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Conserved domains on  [gi|15595880|ref|NP_249374|]
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type II secretion system protein [Pseudomonas aeruginosa PAO1]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GspL_C super family cl14909
GspL periplasmic domain; This domain is the periplasmic domain of the GspL/EpsL family ...
 207-355 1.21e-21

GspL periplasmic domain; This domain is the periplasmic domain of the GspL/EpsL family proteins. These proteins are involved in type II secretion systems.


The actual alignment was detected with superfamily member pfam12693:

Pssm-ID: 449377  Cd Length: 158  Bit Score: 90.52  E-value: 1.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595880   207 SAGNGTWKMPLFCAALALLVWVAGLNLYAGQLAEQGQSLQRQSSQRVQQAFPELPVVLDPLRQARERRDAyLAGKADGDA 286
Cdd:pfam12693   1 SKGWLAWRRVAILAALALLLVVVGGGLQLWQLQRQADALRAQSERIYQQLFPEEKRIVNLRAQMRQQLAR-LAGKASGVA 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595880   287 APGLAALLHGAGEamPFLAGRLQRLDYHAGELDLELlpGLPGGDAAAWQgelgkhGLQADASDKgWQVR 355
Cdd:pfam12693  80 LLDLLAALQTALA--QVPGLRLQSLDYDGARGELRL--QLRAKDFADFE------QLRAQAATY-FQVE 137
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 75-210 7.97e-03

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


The actual alignment was detected with superfamily member cd24017:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 226  Bit Score: 37.36  E-value: 7.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595880  75 LAHGPRGADGRLTLEWLEASALASLEQAVQRLRLDVREVQAAPFLLPLRDDAWVAGEWDGHLLLRRSLSDAVV---HPLP 151
Cdd:cd24017  91 FALGPRQADGRVPVAVVDRERLQAWLAALAAAGLRPDAVVPDALLLPWAEDGWSLLLDGDRVLVRTGEGQGFAldpELLP 170

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15595880 152 EQGLAEVPQELRLfwlgerpawRSAALERAEALDEALRWSGPASPWGLALKAPATSAGN 210
Cdd:cd24017 171 LLLSEGELEALAA---------LLPDALLAAAAPEESASLPELLLLLLLAALAASSAIN 220
 
Name Accession Description Interval E-value
GspL_C pfam12693
GspL periplasmic domain; This domain is the periplasmic domain of the GspL/EpsL family ...
 207-355 1.21e-21

GspL periplasmic domain; This domain is the periplasmic domain of the GspL/EpsL family proteins. These proteins are involved in type II secretion systems.


Pssm-ID: 432724  Cd Length: 158  Bit Score: 90.52  E-value: 1.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595880   207 SAGNGTWKMPLFCAALALLVWVAGLNLYAGQLAEQGQSLQRQSSQRVQQAFPELPVVLDPLRQARERRDAyLAGKADGDA 286
Cdd:pfam12693   1 SKGWLAWRRVAILAALALLLVVVGGGLQLWQLQRQADALRAQSERIYQQLFPEEKRIVNLRAQMRQQLAR-LAGKASGVA 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595880   287 APGLAALLHGAGEamPFLAGRLQRLDYHAGELDLELlpGLPGGDAAAWQgelgkhGLQADASDKgWQVR 355
Cdd:pfam12693  80 LLDLLAALQTALA--QVPGLRLQSLDYDGARGELRL--QLRAKDFADFE------QLRAQAATY-FQVE 137
typeII_sec_gspL TIGR01709
type II secretion system protein L; This model represents GspL, protein L of the main terminal ...
 72-346 2.28e-16

type II secretion system protein L; This model represents GspL, protein L of the main terminal branch of the general secretion pathway, also called type II secretion. It transports folded proteins across the bacterial outer membrane and is widely distributed in Gram-negative pathogens. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 273768 [Multi-domain]  Cd Length: 384  Bit Score: 79.80  E-value: 2.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595880    72 AVRLAHGPRGADGRLTLEWLEASALASLEQAVQRLRLDVREVQAAPFLLPLRDDAWVAGEWDGHLLLRRSL-SDAVVHPL 150
Cdd:TIGR01709  85 DLHFAVLPRDAEGATRVAVVDREWLQAWLDLLTEAGLAPERVVPDPLALPEPESGWAAVALLTEWLVRGSAgQGLVASEL 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595880   151 PEQGLAEVPQELRLFWLGERPAWRSAALE-RAEALDEALRWSG---PASPWGL--ALKAPATSAGNG--TWKMPLFCAAL 222
Cdd:TIGR01709 165 WAQHLAALEPPAALLAYGELPAALGADPEpQALPGTELVALLAapaLFPPINLltGPFAPRRSGRRQlaRWRRALGAAAV 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595880   223 ALLVWVAGLNLYAGQLAEQGQSLQRQSSQRVQQAFPELPVVLDPLRQARERRDAYLAGKADGDaapgLAALLHGAGEAM- 301
Cdd:TIGR01709 245 LLVLSLVGAGLQAWQVARQLDQLRAQSAETYRQLFPEAKKVVNPRTQFKAELSRLAAQGSGQG----FLDLLAALATALg 320

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 15595880   302 PFLAGRLQRLDYHAGELDLELLPGLPGGDAAAWQGELGKHGLQAD 346
Cdd:TIGR01709 321 QLPGLQLQSLDFDGARGELRLKLEAPSDADLEQLRSRLARGFQVA 365
PulL COG3297
Type II secretory pathway, component PulL [Intracellular trafficking, secretion, and vesicular ...
 75-357 1.27e-13

Type II secretory pathway, component PulL [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442526 [Multi-domain]  Cd Length: 404  Bit Score: 71.57  E-value: 1.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595880  75 LAHGPRGADGRLTLEWLEASALASLEQAVQRLRLDVREVQAAPFLLPLRDDAWVAGEWDGHLLLRRS-----------LS 143
Cdd:COG3297  97 FALGPRQGDGRVWVAVVDREWLQAWLDALEAAGLPVDRIVPDALALPLPEGGWSVLLLGDQWLVRTGewqgfaveadlLP 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595880 144 DAVVHPLPEQglAEVPQELRLFWLGERPAWRSAALERAEALDEALRW---SGPASPWGL-----ALKAPATSAGNgTWKM 215
Cdd:COG3297 177 LLLAAALEEA--ESKPAALPLLESYSPLPELEALELAEQPLGDPLQLlaqGLAASAINLlqgefAPRSRRSRLWR-PWRP 253

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595880 216 PLFCAALALLVWVAGLNLYAGQLAEQGQSLQRQSSQRVQQAFPELPVVLDPLRQARerrdAYLAGKADGDAAPGLAALLH 295
Cdd:COG3297 254 AAALAALLLVLQLVGLGVEAWQLRQQAAALRAEIEALYRQAFPGVKRVVDPRRQME----RQLARLRGGAGGSDLLPLLA 329

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15595880 296 GAGEAMPFLAG-RLQRLDY--HAGELDLELLpGLPGGDAAAWQGELGKHGLQAD---ASDKGWQVRAM 357
Cdd:COG3297 330 ALAPALAAVPGlKLQSLRYdaDRGELRLQLT-AASFEALEQLRQALEAAGLQVEigsANQEGGGVEGR 396
ASKHA_T2SSL_N cd24017
N-terminal domain of type II secretion system protein L (T2SSL) and similar proteins; Type II ...
 75-210 7.97e-03

N-terminal domain of type II secretion system protein L (T2SSL) and similar proteins; Type II secretion system is composed of four main components: the outer membrane complex, the inner membrane complex, the cytoplasmic secretion ATPase and the periplasm-spanning pseudopilus. T2SSL, also called T2SS protein L, or general secretion pathway protein L, is an inner membrane component of the type II secretion system, also called secretion-dependent pathway (SDP), required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. T2SSL is predicted to contain a large cytoplasmic domain and has been shown to interact with the autophosphorylating cytoplasmic membrane protein T2SSE. It is thought that the tri-molecular complex of T2SSL, T2SSE and T2SSM might be involved in regulating the opening and closing of the secretion pore and/or transducing energy to the site of outer membrane translocation. The model corresponds to the N-terminal domain of T2SSL. It is a cytoplasmic domain that shows structural homology with the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains. T2SSL is entirely missing domains 1B and 2B of the typical ASKHA proteins. The domain 2B of the ASKHA superfamily is critically important for binding the adenosine part of ATP. Due to the absence of 2B domain in T2SSL, it is therefore unlikely that T2SSL is an ATP-binding protein.


Pssm-ID: 466867 [Multi-domain]  Cd Length: 226  Bit Score: 37.36  E-value: 7.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595880  75 LAHGPRGADGRLTLEWLEASALASLEQAVQRLRLDVREVQAAPFLLPLRDDAWVAGEWDGHLLLRRSLSDAVV---HPLP 151
Cdd:cd24017  91 FALGPRQADGRVPVAVVDRERLQAWLAALAAAGLRPDAVVPDALLLPWAEDGWSLLLDGDRVLVRTGEGQGFAldpELLP 170

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15595880 152 EQGLAEVPQELRLfwlgerpawRSAALERAEALDEALRWSGPASPWGLALKAPATSAGN 210
Cdd:cd24017 171 LLLSEGELEALAA---------LLPDALLAAAAPEESASLPELLLLLLLAALAASSAIN 220
 
Name Accession Description Interval E-value
GspL_C pfam12693
GspL periplasmic domain; This domain is the periplasmic domain of the GspL/EpsL family ...
 207-355 1.21e-21

GspL periplasmic domain; This domain is the periplasmic domain of the GspL/EpsL family proteins. These proteins are involved in type II secretion systems.


Pssm-ID: 432724  Cd Length: 158  Bit Score: 90.52  E-value: 1.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595880   207 SAGNGTWKMPLFCAALALLVWVAGLNLYAGQLAEQGQSLQRQSSQRVQQAFPELPVVLDPLRQARERRDAyLAGKADGDA 286
Cdd:pfam12693   1 SKGWLAWRRVAILAALALLLVVVGGGLQLWQLQRQADALRAQSERIYQQLFPEEKRIVNLRAQMRQQLAR-LAGKASGVA 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595880   287 APGLAALLHGAGEamPFLAGRLQRLDYHAGELDLELlpGLPGGDAAAWQgelgkhGLQADASDKgWQVR 355
Cdd:pfam12693  80 LLDLLAALQTALA--QVPGLRLQSLDYDGARGELRL--QLRAKDFADFE------QLRAQAATY-FQVE 137
typeII_sec_gspL TIGR01709
type II secretion system protein L; This model represents GspL, protein L of the main terminal ...
 72-346 2.28e-16

type II secretion system protein L; This model represents GspL, protein L of the main terminal branch of the general secretion pathway, also called type II secretion. It transports folded proteins across the bacterial outer membrane and is widely distributed in Gram-negative pathogens. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 273768 [Multi-domain]  Cd Length: 384  Bit Score: 79.80  E-value: 2.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595880    72 AVRLAHGPRGADGRLTLEWLEASALASLEQAVQRLRLDVREVQAAPFLLPLRDDAWVAGEWDGHLLLRRSL-SDAVVHPL 150
Cdd:TIGR01709  85 DLHFAVLPRDAEGATRVAVVDREWLQAWLDLLTEAGLAPERVVPDPLALPEPESGWAAVALLTEWLVRGSAgQGLVASEL 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595880   151 PEQGLAEVPQELRLFWLGERPAWRSAALE-RAEALDEALRWSG---PASPWGL--ALKAPATSAGNG--TWKMPLFCAAL 222
Cdd:TIGR01709 165 WAQHLAALEPPAALLAYGELPAALGADPEpQALPGTELVALLAapaLFPPINLltGPFAPRRSGRRQlaRWRRALGAAAV 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595880   223 ALLVWVAGLNLYAGQLAEQGQSLQRQSSQRVQQAFPELPVVLDPLRQARERRDAYLAGKADGDaapgLAALLHGAGEAM- 301
Cdd:TIGR01709 245 LLVLSLVGAGLQAWQVARQLDQLRAQSAETYRQLFPEAKKVVNPRTQFKAELSRLAAQGSGQG----FLDLLAALATALg 320

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 15595880   302 PFLAGRLQRLDYHAGELDLELLPGLPGGDAAAWQGELGKHGLQAD 346
Cdd:TIGR01709 321 QLPGLQLQSLDFDGARGELRLKLEAPSDADLEQLRSRLARGFQVA 365
PulL COG3297
Type II secretory pathway, component PulL [Intracellular trafficking, secretion, and vesicular ...
 75-357 1.27e-13

Type II secretory pathway, component PulL [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442526 [Multi-domain]  Cd Length: 404  Bit Score: 71.57  E-value: 1.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595880  75 LAHGPRGADGRLTLEWLEASALASLEQAVQRLRLDVREVQAAPFLLPLRDDAWVAGEWDGHLLLRRS-----------LS 143
Cdd:COG3297  97 FALGPRQGDGRVWVAVVDREWLQAWLDALEAAGLPVDRIVPDALALPLPEGGWSVLLLGDQWLVRTGewqgfaveadlLP 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595880 144 DAVVHPLPEQglAEVPQELRLFWLGERPAWRSAALERAEALDEALRW---SGPASPWGL-----ALKAPATSAGNgTWKM 215
Cdd:COG3297 177 LLLAAALEEA--ESKPAALPLLESYSPLPELEALELAEQPLGDPLQLlaqGLAASAINLlqgefAPRSRRSRLWR-PWRP 253

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595880 216 PLFCAALALLVWVAGLNLYAGQLAEQGQSLQRQSSQRVQQAFPELPVVLDPLRQARerrdAYLAGKADGDAAPGLAALLH 295
Cdd:COG3297 254 AAALAALLLVLQLVGLGVEAWQLRQQAAALRAEIEALYRQAFPGVKRVVDPRRQME----RQLARLRGGAGGSDLLPLLA 329

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15595880 296 GAGEAMPFLAG-RLQRLDY--HAGELDLELLpGLPGGDAAAWQGELGKHGLQAD---ASDKGWQVRAM 357
Cdd:COG3297 330 ALAPALAAVPGlKLQSLRYdaDRGELRLQLT-AASFEALEQLRQALEAAGLQVEigsANQEGGGVEGR 396
ASKHA_T2SSL_N cd24017
N-terminal domain of type II secretion system protein L (T2SSL) and similar proteins; Type II ...
 75-210 7.97e-03

N-terminal domain of type II secretion system protein L (T2SSL) and similar proteins; Type II secretion system is composed of four main components: the outer membrane complex, the inner membrane complex, the cytoplasmic secretion ATPase and the periplasm-spanning pseudopilus. T2SSL, also called T2SS protein L, or general secretion pathway protein L, is an inner membrane component of the type II secretion system, also called secretion-dependent pathway (SDP), required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. T2SSL is predicted to contain a large cytoplasmic domain and has been shown to interact with the autophosphorylating cytoplasmic membrane protein T2SSE. It is thought that the tri-molecular complex of T2SSL, T2SSE and T2SSM might be involved in regulating the opening and closing of the secretion pore and/or transducing energy to the site of outer membrane translocation. The model corresponds to the N-terminal domain of T2SSL. It is a cytoplasmic domain that shows structural homology with the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains. T2SSL is entirely missing domains 1B and 2B of the typical ASKHA proteins. The domain 2B of the ASKHA superfamily is critically important for binding the adenosine part of ATP. Due to the absence of 2B domain in T2SSL, it is therefore unlikely that T2SSL is an ATP-binding protein.


Pssm-ID: 466867 [Multi-domain]  Cd Length: 226  Bit Score: 37.36  E-value: 7.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595880  75 LAHGPRGADGRLTLEWLEASALASLEQAVQRLRLDVREVQAAPFLLPLRDDAWVAGEWDGHLLLRRSLSDAVV---HPLP 151
Cdd:cd24017  91 FALGPRQADGRVPVAVVDRERLQAWLAALAAAGLRPDAVVPDALLLPWAEDGWSLLLDGDRVLVRTGEGQGFAldpELLP 170

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15595880 152 EQGLAEVPQELRLfwlgerpawRSAALERAEALDEALRWSGPASPWGLALKAPATSAGN 210
Cdd:cd24017 171 LLLSEGELEALAA---------LLPDALLAAAAPEESASLPELLLLLLLAALAASSAIN 220
 
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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