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Conserved domains on  [gi|16131854|ref|NP_418452|]
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capsule biosynthesis GfcC family protein YjbG [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

capsule biosynthesis GfcC family protein( domain architecture ID 12069186)

capsule biosynthesis GfcC family protein similar to Escherichia coli GfcC, a periplasmic protein that is essential for assembly of group 4 polysaccharide capsule (O-antigen capsule)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Caps_syn_GfcC_C pfam06251
Capsule biosynthesis GfcC C-terminal; Many bacteria are covered in a layer of ...
 155-244 2.28e-51

Capsule biosynthesis GfcC C-terminal; Many bacteria are covered in a layer of surface-associated polysaccharide called the capsule. These capsules can be divided into four groups depending upon the organization of genes responsible for capsule assembly, the assembly pathway and regulation. This family plays a role in group 4 capsule biosynthesis. These proteins have a beta-grasp fold. Two beta-grasp domains, D2 and D3, are arranged in tandem. There is a C-terminal amphipathic helix which packs against D3. A helical hairpin insert in D2 binds to D3 and constrains its position, a conserved arginine residue at the end of this hairpin is essential for structural integrity. This is the C-terminal domain which covers D3 and D4 domains.


:

Pssm-ID: 461862  Cd Length: 90  Bit Score: 162.25  E-value: 2.28e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131854   155 RPGKQPFTPGRDVASYLSDQSLLSGADRSYAWVVYPDGRTQKAPVAYWNKRHVEPMPGSIIYVGLADSVWSETPDALNAD 234
Cdd:pfam06251   1 QSGSVPFLPGRSVADYLDDQPLLSGADRSYVYVIYPDGRTQKAPVALWNKRHVEPMPGSTIFVGFSPSVLPEDYSSLNEQ 80

                          90
                  ....*....|
gi 16131854   235 ILQTLTQRIP 244
Cdd:pfam06251  81 IVQLLTNRIP 90
Caps_syn_GfcC_N pfam20616
Capsule biosynthesis GfcC, N-terminal; Many bacteria are covered in a layer of ...
 20-143 7.20e-50

Capsule biosynthesis GfcC, N-terminal; Many bacteria are covered in a layer of surface-associated polysaccharide called the capsule. These capsules can be divided into four groups depending upon the organization of genes responsible for capsule assembly, the assembly pathway and regulation. This family plays a role in group 4 capsule biosynthesis. These proteins have a beta-grasp fold. Two beta-grasp domains, D2 and D3, are arranged in tandem. There is a C-terminal amphipathic helix which packs against D3. A helical hairpin insert in D2 binds to D3 and constrains its position, a conserved arginine residue at the end of this hairpin is essential for structural integrity. This entry represents D2 domain found at the N-terminal.


:

Pssm-ID: 466765  Cd Length: 129  Bit Score: 159.59  E-value: 7.20e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131854    20 AAGTVKVFSNGSSEAKTLTGAEHLIDLVGQP-RLANSWWPGAVISEELATAAALRQQQALLTRLAEQGADSSADD----A 94
Cdd:pfam20616   1 AQGTVSVFLPGESEVLTLTDAERLEQLVGQPqLLANSWWPGAVISDEAATQKALKQRQVLLAQLASLSAEWLFSAdgdlA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 16131854    95 AAINALRQQIQALKVTGRQKINLDPDIVRVAERGNPPLQGNYTLWVGPP 143
Cdd:pfam20616  81 AAINQLRQQLQNLNVTGRIFVNLDPDVVRVDERSNPPLVGDYQLYVAPR 129
 
Name Accession Description Interval E-value
Caps_syn_GfcC_C pfam06251
Capsule biosynthesis GfcC C-terminal; Many bacteria are covered in a layer of ...
 155-244 2.28e-51

Capsule biosynthesis GfcC C-terminal; Many bacteria are covered in a layer of surface-associated polysaccharide called the capsule. These capsules can be divided into four groups depending upon the organization of genes responsible for capsule assembly, the assembly pathway and regulation. This family plays a role in group 4 capsule biosynthesis. These proteins have a beta-grasp fold. Two beta-grasp domains, D2 and D3, are arranged in tandem. There is a C-terminal amphipathic helix which packs against D3. A helical hairpin insert in D2 binds to D3 and constrains its position, a conserved arginine residue at the end of this hairpin is essential for structural integrity. This is the C-terminal domain which covers D3 and D4 domains.


Pssm-ID: 461862  Cd Length: 90  Bit Score: 162.25  E-value: 2.28e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131854   155 RPGKQPFTPGRDVASYLSDQSLLSGADRSYAWVVYPDGRTQKAPVAYWNKRHVEPMPGSIIYVGLADSVWSETPDALNAD 234
Cdd:pfam06251   1 QSGSVPFLPGRSVADYLDDQPLLSGADRSYVYVIYPDGRTQKAPVALWNKRHVEPMPGSTIFVGFSPSVLPEDYSSLNEQ 80

                          90
                  ....*....|
gi 16131854   235 ILQTLTQRIP 244
Cdd:pfam06251  81 IVQLLTNRIP 90
Caps_syn_GfcC_N pfam20616
Capsule biosynthesis GfcC, N-terminal; Many bacteria are covered in a layer of ...
 20-143 7.20e-50

Capsule biosynthesis GfcC, N-terminal; Many bacteria are covered in a layer of surface-associated polysaccharide called the capsule. These capsules can be divided into four groups depending upon the organization of genes responsible for capsule assembly, the assembly pathway and regulation. This family plays a role in group 4 capsule biosynthesis. These proteins have a beta-grasp fold. Two beta-grasp domains, D2 and D3, are arranged in tandem. There is a C-terminal amphipathic helix which packs against D3. A helical hairpin insert in D2 binds to D3 and constrains its position, a conserved arginine residue at the end of this hairpin is essential for structural integrity. This entry represents D2 domain found at the N-terminal.


Pssm-ID: 466765  Cd Length: 129  Bit Score: 159.59  E-value: 7.20e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131854    20 AAGTVKVFSNGSSEAKTLTGAEHLIDLVGQP-RLANSWWPGAVISEELATAAALRQQQALLTRLAEQGADSSADD----A 94
Cdd:pfam20616   1 AQGTVSVFLPGESEVLTLTDAERLEQLVGQPqLLANSWWPGAVISDEAATQKALKQRQVLLAQLASLSAEWLFSAdgdlA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 16131854    95 AAINALRQQIQALKVTGRQKINLDPDIVRVAERGNPPLQGNYTLWVGPP 143
Cdd:pfam20616  81 AAINQLRQQLQNLNVTGRIFVNLDPDVVRVDERSNPPLVGDYQLYVAPR 129
 
Name Accession Description Interval E-value
Caps_syn_GfcC_C pfam06251
Capsule biosynthesis GfcC C-terminal; Many bacteria are covered in a layer of ...
 155-244 2.28e-51

Capsule biosynthesis GfcC C-terminal; Many bacteria are covered in a layer of surface-associated polysaccharide called the capsule. These capsules can be divided into four groups depending upon the organization of genes responsible for capsule assembly, the assembly pathway and regulation. This family plays a role in group 4 capsule biosynthesis. These proteins have a beta-grasp fold. Two beta-grasp domains, D2 and D3, are arranged in tandem. There is a C-terminal amphipathic helix which packs against D3. A helical hairpin insert in D2 binds to D3 and constrains its position, a conserved arginine residue at the end of this hairpin is essential for structural integrity. This is the C-terminal domain which covers D3 and D4 domains.


Pssm-ID: 461862  Cd Length: 90  Bit Score: 162.25  E-value: 2.28e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131854   155 RPGKQPFTPGRDVASYLSDQSLLSGADRSYAWVVYPDGRTQKAPVAYWNKRHVEPMPGSIIYVGLADSVWSETPDALNAD 234
Cdd:pfam06251   1 QSGSVPFLPGRSVADYLDDQPLLSGADRSYVYVIYPDGRTQKAPVALWNKRHVEPMPGSTIFVGFSPSVLPEDYSSLNEQ 80

                          90
                  ....*....|
gi 16131854   235 ILQTLTQRIP 244
Cdd:pfam06251  81 IVQLLTNRIP 90
Caps_syn_GfcC_N pfam20616
Capsule biosynthesis GfcC, N-terminal; Many bacteria are covered in a layer of ...
 20-143 7.20e-50

Capsule biosynthesis GfcC, N-terminal; Many bacteria are covered in a layer of surface-associated polysaccharide called the capsule. These capsules can be divided into four groups depending upon the organization of genes responsible for capsule assembly, the assembly pathway and regulation. This family plays a role in group 4 capsule biosynthesis. These proteins have a beta-grasp fold. Two beta-grasp domains, D2 and D3, are arranged in tandem. There is a C-terminal amphipathic helix which packs against D3. A helical hairpin insert in D2 binds to D3 and constrains its position, a conserved arginine residue at the end of this hairpin is essential for structural integrity. This entry represents D2 domain found at the N-terminal.


Pssm-ID: 466765  Cd Length: 129  Bit Score: 159.59  E-value: 7.20e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131854    20 AAGTVKVFSNGSSEAKTLTGAEHLIDLVGQP-RLANSWWPGAVISEELATAAALRQQQALLTRLAEQGADSSADD----A 94
Cdd:pfam20616   1 AQGTVSVFLPGESEVLTLTDAERLEQLVGQPqLLANSWWPGAVISDEAATQKALKQRQVLLAQLASLSAEWLFSAdgdlA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 16131854    95 AAINALRQQIQALKVTGRQKINLDPDIVRVAERGNPPLQGNYTLWVGPP 143
Cdd:pfam20616  81 AAINQLRQQLQNLNVTGRIFVNLDPDVVRVDERSNPPLVGDYQLYVAPR 129
 
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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