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Conserved domains on  [gi|1125798322|ref|WP_075112948|]
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MULTISPECIES: lipid asymmetry maintenance protein MlaB [Aeromonas]

Protein Classification

lipid asymmetry maintenance protein MlaB( domain architecture ID 10006937)

lipid asymmetry maintenance protein MlaB is part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MlaB COG3113
Binding protein subunit MlaB of the ABC-type intermembrane phospholipid transporter Mla, ...
 2-81 2.47e-16

Binding protein subunit MlaB of the ABC-type intermembrane phospholipid transporter Mla, contains STAS domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442347 [Multi-domain]  Cd Length: 97  Bit Score: 67.20  E-value: 2.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125798322  2 TLCGDLQAPQVNDLWQRRADWWQDD---RLDLGGVTTLDSAGLALLVKWAKAALARGATPQLVGASSDFYTLANLYGVAG 78
Cdd:COG3113   15 RLSGELTRDTVLALWAQLLALLAAGgavEIDLSGVTRVDSAGLALLLELLREARAQGKTLRLTGVPEQLRTLAALYGLDE 94


                 ...
gi 1125798322 79 LFQ 81
Cdd:COG3113   95 LLP 97
 
Name Accession Description Interval E-value
MlaB COG3113
Binding protein subunit MlaB of the ABC-type intermembrane phospholipid transporter Mla, ...
 2-81 2.47e-16

Binding protein subunit MlaB of the ABC-type intermembrane phospholipid transporter Mla, contains STAS domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442347 [Multi-domain]  Cd Length: 97  Bit Score: 67.20  E-value: 2.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125798322  2 TLCGDLQAPQVNDLWQRRADWWQDD---RLDLGGVTTLDSAGLALLVKWAKAALARGATPQLVGASSDFYTLANLYGVAG 78
Cdd:COG3113   15 RLSGELTRDTVLALWAQLLALLAAGgavEIDLSGVTRVDSAGLALLLELLREARAQGKTLRLTGVPEQLRTLAALYGLDE 94


                 ...
gi 1125798322 79 LFQ 81
Cdd:COG3113   95 LLP 97
STAS_2 pfam13466
STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is ...
 1-77 1.60e-08

STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is found in the C-terminal region of Sulphate transporters and bacterial antisigma factor antagonists. It has been suggested that this domain may have a general NTP binding function.


Pssm-ID: 433231 [Multi-domain]  Cd Length: 80  Bit Score: 46.83  E-value: 1.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125798322  1 MTLCGDLQAPQVNDLWQRRADWWQDD---RLDLGGVTTLDSAGLALLVKWAKAALARGATPQLVGASSDFYTLANLYGVA 77
Cdd:pfam13466  1 LSLSGELDADTAPALREALLAALAAGspvVVDLSGVERVDSAGLALLLALARRARARGKRLVLRGLPPALLRLLRLLGLD 80
STAS_anti-anti-sigma_factors cd07043
Sulphate Transporter and Anti-Sigma factor antagonist) domain of anti-anti-sigma factors, key ...
 2-84 3.94e-08

Sulphate Transporter and Anti-Sigma factor antagonist) domain of anti-anti-sigma factors, key regulators of anti-sigma factors by phosphorylation; Anti-anti-sigma factors play an important role in the regulation of several sigma factors and their corresponding anti-sigma factors. Upon dephosphorylation they bind the anti-sigma factor and induce the release of the sigma factor from the anti-sigma factor. In a feedback mechanism the anti-anti-sigma factor can be inactivated via phosphorylation by the anti-sigma factor. Well studied examples from Bacillus subtilis are SpoIIAA (regulating sigmaF and sigmaC which play an important role in sporulation) and RsbV (regulating sigmaB involved in the general stress response). The STAS domain is also found in the C- terminal region of sulphate transporters and stressosomes.


Pssm-ID: 132914 [Multi-domain]  Cd Length: 99  Bit Score: 46.36  E-value: 3.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125798322  2 TLCGDLQAPQVNDLWQRRADWWQDDR----LDLGGVTTLDSAGLALLVKWAKAALARGATPQLVGASSDFYTLANLYGVA 77
Cdd:cd07043   13 RLSGELDAATAPELREALEELLAEGPrrlvLDLSGVTFIDSSGLGVLLGAYKRARAAGGRLVLVNVSPAVRRVLELTGLD 92


                 ....*..
gi 1125798322 78 GLFQSTP 84
Cdd:cd07043   93 RLFPIYP 99
ant_ant_sig TIGR00377
anti-anti-sigma factor; This superfamily includes small (105-125 residue) proteins related to ...
 28-89 1.90e-03

anti-anti-sigma factor; This superfamily includes small (105-125 residue) proteins related to SpoIIAA of Bacillus subtilis, an anti-anti-sigma factor. SpoIIAA can bind to and inhibit the anti-sigma F factor SpoIIAB. Also, it can be phosphorylated by SpoIIAB on a Ser residue at position 59 of the seed alignment. A similar arrangement is inferred for RsbV, an anti-anti-sigma factor for sigma B. This Ser is fairly well conserved within a motif resembling MXS[STA]G[VIL]X[VIL][VILF] among homologous known or predicted anti-anti-sigma factors. Regions similar to SpoIIAA and apparently homologous, but differing considerably near the phosphorlated Ser of SpoIIAA, appear in a single copy in several longer proteins. [Regulatory functions, Protein interactions]


Pssm-ID: 273042 [Multi-domain]  Cd Length: 108  Bit Score: 34.50  E-value: 1.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125798322  28 LDLGGVTTLDSAGLALLVKWAKAALARGATPQLVGASSdfyTLANLYGVAGLFQSTPL-TTED 89
Cdd:TIGR00377  48 LDLEDLEFMDSSGLGVLLGRYKQVRRVGGQLVLVSVSP---RVARLLDITGLLRIIPIyPTVE 107
 
Name Accession Description Interval E-value
MlaB COG3113
Binding protein subunit MlaB of the ABC-type intermembrane phospholipid transporter Mla, ...
 2-81 2.47e-16

Binding protein subunit MlaB of the ABC-type intermembrane phospholipid transporter Mla, contains STAS domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442347 [Multi-domain]  Cd Length: 97  Bit Score: 67.20  E-value: 2.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125798322  2 TLCGDLQAPQVNDLWQRRADWWQDD---RLDLGGVTTLDSAGLALLVKWAKAALARGATPQLVGASSDFYTLANLYGVAG 78
Cdd:COG3113   15 RLSGELTRDTVLALWAQLLALLAAGgavEIDLSGVTRVDSAGLALLLELLREARAQGKTLRLTGVPEQLRTLAALYGLDE 94


                 ...
gi 1125798322 79 LFQ 81
Cdd:COG3113   95 LLP 97
STAS_2 pfam13466
STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is ...
 1-77 1.60e-08

STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is found in the C-terminal region of Sulphate transporters and bacterial antisigma factor antagonists. It has been suggested that this domain may have a general NTP binding function.


Pssm-ID: 433231 [Multi-domain]  Cd Length: 80  Bit Score: 46.83  E-value: 1.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125798322  1 MTLCGDLQAPQVNDLWQRRADWWQDD---RLDLGGVTTLDSAGLALLVKWAKAALARGATPQLVGASSDFYTLANLYGVA 77
Cdd:pfam13466  1 LSLSGELDADTAPALREALLAALAAGspvVVDLSGVERVDSAGLALLLALARRARARGKRLVLRGLPPALLRLLRLLGLD 80
STAS_anti-anti-sigma_factors cd07043
Sulphate Transporter and Anti-Sigma factor antagonist) domain of anti-anti-sigma factors, key ...
 2-84 3.94e-08

Sulphate Transporter and Anti-Sigma factor antagonist) domain of anti-anti-sigma factors, key regulators of anti-sigma factors by phosphorylation; Anti-anti-sigma factors play an important role in the regulation of several sigma factors and their corresponding anti-sigma factors. Upon dephosphorylation they bind the anti-sigma factor and induce the release of the sigma factor from the anti-sigma factor. In a feedback mechanism the anti-anti-sigma factor can be inactivated via phosphorylation by the anti-sigma factor. Well studied examples from Bacillus subtilis are SpoIIAA (regulating sigmaF and sigmaC which play an important role in sporulation) and RsbV (regulating sigmaB involved in the general stress response). The STAS domain is also found in the C- terminal region of sulphate transporters and stressosomes.


Pssm-ID: 132914 [Multi-domain]  Cd Length: 99  Bit Score: 46.36  E-value: 3.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125798322  2 TLCGDLQAPQVNDLWQRRADWWQDDR----LDLGGVTTLDSAGLALLVKWAKAALARGATPQLVGASSDFYTLANLYGVA 77
Cdd:cd07043   13 RLSGELDAATAPELREALEELLAEGPrrlvLDLSGVTFIDSSGLGVLLGAYKRARAAGGRLVLVNVSPAVRRVLELTGLD 92


                 ....*..
gi 1125798322 78 GLFQSTP 84
Cdd:cd07043   93 RLFPIYP 99
SpoIIAA COG1366
Anti-anti-sigma regulatory factor (antagonist of anti-sigma factor) [Signal transduction ...
 1-64 5.86e-08

Anti-anti-sigma regulatory factor (antagonist of anti-sigma factor) [Signal transduction mechanisms];


Pssm-ID: 440977 [Multi-domain]  Cd Length: 93  Bit Score: 45.62  E-value: 5.86e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1125798322  1 MTLCGDLQAPQVNDLWQRRADWWQDDR----LDLGGVTTLDSAGLALLVKWAKAALARGATPQLVGAS 64
Cdd:COG1366   13 LPLIGELDAARAPELREALLEALETGArrvvLDLSGVTFIDSSGLGALLSLAKAARLLGGRLVLVGVS 80
STAS pfam01740
STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is ...
 14-90 1.11e-04

STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is found in the C terminal region of Sulphate transporters and bacterial antisigma factor antagonists. It has been suggested that this domain may have a general NTP binding function.


Pssm-ID: 426404 [Multi-domain]  Cd Length: 106  Bit Score: 37.59  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125798322  14 DLWQRR-ADWWQDDR-----LDLGGVTTLDSAGLALLVKWAKAALARGATPQLVGASSDFYTLANLYGVAGLFQsTPLTT 87
Cdd:pfam01740  25 ESLRERlLRALEEGEikhvvLDLSAVPFIDSSGLGALEELYKELRRRGVELVLVGPSPEVARTLEKTGLDDIIK-IFPTV 103


                  ...
gi 1125798322  88 EDA 90
Cdd:pfam01740 104 AEA 106
ant_ant_sig TIGR00377
anti-anti-sigma factor; This superfamily includes small (105-125 residue) proteins related to ...
 28-89 1.90e-03

anti-anti-sigma factor; This superfamily includes small (105-125 residue) proteins related to SpoIIAA of Bacillus subtilis, an anti-anti-sigma factor. SpoIIAA can bind to and inhibit the anti-sigma F factor SpoIIAB. Also, it can be phosphorylated by SpoIIAB on a Ser residue at position 59 of the seed alignment. A similar arrangement is inferred for RsbV, an anti-anti-sigma factor for sigma B. This Ser is fairly well conserved within a motif resembling MXS[STA]G[VIL]X[VIL][VILF] among homologous known or predicted anti-anti-sigma factors. Regions similar to SpoIIAA and apparently homologous, but differing considerably near the phosphorlated Ser of SpoIIAA, appear in a single copy in several longer proteins. [Regulatory functions, Protein interactions]


Pssm-ID: 273042 [Multi-domain]  Cd Length: 108  Bit Score: 34.50  E-value: 1.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125798322  28 LDLGGVTTLDSAGLALLVKWAKAALARGATPQLVGASSdfyTLANLYGVAGLFQSTPL-TTED 89
Cdd:TIGR00377  48 LDLEDLEFMDSSGLGVLLGRYKQVRRVGGQLVLVSVSP---RVARLLDITGLLRIIPIyPTVE 107
 
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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