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Conserved domains on  [gi|446451200|ref|WP_000529055|]
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Bax inhibitor-1 family protein [Salmonella enterica]

Protein Classification

Bax inhibitor 1 family protein( domain architecture ID 1847)

Bax inhibitor 1 family protein similar to Saccharomyces cerevisiae Bax inhibitor 1 that links the unfolded protein response and programmed cell death, and mediates mitochondrial-dependent apoptosis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BI-1-like super family cl00473
BAX inhibitor (BI)-1/YccA-like protein family; Mammalian members of the BAX inhibitor (BI)-1 ...
 23-213 2.62e-14

BAX inhibitor (BI)-1/YccA-like protein family; Mammalian members of the BAX inhibitor (BI)-1 like family of small transmembrane proteins have been shown to have an antiapoptotic effect either by stimulating the antiapoptotic function of Bcl-2, a well-characterized oncogene, or by inhibiting the proapoptotic effect of Bax, another member of the Bcl-2 family. Their broad tissue distribution and high degree of conservation suggests an important regulatory role. This superfamily also contains the lifeguard(LFG)-like proteins and other subfamilies which appear to be related by common descent and also function as inhibitors of apoptosis. In plants, BI-1 like proteins play a role in pathogen resistance. A prokaryotic member, Escherichia coli YccA, has been shown to interact with ATP-dependent protease FtsH, which degrades abnormal membrane proteins as part of a quality control mechanism to keep the integrity of biological membranes.


The actual alignment was detected with superfamily member cd10432:

Pssm-ID: 469783  Cd Length: 211  Bit Score: 69.13  E-value: 2.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451200  23 TYWYTALGLWCTAGIIWLTLYTHFLITHVQPVVVLWISALLLGLGYGAITCLSRFGTVVATLIYIAIITLTGVSLAYLFS 102
Cdd:cd10432    9 VYGLMAAGLLLTAVGAYVGASTPALLLIAGSPLMWVLLIAELALVFGLSFRINKMSVATALPLFFAFAALTGLTLSPILL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451200 103 -----SGATIFVIVGIMFSLNALFIFYLNISSGLFRPLIFMAVSGIIAAIVVNSLVASSTMVWIVSMLTVLVWTLITALE 177
Cdd:cd10432   89 vytgaSIAQAFFTTAATFGGLSLYGYTTKKDLSFLGSFLFMGLIGLIIASLVNIFLQSSALQFAISAIGVLIFSGLIAYD 168

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446451200 178 KSTLhdyARMLYRSEFSSLSRCALFGALTLYLGIIN 213
Cdd:cd10432  169 TQRI---KRMYEAGGGESGYKDAIMGALSLYLDFIN 201
 
Name Accession Description Interval E-value
BI-1-like_bacterial cd10432
Bacterial BAX inhibitor (BI)-1/YccA-like proteins; This family is comprised of bacterial ...
 23-213 2.62e-14

Bacterial BAX inhibitor (BI)-1/YccA-like proteins; This family is comprised of bacterial relatives of the mammalian members of the BAX inhibitor (BI)-1 like family of small transmembrane proteins, which have been shown to have an antiapoptotic effect either by stimulating the antiapoptotic function of Bcl-2, a well-characterized oncogene, or by inhibiting the proapoptotic effect of Bax, another member of the Bcl-2 family. In plants, BI-1 like proteins play a role in pathogen resistance. A characterized prokaryotic member, Escherichia coli YccA, has been shown to interact with ATP-dependent protease FtsH, which degrades abnormal membrane proteins as part of a quality control mechanism to keep the integrity of biological membranes.


Pssm-ID: 198414  Cd Length: 211  Bit Score: 69.13  E-value: 2.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451200  23 TYWYTALGLWCTAGIIWLTLYTHFLITHVQPVVVLWISALLLGLGYGAITCLSRFGTVVATLIYIAIITLTGVSLAYLFS 102
Cdd:cd10432    9 VYGLMAAGLLLTAVGAYVGASTPALLLIAGSPLMWVLLIAELALVFGLSFRINKMSVATALPLFFAFAALTGLTLSPILL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451200 103 -----SGATIFVIVGIMFSLNALFIFYLNISSGLFRPLIFMAVSGIIAAIVVNSLVASSTMVWIVSMLTVLVWTLITALE 177
Cdd:cd10432   89 vytgaSIAQAFFTTAATFGGLSLYGYTTKKDLSFLGSFLFMGLIGLIIASLVNIFLQSSALQFAISAIGVLIFSGLIAYD 168

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446451200 178 KSTLhdyARMLYRSEFSSLSRCALFGALTLYLGIIN 213
Cdd:cd10432  169 TQRI---KRMYEAGGGESGYKDAIMGALSLYLDFIN 201
Bax1-I pfam01027
Inhibitor of apoptosis-promoting Bax1; Programmed cell-death involves a set of Bcl-2 family ...
 20-220 1.97e-12

Inhibitor of apoptosis-promoting Bax1; Programmed cell-death involves a set of Bcl-2 family proteins, some of which inhibit apoptosis (Bcl-2 and Bcl-XL) and some of which promote it (Bax and Bak). Human Bax inhibitor, BI-1, is an evolutionarily conserved integral membrane protein containing multiple membrane-spanning segments predominantly localized to intracellular membranes. It has 6-7 membrane-spanning domains. The C termini of the mammalian BI-1 proteins are comprised of basic amino acids resembling some nuclear targeting sequences, but otherwise the predicted proteins lack motifs that suggest a function. As plant BI-1 appears to localize predominantly to the ER, we hypothesized that plant BI-1 could also regulate cell death triggered by ER stress. BI-1 appears to exert its effect through an interaction with calmodulin. The budding yeast member of this family has been found unexpectedly to encode a BH3 domain-containing protein (Ybh3p) that regulates the mitochondrial pathway of apoptosis in a phylogenetically conserved manner. Examination of the crystal structure of a bacterial member of this family shows that these proteins mediate a calcium leak across the membrane that is pH-dependent. Calcium homoeostasis balances passive calcium leak with active calcium uptake. The structure exists in a pore-closed and pore-open conformation, at pHs of 8 and 6 respectively, and the pore can be opened by intracrystalline transition; together these findings suggest that pH controls the conformational transition.


Pssm-ID: 460029  Cd Length: 207  Bit Score: 64.12  E-value: 1.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451200   20 LSLTYWYTALGLWCTAGIIWLTLYT---HFLITHVQPVVVLWISALLLGLGYGAITCLSRFGTVVATLIYIAIITLTGVS 96
Cdd:pfam01027   4 LRKVYGLLALGLLLTAAVAYLVLSSpalLFPSLHPPLFWVLIIAPLGLLFGALLLARKRKYSSNVALLLLLAFTLLMGLT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451200   97 LAYLFSSG-----ATIFVIVGIMFSLNALFIFYLNISSGLFRPLIFMAVSGIIAAIVVNSLVASSTMVWIVSMLTVLVWT 171
Cdd:pfam01027  84 LGPLLLVYtgaiiATAFLGTAAIFGGLSLYALTTKRDLSFLGGFLFAGLIGLIVASLVNIFLPSSALSLAISYLGVLLFS 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 446451200  172 LITALEKSTLHDYARMLYrsefsslSRCALFGALTLYLGIINAVVTLCR 220
Cdd:pfam01027 164 GFILYDTQRIIKRYGEYG-------DYDAILAALSLYLDFINLFLSLLR 205
YbhL COG0670
Integral membrane protein YbhL, putative Ca2+ regulator, Bax inhibitor (BI-1)/TMBIM family ...
 23-213 2.17e-06

Integral membrane protein YbhL, putative Ca2+ regulator, Bax inhibitor (BI-1)/TMBIM family [Inorganic ion transport and metabolism];


Pssm-ID: 440434  Cd Length: 231  Bit Score: 47.10  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451200  23 TYWYTALGLWCTAGIIWLTLYTHFLITHVQPVVVLWISALL--LGLGYGAITCLSRFGTVVATLIYIAIITLTGVSLAYL 100
Cdd:COG0670   26 TYGLLALGLLLTALVAYLGMALPGLAALLFGSPGLFWVLLIapLGLVFLLSKLANRANSAAALALLFAYTALMGLTLSPI 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451200 101 F---------SSGATIFVIVGIMFSLNALFIFYLNISSGLFRPLIFMAVSGIIAAIVVNSLVASSTMVWIVSMLTVLVWT 171
Cdd:COG0670  106 LlvytglsgpASIAQAFGGTAATFGGLSLYGYTTKRDLSFLGSFLFMGLIGLIIASLVNIFLQSPALSLAISVAGVLLFS 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446451200 172 LITALEKSTLhdyaRMLYRSefsslSRCALFGALTLYLGIIN 213
Cdd:COG0670  186 GLTLYDTQRI----KHGYET-----NKQYIMAALSLYLDFIN 218
 
Name Accession Description Interval E-value
BI-1-like_bacterial cd10432
Bacterial BAX inhibitor (BI)-1/YccA-like proteins; This family is comprised of bacterial ...
 23-213 2.62e-14

Bacterial BAX inhibitor (BI)-1/YccA-like proteins; This family is comprised of bacterial relatives of the mammalian members of the BAX inhibitor (BI)-1 like family of small transmembrane proteins, which have been shown to have an antiapoptotic effect either by stimulating the antiapoptotic function of Bcl-2, a well-characterized oncogene, or by inhibiting the proapoptotic effect of Bax, another member of the Bcl-2 family. In plants, BI-1 like proteins play a role in pathogen resistance. A characterized prokaryotic member, Escherichia coli YccA, has been shown to interact with ATP-dependent protease FtsH, which degrades abnormal membrane proteins as part of a quality control mechanism to keep the integrity of biological membranes.


Pssm-ID: 198414  Cd Length: 211  Bit Score: 69.13  E-value: 2.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451200  23 TYWYTALGLWCTAGIIWLTLYTHFLITHVQPVVVLWISALLLGLGYGAITCLSRFGTVVATLIYIAIITLTGVSLAYLFS 102
Cdd:cd10432    9 VYGLMAAGLLLTAVGAYVGASTPALLLIAGSPLMWVLLIAELALVFGLSFRINKMSVATALPLFFAFAALTGLTLSPILL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451200 103 -----SGATIFVIVGIMFSLNALFIFYLNISSGLFRPLIFMAVSGIIAAIVVNSLVASSTMVWIVSMLTVLVWTLITALE 177
Cdd:cd10432   89 vytgaSIAQAFFTTAATFGGLSLYGYTTKKDLSFLGSFLFMGLIGLIIASLVNIFLQSSALQFAISAIGVLIFSGLIAYD 168

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446451200 178 KSTLhdyARMLYRSEFSSLSRCALFGALTLYLGIIN 213
Cdd:cd10432  169 TQRI---KRMYEAGGGESGYKDAIMGALSLYLDFIN 201
Bax1-I pfam01027
Inhibitor of apoptosis-promoting Bax1; Programmed cell-death involves a set of Bcl-2 family ...
 20-220 1.97e-12

Inhibitor of apoptosis-promoting Bax1; Programmed cell-death involves a set of Bcl-2 family proteins, some of which inhibit apoptosis (Bcl-2 and Bcl-XL) and some of which promote it (Bax and Bak). Human Bax inhibitor, BI-1, is an evolutionarily conserved integral membrane protein containing multiple membrane-spanning segments predominantly localized to intracellular membranes. It has 6-7 membrane-spanning domains. The C termini of the mammalian BI-1 proteins are comprised of basic amino acids resembling some nuclear targeting sequences, but otherwise the predicted proteins lack motifs that suggest a function. As plant BI-1 appears to localize predominantly to the ER, we hypothesized that plant BI-1 could also regulate cell death triggered by ER stress. BI-1 appears to exert its effect through an interaction with calmodulin. The budding yeast member of this family has been found unexpectedly to encode a BH3 domain-containing protein (Ybh3p) that regulates the mitochondrial pathway of apoptosis in a phylogenetically conserved manner. Examination of the crystal structure of a bacterial member of this family shows that these proteins mediate a calcium leak across the membrane that is pH-dependent. Calcium homoeostasis balances passive calcium leak with active calcium uptake. The structure exists in a pore-closed and pore-open conformation, at pHs of 8 and 6 respectively, and the pore can be opened by intracrystalline transition; together these findings suggest that pH controls the conformational transition.


Pssm-ID: 460029  Cd Length: 207  Bit Score: 64.12  E-value: 1.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451200   20 LSLTYWYTALGLWCTAGIIWLTLYT---HFLITHVQPVVVLWISALLLGLGYGAITCLSRFGTVVATLIYIAIITLTGVS 96
Cdd:pfam01027   4 LRKVYGLLALGLLLTAAVAYLVLSSpalLFPSLHPPLFWVLIIAPLGLLFGALLLARKRKYSSNVALLLLLAFTLLMGLT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451200   97 LAYLFSSG-----ATIFVIVGIMFSLNALFIFYLNISSGLFRPLIFMAVSGIIAAIVVNSLVASSTMVWIVSMLTVLVWT 171
Cdd:pfam01027  84 LGPLLLVYtgaiiATAFLGTAAIFGGLSLYALTTKRDLSFLGGFLFAGLIGLIVASLVNIFLPSSALSLAISYLGVLLFS 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 446451200  172 LITALEKSTLHDYARMLYrsefsslSRCALFGALTLYLGIINAVVTLCR 220
Cdd:pfam01027 164 GFILYDTQRIIKRYGEYG-------DYDAILAALSLYLDFINLFLSLLR 205
YbhL COG0670
Integral membrane protein YbhL, putative Ca2+ regulator, Bax inhibitor (BI-1)/TMBIM family ...
 23-213 2.17e-06

Integral membrane protein YbhL, putative Ca2+ regulator, Bax inhibitor (BI-1)/TMBIM family [Inorganic ion transport and metabolism];


Pssm-ID: 440434  Cd Length: 231  Bit Score: 47.10  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451200  23 TYWYTALGLWCTAGIIWLTLYTHFLITHVQPVVVLWISALL--LGLGYGAITCLSRFGTVVATLIYIAIITLTGVSLAYL 100
Cdd:COG0670   26 TYGLLALGLLLTALVAYLGMALPGLAALLFGSPGLFWVLLIapLGLVFLLSKLANRANSAAALALLFAYTALMGLTLSPI 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451200 101 F---------SSGATIFVIVGIMFSLNALFIFYLNISSGLFRPLIFMAVSGIIAAIVVNSLVASSTMVWIVSMLTVLVWT 171
Cdd:COG0670  106 LlvytglsgpASIAQAFGGTAATFGGLSLYGYTTKRDLSFLGSFLFMGLIGLIIASLVNIFLQSPALSLAISVAGVLLFS 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446451200 172 LITALEKSTLhdyaRMLYRSefsslSRCALFGALTLYLGIIN 213
Cdd:COG0670  186 GLTLYDTQRI----KHGYET-----NKQYIMAALSLYLDFIN 218
 
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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