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Conserved domains on  [gi|2198970558|ref|WP_239641485|]
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pilus assembly protein [Salmonella enterica]

Protein Classification

PRK15221 family protein( domain architecture ID 10015015)

PRK15221 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK15221 PRK15221
Saf-pilin pilus formation protein SafA; Provisional
 1-159 4.54e-89

Saf-pilin pilus formation protein SafA; Provisional


:

Pssm-ID: 185143  Cd Length: 165  Bit Score: 256.64  E-value: 4.54e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198970558   1 MIIASALSMMAASCYAGSFLPNTEQEKSVDISFAAPEHLTISLEQTPGLIAGKGKPDTVVAKLTVNSTSIKEFGVRGVSG 80
Cdd:PRK15221    7 LIIASALSMMAASCYAGSFLPNTEQQKSVDINFASPQQLTVSLDPVSGLKAGKNKSDTAIAKLTVSSTSAKEFGVRGDAN 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2198970558  81 TMLNDLGSMWNITGKNSGSTVSVGFSSQTLGNSHSPQTWNGLRWYTFDVNDPVNIALVRDQNIPPDTYPLTVDVVGYQP 159
Cdd:PRK15221   87 AVVDNAGDVWTVTGKNTGNGIKVGFSGEACTRSKGNVNWNGHKWITFDTNDKLDIKLAGAQNVPADTYPITLDVVGYQA 165
 
Name Accession Description Interval E-value
PRK15221 PRK15221
Saf-pilin pilus formation protein SafA; Provisional
 1-159 4.54e-89

Saf-pilin pilus formation protein SafA; Provisional


Pssm-ID: 185143  Cd Length: 165  Bit Score: 256.64  E-value: 4.54e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198970558   1 MIIASALSMMAASCYAGSFLPNTEQEKSVDISFAAPEHLTISLEQTPGLIAGKGKPDTVVAKLTVNSTSIKEFGVRGVSG 80
Cdd:PRK15221    7 LIIASALSMMAASCYAGSFLPNTEQQKSVDINFASPQQLTVSLDPVSGLKAGKNKSDTAIAKLTVSSTSAKEFGVRGDAN 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2198970558  81 TMLNDLGSMWNITGKNSGSTVSVGFSSQTLGNSHSPQTWNGLRWYTFDVNDPVNIALVRDQNIPPDTYPLTVDVVGYQP 159
Cdd:PRK15221   87 AVVDNAGDVWTVTGKNTGNGIKVGFSGEACTRSKGNVNWNGHKWITFDTNDKLDIKLAGAQNVPADTYPITLDVVGYQA 165
SafA-like cd18775
Saf-pilin pilus formation protein SafA; This subfamily is composed of Saf-pilin pilus ...
 39-159 7.84e-41

Saf-pilin pilus formation protein SafA; This subfamily is composed of Saf-pilin pilus formation protein SafA from Salmonella enterica and similar proteins. SafA is the major subunit of Saf pili, which are often found in clinical isolates of Salmonella and are assembled by the chaperone-usher secretion pathway. In addition to safA, the saf operon is also composed of safB (periplasmic chaperone), safC (outer membrane usher), and safD (minor subunit). SafA and SafD subunits are transported from the cytoplasm into the periplasm via the SEC machinery, and the periplasmic chaperone SafB donates its G1 strand to complete the correct folding of SafA or SafD. In Saf pili assembly, the N-terminal extension (NTE) of an incoming SafA replaces the G1 strand (in SafB) via a zip-in-zip-out mechanism (also called donor-strand complementation or exchange) to form the polymer of SafD-(SafA)n (n > 100).


Pssm-ID: 350651  Cd Length: 122  Bit Score: 133.20  E-value: 7.84e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198970558  39 LTISLEQTPGLIAGKGKPDTVVAKLTVNSTSIKEFGVRGVSGTMLNDLGSMWNITGKNSGSTVSVGFSsqTLGNSHSPQT 118
Cdd:cd18775     1 LTVSLTPVSGLVAGKHADNTVIAKGTVTSTDAKRFAVRGTAGTGEDSNGSAWTITGKNDGNKLKVKLS--PDSTSGSTVK 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2198970558 119 WNGLRWYTFDVN---DPVNIALVRDQNIPPDTYPLTVDVVGYQP 159
Cdd:cd18775    79 WNGGTWFVFNINaptDTYDIKLDGDQNVPADTYPITLDAAAYQA 122
 
Name Accession Description Interval E-value
PRK15221 PRK15221
Saf-pilin pilus formation protein SafA; Provisional
 1-159 4.54e-89

Saf-pilin pilus formation protein SafA; Provisional


Pssm-ID: 185143  Cd Length: 165  Bit Score: 256.64  E-value: 4.54e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198970558   1 MIIASALSMMAASCYAGSFLPNTEQEKSVDISFAAPEHLTISLEQTPGLIAGKGKPDTVVAKLTVNSTSIKEFGVRGVSG 80
Cdd:PRK15221    7 LIIASALSMMAASCYAGSFLPNTEQQKSVDINFASPQQLTVSLDPVSGLKAGKNKSDTAIAKLTVSSTSAKEFGVRGDAN 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2198970558  81 TMLNDLGSMWNITGKNSGSTVSVGFSSQTLGNSHSPQTWNGLRWYTFDVNDPVNIALVRDQNIPPDTYPLTVDVVGYQP 159
Cdd:PRK15221   87 AVVDNAGDVWTVTGKNTGNGIKVGFSGEACTRSKGNVNWNGHKWITFDTNDKLDIKLAGAQNVPADTYPITLDVVGYQA 165
SafA-like cd18775
Saf-pilin pilus formation protein SafA; This subfamily is composed of Saf-pilin pilus ...
 39-159 7.84e-41

Saf-pilin pilus formation protein SafA; This subfamily is composed of Saf-pilin pilus formation protein SafA from Salmonella enterica and similar proteins. SafA is the major subunit of Saf pili, which are often found in clinical isolates of Salmonella and are assembled by the chaperone-usher secretion pathway. In addition to safA, the saf operon is also composed of safB (periplasmic chaperone), safC (outer membrane usher), and safD (minor subunit). SafA and SafD subunits are transported from the cytoplasm into the periplasm via the SEC machinery, and the periplasmic chaperone SafB donates its G1 strand to complete the correct folding of SafA or SafD. In Saf pili assembly, the N-terminal extension (NTE) of an incoming SafA replaces the G1 strand (in SafB) via a zip-in-zip-out mechanism (also called donor-strand complementation or exchange) to form the polymer of SafD-(SafA)n (n > 100).


Pssm-ID: 350651  Cd Length: 122  Bit Score: 133.20  E-value: 7.84e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198970558  39 LTISLEQTPGLIAGKGKPDTVVAKLTVNSTSIKEFGVRGVSGTMLNDLGSMWNITGKNSGSTVSVGFSsqTLGNSHSPQT 118
Cdd:cd18775     1 LTVSLTPVSGLVAGKHADNTVIAKGTVTSTDAKRFAVRGTAGTGEDSNGSAWTITGKNDGNKLKVKLS--PDSTSGSTVK 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2198970558 119 WNGLRWYTFDVN---DPVNIALVRDQNIPPDTYPLTVDVVGYQP 159
Cdd:cd18775    79 WNGGTWFVFNINaptDTYDIKLDGDQNVPADTYPITLDAAAYQA 122
AfaD_SafA-like cd16911
AfaD-like family of invasins; This family consists of Escherichia coli AfaD, Salmonella SafA ...
 39-157 7.03e-12

AfaD-like family of invasins; This family consists of Escherichia coli AfaD, Salmonella SafA and SafD, Yersinia pestis PsaA, Yersinia enterocolitica MyfA, and similar proteins. The afa gene clusters encode an afimbrial adhesive sheath produced by Escherichia coli. The adhesive sheath is composed of two proteins, AfaD and AfaE, which are independently exposed at the bacterial cell surface. AfaE is required for bacterial adhesion to HeLa cells and AfaD for the uptake of adherent bacteria into these cells. Saf-pilin pilus formation proteins SafA and SafD are the major and minor subunits, respectively, of Saf pili, which are often found in clinical isolates of Salmonella and are assembled by the chaperone-usher secretion pathway. PsaA and MyfA are the major subunits of pH 6 antigen (Psa) and Myf fimbrial homopolymers. Also included is the enteroaggregative Escherichia coli AAF/IV pilus tip protein, which is implicated in adhesion as well. During fimbria/pili assembly, polymerization occurs when the N-terminal extension (NTE) of one AfaD-like family monomer is inserted into an adjacent monomer, providing the final beta strand or G-strand, to complete the Ig-like fold, in a mechanism called the donor-strand complementation (DSC) or donor-strand exchange (DSE).


Pssm-ID: 350650  Cd Length: 120  Bit Score: 59.00  E-value: 7.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2198970558  39 LTISLEQTPGLIAGKGKPDTVVAKLTVNST-SIKEFGVRGVSGTMLNDLGSM-WNITGKNSGSTVSVGFSsqtlGNSHSP 116
Cdd:cd16911     1 FSATLTPVTGLGAGTQPDGTKIATLSVTNTgSHGGWRVYTNPNSVDGVGGAKgYTVRSKDGSKKVGVRIG----GDGYSG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2198970558 117 QTWNGLRWYTFDVN---DPVNIALVRDQNIPPDTYPLTVDVVGY 157
Cdd:cd16911    77 VKGGGGNWVGTGPTtkyITFDIVTDGGQQVKAGTYLFTVSVAEY 120
 
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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