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Conserved domains on  [gi|1319856412|gb|PLL41582|]
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conjugal transfer protein [Klebsiella pneumoniae]

Protein Classification

fertility inhibition protein FinO( domain architecture ID 11486840)

fertility inhibition protein FinO is one of the components on the FinOP fertility inhibition complex, which inhibits the expression of traJ gene, which in turn regulates the expression of some 20 transfer genes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13754 PRK13754
fertility inhibition protein FinO;
1-196 2.19e-78

fertility inhibition protein FinO;


:

Pssm-ID: 184304 [Multi-domain]  Cd Length: 186  Bit Score: 232.07  E-value: 2.19e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319856412   1 MSEEKRPVLSLKRKPAENSTAPAEATpapgvvrrkkVVVVSSPPAWKAKKAKLEKvkqaAEAATRNAAPVKVVKTPPPVR 80
Cdd:PRK13754    1 MTEQKRPVLTLKRKTEGETPVRSRKT----------IINVTTPPKWKVKKQKLAE----KAAREAELAAKKAQARQALSI 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319856412  81 YLRLLPPEQAIMTLKAFWPQLFDGNSPRLLATGMREQLFADIVNRDLPLSHKQVIKCLKSLTRSAGYLSRMKVGASRYDL 160
Cdd:PRK13754   67 YLNLPPLDEAVNTLKPWWPGLFDGDTPRLLACGIREVLLEDVAQRNIPLSHKKLRRALKAITRSESYLCAMKAGACRYDT 146

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1319856412 161 QGNAVATVTAEEAQYASERmMKELLRTERMRSQSAG 196
Cdd:PRK13754  147 EGYVTEHISQEEEAYAAER-LDKIRRQNRIKAELQA 181
 
Name Accession Description Interval E-value
PRK13754 PRK13754
fertility inhibition protein FinO;
1-196 2.19e-78

fertility inhibition protein FinO;


Pssm-ID: 184304 [Multi-domain]  Cd Length: 186  Bit Score: 232.07  E-value: 2.19e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319856412   1 MSEEKRPVLSLKRKPAENSTAPAEATpapgvvrrkkVVVVSSPPAWKAKKAKLEKvkqaAEAATRNAAPVKVVKTPPPVR 80
Cdd:PRK13754    1 MTEQKRPVLTLKRKTEGETPVRSRKT----------IINVTTPPKWKVKKQKLAE----KAAREAELAAKKAQARQALSI 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319856412  81 YLRLLPPEQAIMTLKAFWPQLFDGNSPRLLATGMREQLFADIVNRDLPLSHKQVIKCLKSLTRSAGYLSRMKVGASRYDL 160
Cdd:PRK13754   67 YLNLPPLDEAVNTLKPWWPGLFDGDTPRLLACGIREVLLEDVAQRNIPLSHKKLRRALKAITRSESYLCAMKAGACRYDT 146

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1319856412 161 QGNAVATVTAEEAQYASERmMKELLRTERMRSQSAG 196
Cdd:PRK13754  147 EGYVTEHISQEEEAYAAER-LDKIRRQNRIKAELQA 181
ProQ pfam04352
ProQ/FINO family; This family includes ProQ, which is required for full activation of the ...
 87-193 1.22e-28

ProQ/FINO family; This family includes ProQ, which is required for full activation of the osmoprotectant transporter, ProP, in Escherichia coli. This family includes several bacterial fertility inhibition (FINO) proteins. The conjugative transfer of F-like plasmids is repressed by FinO, an RNA binding protein. FinO interacts with the F-plasmid encoded traJ mRNA and its antisense RNA, FinP, stabilising FinP against endonucleolytic degradation and facilitating sense-antisense RNA recognition. ProQ operates as an RNA-chaperone, binding RNA and bringing about both RNA strand-exchange and RNA duplexing. This suggests that in fact it does not regulate ProP transcription but rather regulates ProP translation through activity as an RNA-binding protein.


Pssm-ID: 461270  Cd Length: 106  Bit Score: 102.68  E-value: 1.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319856412  87 PEQAIMTLKAFWPQLFDGNS-PRLLATGMREQLFAdiVNRDLPLSHKQVIKCLKSLTRSAGYLSRMKVGASRYDLQGNAV 165
Cdd:pfam04352   1 VKELIARLAERFPLAFPAEGeKLPLKIGIFQDLLE--LADDLGLSKTQLRQALRTYTRSWRYLAAMKEGAARVDLDGNPA 78

                          90       100
                  ....*....|....*....|....*...
gi 1319856412 166 ATVTAEEAQYASERMMKELLRTERMRSQ 193
Cdd:pfam04352  79 GEVTAEHAEHARQQLARRRQKRAQRRAA 106
ProQ COG3109
sRNA-binding protein ProQ [Signal transduction mechanisms];
84-195 2.21e-27

sRNA-binding protein ProQ [Signal transduction mechanisms];


Pssm-ID: 442343 [Multi-domain]  Cd Length: 153  Bit Score: 101.21  E-value: 2.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319856412  84 LLPPEQAIMTLKAFWPQLFDGNSPRLLATGMREQLFADIvnRDLPLSHKQVIKCLKSLTRSAGYLSRMKVGASRYDLQGN 163
Cdd:COG3109    10 LESPKEVIAYLAERFPACFDLEEPKPLKIGIFQDLAARL--PDDELSKTQLRRALRRYTRSWRYLKAVKEGAQRVDLDGN 87

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1319856412 164 AVATVTAEEAQYASERMMKELLRTERMRSQSA 195
Cdd:COG3109    88 PAGEVTEEHAEHAREQLAERKAKVAARRAAEQ 119
FinO_conjug_rep cd00236
FinO bacterial conjugation repressor domain; the basic protein FinO is part of the the two ...
 80-193 1.04e-18

FinO bacterial conjugation repressor domain; the basic protein FinO is part of the the two component FinOP system which is responsible for repressing bacterial conjugation; the FinOP system represses the transfer (tra) operon of the F-plasmid which encodes the proteins responsible for conjugative transfer of this plasmid from host to recipient Escherichia coli cells; antisense RNA, FinP is thought to interact with traJ mRNA to occlude its ribosome binding site, blocking traJ translation and thereby inhibiting transcription of the tra operon; FinO protects FinP against degradation by binding to FinP and sterically blocking the cellular endonuclease RNase E; FinO also also binds to the complementary stem-loop structures in traJ mRNA and promotes duplex formation between FinP and traJ RNA in vitro; this domain contains two independent RNA binding regions


Pssm-ID: 238145  Cd Length: 146  Bit Score: 78.40  E-value: 1.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319856412  80 RYLRLLPPEQAIMTLKAFWPQLFDGNSPRLLATGMREQLFADIV-NRDLPLSHKQVIKCLKSLTRSAGYLSRMKVGASRY 158
Cdd:cd00236    29 IYLNLPTVEYAVECLKKWFPGLFPGDTPRLLKCGIKDGILQDVAqHPNIPLTHEELRCAVKAITRRESYLQAMVAGAPRY 108

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1319856412 159 DLQGNAVATVTAEEAQYASERMMKeLLRTERMRSQ 193
Cdd:cd00236   109 DLEGYVAGHISQEAEVYAARLLDK-IRRQQRIKKE 142
ProQ smart00945
ProQ/FINO family; This family includes ProQ, which is required for full activation of the ...
 83-182 5.89e-15

ProQ/FINO family; This family includes ProQ, which is required for full activation of the osmoprotectant transporter, ProQ, in Escherichia coli.


Pssm-ID: 198013 [Multi-domain]  Cd Length: 113  Bit Score: 67.77  E-value: 5.89e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319856412   83 RLLPPEQAIMTLKAFWPQLFDGN-SPRLLATGMREQLFADIVNRDLPlSHKQVIKCLKSLTRSAGYLSRMKVGASRYDLQ 161
Cdd:smart00945   1 KLDDVKALLEKLQERFPLCFGANgAPKPLKIGIFQDLLARLEEDEKV-SKTALREALRTYTRSWRYLKAVKAGAVRVDLQ 79

                           90       100
                   ....*....|....*....|.
gi 1319856412  162 GNAVATVTAEEAQYASERMMK 182
Cdd:smart00945  80 GNPAEEVTEEHAAHALKKLKE 100
 
Name Accession Description Interval E-value
PRK13754 PRK13754
fertility inhibition protein FinO;
1-196 2.19e-78

fertility inhibition protein FinO;


Pssm-ID: 184304 [Multi-domain]  Cd Length: 186  Bit Score: 232.07  E-value: 2.19e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319856412   1 MSEEKRPVLSLKRKPAENSTAPAEATpapgvvrrkkVVVVSSPPAWKAKKAKLEKvkqaAEAATRNAAPVKVVKTPPPVR 80
Cdd:PRK13754    1 MTEQKRPVLTLKRKTEGETPVRSRKT----------IINVTTPPKWKVKKQKLAE----KAAREAELAAKKAQARQALSI 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319856412  81 YLRLLPPEQAIMTLKAFWPQLFDGNSPRLLATGMREQLFADIVNRDLPLSHKQVIKCLKSLTRSAGYLSRMKVGASRYDL 160
Cdd:PRK13754   67 YLNLPPLDEAVNTLKPWWPGLFDGDTPRLLACGIREVLLEDVAQRNIPLSHKKLRRALKAITRSESYLCAMKAGACRYDT 146

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1319856412 161 QGNAVATVTAEEAQYASERmMKELLRTERMRSQSAG 196
Cdd:PRK13754  147 EGYVTEHISQEEEAYAAER-LDKIRRQNRIKAELQA 181
ProQ pfam04352
ProQ/FINO family; This family includes ProQ, which is required for full activation of the ...
 87-193 1.22e-28

ProQ/FINO family; This family includes ProQ, which is required for full activation of the osmoprotectant transporter, ProP, in Escherichia coli. This family includes several bacterial fertility inhibition (FINO) proteins. The conjugative transfer of F-like plasmids is repressed by FinO, an RNA binding protein. FinO interacts with the F-plasmid encoded traJ mRNA and its antisense RNA, FinP, stabilising FinP against endonucleolytic degradation and facilitating sense-antisense RNA recognition. ProQ operates as an RNA-chaperone, binding RNA and bringing about both RNA strand-exchange and RNA duplexing. This suggests that in fact it does not regulate ProP transcription but rather regulates ProP translation through activity as an RNA-binding protein.


Pssm-ID: 461270  Cd Length: 106  Bit Score: 102.68  E-value: 1.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319856412  87 PEQAIMTLKAFWPQLFDGNS-PRLLATGMREQLFAdiVNRDLPLSHKQVIKCLKSLTRSAGYLSRMKVGASRYDLQGNAV 165
Cdd:pfam04352   1 VKELIARLAERFPLAFPAEGeKLPLKIGIFQDLLE--LADDLGLSKTQLRQALRTYTRSWRYLAAMKEGAARVDLDGNPA 78

                          90       100
                  ....*....|....*....|....*...
gi 1319856412 166 ATVTAEEAQYASERMMKELLRTERMRSQ 193
Cdd:pfam04352  79 GEVTAEHAEHARQQLARRRQKRAQRRAA 106
ProQ COG3109
sRNA-binding protein ProQ [Signal transduction mechanisms];
84-195 2.21e-27

sRNA-binding protein ProQ [Signal transduction mechanisms];


Pssm-ID: 442343 [Multi-domain]  Cd Length: 153  Bit Score: 101.21  E-value: 2.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319856412  84 LLPPEQAIMTLKAFWPQLFDGNSPRLLATGMREQLFADIvnRDLPLSHKQVIKCLKSLTRSAGYLSRMKVGASRYDLQGN 163
Cdd:COG3109    10 LESPKEVIAYLAERFPACFDLEEPKPLKIGIFQDLAARL--PDDELSKTQLRRALRRYTRSWRYLKAVKEGAQRVDLDGN 87

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1319856412 164 AVATVTAEEAQYASERMMKELLRTERMRSQSA 195
Cdd:COG3109    88 PAGEVTEEHAEHAREQLAERKAKVAARRAAEQ 119
FinO_conjug_rep cd00236
FinO bacterial conjugation repressor domain; the basic protein FinO is part of the the two ...
 80-193 1.04e-18

FinO bacterial conjugation repressor domain; the basic protein FinO is part of the the two component FinOP system which is responsible for repressing bacterial conjugation; the FinOP system represses the transfer (tra) operon of the F-plasmid which encodes the proteins responsible for conjugative transfer of this plasmid from host to recipient Escherichia coli cells; antisense RNA, FinP is thought to interact with traJ mRNA to occlude its ribosome binding site, blocking traJ translation and thereby inhibiting transcription of the tra operon; FinO protects FinP against degradation by binding to FinP and sterically blocking the cellular endonuclease RNase E; FinO also also binds to the complementary stem-loop structures in traJ mRNA and promotes duplex formation between FinP and traJ RNA in vitro; this domain contains two independent RNA binding regions


Pssm-ID: 238145  Cd Length: 146  Bit Score: 78.40  E-value: 1.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319856412  80 RYLRLLPPEQAIMTLKAFWPQLFDGNSPRLLATGMREQLFADIV-NRDLPLSHKQVIKCLKSLTRSAGYLSRMKVGASRY 158
Cdd:cd00236    29 IYLNLPTVEYAVECLKKWFPGLFPGDTPRLLKCGIKDGILQDVAqHPNIPLTHEELRCAVKAITRRESYLQAMVAGAPRY 108

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1319856412 159 DLQGNAVATVTAEEAQYASERMMKeLLRTERMRSQ 193
Cdd:cd00236   109 DLEGYVAGHISQEAEVYAARLLDK-IRRQQRIKKE 142
ProQ smart00945
ProQ/FINO family; This family includes ProQ, which is required for full activation of the ...
 83-182 5.89e-15

ProQ/FINO family; This family includes ProQ, which is required for full activation of the osmoprotectant transporter, ProQ, in Escherichia coli.


Pssm-ID: 198013 [Multi-domain]  Cd Length: 113  Bit Score: 67.77  E-value: 5.89e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319856412   83 RLLPPEQAIMTLKAFWPQLFDGN-SPRLLATGMREQLFADIVNRDLPlSHKQVIKCLKSLTRSAGYLSRMKVGASRYDLQ 161
Cdd:smart00945   1 KLDDVKALLEKLQERFPLCFGANgAPKPLKIGIFQDLLARLEEDEKV-SKTALREALRTYTRSWRYLKAVKAGAVRVDLQ 79

                           90       100
                   ....*....|....*....|.
gi 1319856412  162 GNAVATVTAEEAQYASERMMK 182
Cdd:smart00945  80 GNPAEEVTEEHAAHALKKLKE 100
FinO_N pfam12602
Fertility inhibition protein N terminal; This domain family is found in bacteria, and is ...
 1-71 1.45e-07

Fertility inhibition protein N terminal; This domain family is found in bacteria, and is typically between 62 and 102 amino acids in length. The family is found in association with pfam04352. The FinOP (fertility inhibition) system of F-like plasmids consists of an antisense RNA (FinP) and a 22 kDa protein (FinO) which act in concert to prevent the translation of TraJ, the positive regulator of the transfer operon.


Pssm-ID: 315304  Cd Length: 62  Bit Score: 46.67  E-value: 1.45e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1319856412   1 MSEEKRPVLSLKRKPaeNSTAPAEAtpapgvvrRKKVVVVSSPPAWKAKKAKL-EKVKQAAEAATRNAAPVK 71
Cdd:pfam12602   1 MTEQKRPVLTLKRKT--NGTAPARS--------RKTIINVTTPPKWKVKKQKLaEKAKREAELAAKKAAARP 62
PRK04950 PRK04950
ProP expression regulator; Provisional
 118-176 4.03e-03

ProP expression regulator; Provisional


Pssm-ID: 235322 [Multi-domain]  Cd Length: 213  Bit Score: 36.83  E-value: 4.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1319856412 118 LFADIVNR---DLPLSHKQVIKCLKSLTRSAGYLSRMKVGASRYDLQGNAVATVTAEEAQYA 176
Cdd:PRK04950   38 IFQDLAERladDEKVSKTQLRSALRLYTSSWRYLYGVKAGAQRVDLDGNPCGELEEEHVEHA 99
 
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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