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Conserved domains on  [gi|1701943214|ref|WP_142273439|]
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LPXTG cell wall anchor domain-containing protein, partial [Staphylococcus aureus]

Protein Classification

Fn_bind and Gram_pos_anchor domain-containing protein( domain architecture ID 10503148)

Fn_bind and Gram_pos_anchor domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Gram_pos_anchor pfam00746
LPXTG cell wall anchor motif;
190-231 4.33e-06

LPXTG cell wall anchor motif;


:

Pssm-ID: 366278 [Multi-domain]  Cd Length: 43  Bit Score: 42.53  E-value: 4.33e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1701943214 190 QSKKSELPETGgEESTNKGMLFGGLFSILGLALLRRNKKNNK 231
Cdd:pfam00746   3 KSKKKTLPKTG-ENSNIFLTAAGLLALLGGLLLLVKRRKKEK 43
Fn_bind pfam02986
Fibronectin binding repeat; The ability of bacteria to bind fibronectin is thought to enable ...
2-35 4.14e-04

Fibronectin binding repeat; The ability of bacteria to bind fibronectin is thought to enable the colonization of wound tissue and blood clots. The fibronectin binding repeat is found in bacterial fibronectin binding proteins and serum opacity factor. Bacterial fibronectin binding proteins are surface proteins that covalently link to the bacterial cell wall, mediate adherence of the bacteria to host cells and trigger the fibronectin/integrin-mediated uptake of bacteria by host cells. Each fibronectin binding repeat is an array of short motifs that bind to fibronectin type I domains. Fibronectin binding repeats are natively unfolded in the absence of fibronectin and are thought to adopt a well-defined conformation (tandem beta-zipper) upon binding.


:

Pssm-ID: 397232 [Multi-domain]  Cd Length: 33  Bit Score: 36.81  E-value: 4.14e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1701943214   2 DFDSVPQIHGFNKHNeIIEEDTNKDKPNYQFGGH 35
Cdd:pfam02986   1 TEDTQPGMSGQSGGT-TEEEDTKKPKRKVIIGGQ 33
 
Name Accession Description Interval E-value
Gram_pos_anchor pfam00746
LPXTG cell wall anchor motif;
190-231 4.33e-06

LPXTG cell wall anchor motif;


Pssm-ID: 366278 [Multi-domain]  Cd Length: 43  Bit Score: 42.53  E-value: 4.33e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1701943214 190 QSKKSELPETGgEESTNKGMLFGGLFSILGLALLRRNKKNNK 231
Cdd:pfam00746   3 KSKKKTLPKTG-ENSNIFLTAAGLLALLGGLLLLVKRRKKEK 43
Fn_bind pfam02986
Fibronectin binding repeat; The ability of bacteria to bind fibronectin is thought to enable ...
2-35 4.14e-04

Fibronectin binding repeat; The ability of bacteria to bind fibronectin is thought to enable the colonization of wound tissue and blood clots. The fibronectin binding repeat is found in bacterial fibronectin binding proteins and serum opacity factor. Bacterial fibronectin binding proteins are surface proteins that covalently link to the bacterial cell wall, mediate adherence of the bacteria to host cells and trigger the fibronectin/integrin-mediated uptake of bacteria by host cells. Each fibronectin binding repeat is an array of short motifs that bind to fibronectin type I domains. Fibronectin binding repeats are natively unfolded in the absence of fibronectin and are thought to adopt a well-defined conformation (tandem beta-zipper) upon binding.


Pssm-ID: 397232 [Multi-domain]  Cd Length: 33  Bit Score: 36.81  E-value: 4.14e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1701943214   2 DFDSVPQIHGFNKHNeIIEEDTNKDKPNYQFGGH 35
Cdd:pfam02986   1 TEDTQPGMSGQSGGT-TEEEDTKKPKRKVIIGGQ 33
LPXTG_anchor TIGR01167
LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region ...
195-229 4.47e-04

LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region found at the C-terminus of many surface proteins of Streptococcus and Streptomyces species. Cleavage between the Thr and Gly by sortase or a related enzyme leads to covalent anchoring at the new C-terminal Thr to the cell wall. Hits that do not lie at the C-terminus or are not found in Gram-positive bacteria are probably false-positive. A common feature of this proteins containing this domain appears to be a high proportion of charged and zwitterionic residues immediatedly upstream of the LPXTG motif. This model differs from other descriptions of the LPXTG region by including a portion of that upstream charged region. [Cell envelope, Other]


Pssm-ID: 273478 [Multi-domain]  Cd Length: 34  Bit Score: 36.68  E-value: 4.47e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1701943214 195 ELPETGgEESTNKGMLFGGLFSILGLALLRRNKKN 229
Cdd:TIGR01167   1 KLPKTG-ESGNSLLLLLGLLLLGLGGLLLRKRKKK 34
 
Name Accession Description Interval E-value
Gram_pos_anchor pfam00746
LPXTG cell wall anchor motif;
190-231 4.33e-06

LPXTG cell wall anchor motif;


Pssm-ID: 366278 [Multi-domain]  Cd Length: 43  Bit Score: 42.53  E-value: 4.33e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1701943214 190 QSKKSELPETGgEESTNKGMLFGGLFSILGLALLRRNKKNNK 231
Cdd:pfam00746   3 KSKKKTLPKTG-ENSNIFLTAAGLLALLGGLLLLVKRRKKEK 43
Fn_bind pfam02986
Fibronectin binding repeat; The ability of bacteria to bind fibronectin is thought to enable ...
2-35 4.14e-04

Fibronectin binding repeat; The ability of bacteria to bind fibronectin is thought to enable the colonization of wound tissue and blood clots. The fibronectin binding repeat is found in bacterial fibronectin binding proteins and serum opacity factor. Bacterial fibronectin binding proteins are surface proteins that covalently link to the bacterial cell wall, mediate adherence of the bacteria to host cells and trigger the fibronectin/integrin-mediated uptake of bacteria by host cells. Each fibronectin binding repeat is an array of short motifs that bind to fibronectin type I domains. Fibronectin binding repeats are natively unfolded in the absence of fibronectin and are thought to adopt a well-defined conformation (tandem beta-zipper) upon binding.


Pssm-ID: 397232 [Multi-domain]  Cd Length: 33  Bit Score: 36.81  E-value: 4.14e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1701943214   2 DFDSVPQIHGFNKHNeIIEEDTNKDKPNYQFGGH 35
Cdd:pfam02986   1 TEDTQPGMSGQSGGT-TEEEDTKKPKRKVIIGGQ 33
LPXTG_anchor TIGR01167
LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region ...
195-229 4.47e-04

LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region found at the C-terminus of many surface proteins of Streptococcus and Streptomyces species. Cleavage between the Thr and Gly by sortase or a related enzyme leads to covalent anchoring at the new C-terminal Thr to the cell wall. Hits that do not lie at the C-terminus or are not found in Gram-positive bacteria are probably false-positive. A common feature of this proteins containing this domain appears to be a high proportion of charged and zwitterionic residues immediatedly upstream of the LPXTG motif. This model differs from other descriptions of the LPXTG region by including a portion of that upstream charged region. [Cell envelope, Other]


Pssm-ID: 273478 [Multi-domain]  Cd Length: 34  Bit Score: 36.68  E-value: 4.47e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1701943214 195 ELPETGgEESTNKGMLFGGLFSILGLALLRRNKKN 229
Cdd:TIGR01167   1 KLPKTG-ESGNSLLLLLGLLLLGLGGLLLRKRKKK 34
 
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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