NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|917529207|ref|WP_052135624|]
View 

porin [Burkholderia pseudomallei]

Protein Classification

porin( domain architecture ID 10085924)

porin forming an aqueous channel for the diffusion of small hydrophilic molecules across the outer membrane, similar to outer membrane protein P2

Gene Ontology:  GO:0009279|GO:0015288
PubMed:  31214985|31792365
TCDB:  1.B.1

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
gram_neg_porins cd00342
Porins form aqueous channels for the diffusion of small hydrophillic molecules across the ...
 31-192 8.84e-17

Porins form aqueous channels for the diffusion of small hydrophillic molecules across the outer membrane. Individual 16-strand anti-parallel beta-barrels form a central pore, and trimerizes thru mainly hydrophobic interactions at the interface. Trimers are stabilized by hytrophillic clamping of Loop L2. Loop 3 bends into the pore, creating an elliptical constriction of about 7 x 11A, large enough to allow passage of a glucose molecule without steric hindrance. Removal of the C-terminal residue (usuallly F) destabilizes the trimer and removal of the 16th beta-sheet abolishes trimerization. Unlike typical membrane proteins, porins lack long hydrophobic stretches. Short turns are found at the smooth, periplasmic end, longer irregular loops are found at the rough, extracellular end. C-terminal residue forms salt bridge with N-terminus.


:

Pssm-ID: 238208 [Multi-domain]  Cd Length: 329  Bit Score: 76.64  E-value: 8.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917529207  31 GAVTGDNTFDASSQQNVGIGATYAFSKALIGFAYSHVDVYDPTSNayftgttrpagehwQSWKFDHFEINGRYRVTPAFY 110
Cdd:cd00342  187 GGGAAGGAAGATSQRAYGAGASYDFGGLKLGAGYTNTRNDNGGGG--------------GSAKFNGYELGATYQLTPALR 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917529207 111 AGAAYTYTQARADSTAGafhPKWRPLSTKLDYDLSKRSSGFAEGVYQHAQHAMNARtgtdfdhayIPGAANIASGPNQYV 190
Cdd:cd00342  253 LGAAYYYTKDRNDGGGD---GKANQVALGADYALSKRTDLYAEYGYQKNSGGASTG---------LAGGGGPSSGNNQDG 320


                 ..
gi 917529207 191 VR 192
Cdd:cd00342  321 VA 322
 
Name Accession Description Interval E-value
gram_neg_porins cd00342
Porins form aqueous channels for the diffusion of small hydrophillic molecules across the ...
 31-192 8.84e-17

Porins form aqueous channels for the diffusion of small hydrophillic molecules across the outer membrane. Individual 16-strand anti-parallel beta-barrels form a central pore, and trimerizes thru mainly hydrophobic interactions at the interface. Trimers are stabilized by hytrophillic clamping of Loop L2. Loop 3 bends into the pore, creating an elliptical constriction of about 7 x 11A, large enough to allow passage of a glucose molecule without steric hindrance. Removal of the C-terminal residue (usuallly F) destabilizes the trimer and removal of the 16th beta-sheet abolishes trimerization. Unlike typical membrane proteins, porins lack long hydrophobic stretches. Short turns are found at the smooth, periplasmic end, longer irregular loops are found at the rough, extracellular end. C-terminal residue forms salt bridge with N-terminus.


Pssm-ID: 238208 [Multi-domain]  Cd Length: 329  Bit Score: 76.64  E-value: 8.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917529207  31 GAVTGDNTFDASSQQNVGIGATYAFSKALIGFAYSHVDVYDPTSNayftgttrpagehwQSWKFDHFEINGRYRVTPAFY 110
Cdd:cd00342  187 GGGAAGGAAGATSQRAYGAGASYDFGGLKLGAGYTNTRNDNGGGG--------------GSAKFNGYELGATYQLTPALR 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917529207 111 AGAAYTYTQARADSTAGafhPKWRPLSTKLDYDLSKRSSGFAEGVYQHAQHAMNARtgtdfdhayIPGAANIASGPNQYV 190
Cdd:cd00342  253 LGAAYYYTKDRNDGGGD---GKANQVALGADYALSKRTDLYAEYGYQKNSGGASTG---------LAGGGGPSSGNNQDG 320


                 ..
gi 917529207 191 VR 192
Cdd:cd00342  321 VA 322
OmpC COG3203
Outer membrane porin OmpC/OmpF/PhoE [Cell wall/membrane/envelope biogenesis];
34-170 8.09e-10

Outer membrane porin OmpC/OmpF/PhoE [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442436 [Multi-domain]  Cd Length: 336  Bit Score: 56.94  E-value: 8.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917529207  34 TGDNTFDASSQQNVGIGATYAFSKALIGFAYSHVDVYDPTSNAyftgttrpagehwqSWKFDHFEINGRYRVTPAFYAGA 113
Cdd:COG3203  204 AQGATAGGDDADAWGLGASYDFGNLKLAAGYGQTKNDDAGGAG--------------NAKADGYELGASYPFGPALTLSA 269

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 917529207 114 AYTYTQARADSTAGafhpKWRPLSTKLDYDLSKRSSGFAEGVYQHAQHAMNARTGTD 170
Cdd:COG3203  270 SYGYTDAKDGADDD----DANQYALGADYALSKRTSLYAEYGYNDNDGNANFTAAAG 322
 
Name Accession Description Interval E-value
gram_neg_porins cd00342
Porins form aqueous channels for the diffusion of small hydrophillic molecules across the ...
 31-192 8.84e-17

Porins form aqueous channels for the diffusion of small hydrophillic molecules across the outer membrane. Individual 16-strand anti-parallel beta-barrels form a central pore, and trimerizes thru mainly hydrophobic interactions at the interface. Trimers are stabilized by hytrophillic clamping of Loop L2. Loop 3 bends into the pore, creating an elliptical constriction of about 7 x 11A, large enough to allow passage of a glucose molecule without steric hindrance. Removal of the C-terminal residue (usuallly F) destabilizes the trimer and removal of the 16th beta-sheet abolishes trimerization. Unlike typical membrane proteins, porins lack long hydrophobic stretches. Short turns are found at the smooth, periplasmic end, longer irregular loops are found at the rough, extracellular end. C-terminal residue forms salt bridge with N-terminus.


Pssm-ID: 238208 [Multi-domain]  Cd Length: 329  Bit Score: 76.64  E-value: 8.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917529207  31 GAVTGDNTFDASSQQNVGIGATYAFSKALIGFAYSHVDVYDPTSNayftgttrpagehwQSWKFDHFEINGRYRVTPAFY 110
Cdd:cd00342  187 GGGAAGGAAGATSQRAYGAGASYDFGGLKLGAGYTNTRNDNGGGG--------------GSAKFNGYELGATYQLTPALR 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917529207 111 AGAAYTYTQARADSTAGafhPKWRPLSTKLDYDLSKRSSGFAEGVYQHAQHAMNARtgtdfdhayIPGAANIASGPNQYV 190
Cdd:cd00342  253 LGAAYYYTKDRNDGGGD---GKANQVALGADYALSKRTDLYAEYGYQKNSGGASTG---------LAGGGGPSSGNNQDG 320


                 ..
gi 917529207 191 VR 192
Cdd:cd00342  321 VA 322
OmpC COG3203
Outer membrane porin OmpC/OmpF/PhoE [Cell wall/membrane/envelope biogenesis];
34-170 8.09e-10

Outer membrane porin OmpC/OmpF/PhoE [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442436 [Multi-domain]  Cd Length: 336  Bit Score: 56.94  E-value: 8.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917529207  34 TGDNTFDASSQQNVGIGATYAFSKALIGFAYSHVDVYDPTSNAyftgttrpagehwqSWKFDHFEINGRYRVTPAFYAGA 113
Cdd:COG3203  204 AQGATAGGDDADAWGLGASYDFGNLKLAAGYGQTKNDDAGGAG--------------NAKADGYELGASYPFGPALTLSA 269

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 917529207 114 AYTYTQARADSTAGafhpKWRPLSTKLDYDLSKRSSGFAEGVYQHAQHAMNARTGTD 170
Cdd:COG3203  270 SYGYTDAKDGADDD----DANQYALGADYALSKRTSLYAEYGYNDNDGNANFTAAAG 322
FepA COG4771
Outer membrane receptor for ferrienterochelin and colicins [Inorganic ion transport and ...
 97-175 3.90e-03

Outer membrane receptor for ferrienterochelin and colicins [Inorganic ion transport and metabolism];


Pssm-ID: 443803 [Multi-domain]  Cd Length: 612  Bit Score: 37.53  E-value: 3.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917529207  97 FEINGRYRVTPAFYAGAAYTYTQARADSTAG----AFHPKWRpLSTKLDYDLSKRSSGFAEGVYQHAQHAMNARTGTDFD 172
Cdd:COG4771  512 LELELKYRLGKGLTLTASYTYLDSKIDDGDTgeplPNVPPHK-ANLGLDYRLPKWWLLLLLTRYYGGRYVTPPSGRLEGY 590


                 ...
gi 917529207 173 HAY 175
Cdd:COG4771  591 TPG 593
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH