of the hexamer. Urea enters at the periplasmic opening of UreI and must pass 2 constriction sites, one on each side of a conserved Glu (Glu 177, H. pylori numbering), to reach the cytoplasm. Urea/thiourea selectivity is diminished by mutation of a conserved Trp to Ala or Phe in constriction site 2 (cytoplasmic). Channel functionality is greatly diminished by mutation of a conserved Trp in constriction site 1 (periplasmic) and a conserved Tyr in constriction site 2, and to a lesser extent a conserved Phe in site 1. In the cytoplasm, urease hydrolyzes urea to form ammonia and carbamate, which decomposes to carbonic acid. UreI is fully open at pH 5.0 to facilitate urea influx, but closes at neutral pH, preventing over-alkalization. Glu 177 (H. pylori numbering) is present in urea channel proteins, but absent in the related amide channels, suggesting that it plays a role in urea specificity.


Pssm-ID: 259834  Cd Length: 167  Bit Score: 91.99  E-value: 1.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464713   4 VGLLLSGAALFLNSLVILGKAEMKSAGVFNLFVGALQIIIPFYLIMISDQSNWTVYSYAATFLFGLTYLYVGVTFIKGMD 83
Cdd:cd13747    2 LVLLYVGAVLFLNGLWLLGKIDDKEVAVINLFVGILTFIVALYLAFVHGADAISIKAGALTLLFSFTYLWVAINRRVNVD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464713  84 SSGLGWFCIWVAIIALFYMVVSFVQFH---DVVNALTWFMWALLWYLFFVLNTQKKNINQYLGRIAFVQSWVTLTLPSLF 160
Cdd:cd13747   82 GRGLGWYCLFVALTAVPVAINALAGATgdwDIWLGFNWAAWAVLWFLYFLLLVLGRPIQRITGYFTILVGIFTGWIPGLL 161


                 ....*.
gi 446464713 161 YFMGVW 166
Cdd:cd13747  162 LLQGYW 167
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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