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Conserved domains on  [gi|490890582|ref|WP_004752535|]
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lipid asymmetry maintenance protein MlaB [Leptospira kirschneri]

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, ...
7-102 1.61e-17

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: 71.43  E-value: 1.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490890582   7 TDFQESDVPTLKVRIEDELTIYEASEFKEKINLILKnSAAVLEIDLFKIQKIDTSCLQILLSFKKVALTKYEQVRFVNFS 86
Cdd:COG3113    2 SEALLWNAEGGTLRLSGELTRDTVLALWAQLLALLA-AGGAVEIDLSGVTRVDSAGLALLLELLREARAQGKTLRLTGVP 80
                         90
                 ....*....|....*.
gi 490890582  87 NNVLSLIDLYNLSDFF 102
Cdd:COG3113   81 EQLRTLAALYGLDELL 96
 
Name Accession Description Interval E-value
MlaB COG3113
Binding protein subunit MlaB of the ABC-type intermembrane phospholipid transporter Mla, ...
7-102 1.61e-17

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: 71.43  E-value: 1.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490890582   7 TDFQESDVPTLKVRIEDELTIYEASEFKEKINLILKnSAAVLEIDLFKIQKIDTSCLQILLSFKKVALTKYEQVRFVNFS 86
Cdd:COG3113    2 SEALLWNAEGGTLRLSGELTRDTVLALWAQLLALLA-AGGAVEIDLSGVTRVDSAGLALLLELLREARAQGKTLRLTGVP 80
                         90
                 ....*....|....*.
gi 490890582  87 NNVLSLIDLYNLSDFF 102
Cdd:COG3113   81 EQLRTLAALYGLDELL 96
STAS_anti-anti-sigma_factors cd07043
Sulphate Transporter and Anti-Sigma factor antagonist) domain of anti-anti-sigma factors, key ...
16-103 4.89e-12

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: 57.53  E-value: 4.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490890582  16 TLKVRIEDELTIYEASEFKEKINLILKNSAAVLEIDLFKIQKIDTSCLQILLSFKKVALTKYEQVRFVNFSNNVLSLIDL 95
Cdd:cd07043    9 VLVVRLSGELDAATAPELREALEELLAEGPRRLVLDLSGVTFIDSSGLGVLLGAYKRARAAGGRLVLVNVSPAVRRVLEL 88

                 ....*...
gi 490890582  96 YNLSDFFR 103
Cdd:cd07043   89 TGLDRLFP 96
STAS_2 pfam13466
STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is ...
19-99 1.81e-06

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: 42.60  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490890582   19 VRIEDELTIYEASEFKEKINLILKNSAAVlEIDLFKIQKIDTSCLQILLSFKKVALTKYEQVRFVNFSNNVLSLIDLYNL 98
Cdd:pfam13466   1 LSLSGELDADTAPALREALLAALAAGSPV-VVDLSGVERVDSAGLALLLALARRARARGKRLVLRGLPPALLRLLRLLGL 79

                  .
gi 490890582   99 S 99
Cdd:pfam13466  80 D 80
 
Name Accession Description Interval E-value
MlaB COG3113
Binding protein subunit MlaB of the ABC-type intermembrane phospholipid transporter Mla, ...
7-102 1.61e-17

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: 71.43  E-value: 1.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490890582   7 TDFQESDVPTLKVRIEDELTIYEASEFKEKINLILKnSAAVLEIDLFKIQKIDTSCLQILLSFKKVALTKYEQVRFVNFS 86
Cdd:COG3113    2 SEALLWNAEGGTLRLSGELTRDTVLALWAQLLALLA-AGGAVEIDLSGVTRVDSAGLALLLELLREARAQGKTLRLTGVP 80
                         90
                 ....*....|....*.
gi 490890582  87 NNVLSLIDLYNLSDFF 102
Cdd:COG3113   81 EQLRTLAALYGLDELL 96
STAS_anti-anti-sigma_factors cd07043
Sulphate Transporter and Anti-Sigma factor antagonist) domain of anti-anti-sigma factors, key ...
16-103 4.89e-12

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: 57.53  E-value: 4.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490890582  16 TLKVRIEDELTIYEASEFKEKINLILKNSAAVLEIDLFKIQKIDTSCLQILLSFKKVALTKYEQVRFVNFSNNVLSLIDL 95
Cdd:cd07043    9 VLVVRLSGELDAATAPELREALEELLAEGPRRLVLDLSGVTFIDSSGLGVLLGAYKRARAAGGRLVLVNVSPAVRRVLEL 88

                 ....*...
gi 490890582  96 YNLSDFFR 103
Cdd:cd07043   89 TGLDRLFP 96
SpoIIAA COG1366
Anti-anti-sigma regulatory factor (antagonist of anti-sigma factor) [Signal transduction ...
16-98 5.55e-07

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


Pssm-ID: 440977 [Multi-domain]  Cd Length: 93  Bit Score: 44.07  E-value: 5.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490890582  16 TLKVRIEDELTIYEASEFKEKINLILKNSAAVLEIDLFKIQKIDTSCLQILLSFKKVALTKYEQVRFVNFSNNVLSLIDL 95
Cdd:COG1366   10 VLVLPLIGELDAARAPELREALLEALETGARRVVLDLSGVTFIDSSGLGALLSLAKAARLLGGRLVLVGVSPAVARVLEL 89

                 ...
gi 490890582  96 YNL 98
Cdd:COG1366   90 TGL 92
STAS_2 pfam13466
STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is ...
19-99 1.81e-06

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: 42.60  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490890582   19 VRIEDELTIYEASEFKEKINLILKNSAAVlEIDLFKIQKIDTSCLQILLSFKKVALTKYEQVRFVNFSNNVLSLIDLYNL 98
Cdd:pfam13466   1 LSLSGELDADTAPALREALLAALAAGSPV-VVDLSGVERVDSAGLALLLALARRARARGKRLVLRGLPPALLRLLRLLGL 79

                  .
gi 490890582   99 S 99
Cdd:pfam13466  80 D 80
STAS pfam01740
STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is ...
16-103 6.05e-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: 36.44  E-value: 6.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490890582   16 TLKVRIEDELTIYEASEFKEKI-NLILKNSAAVLEIDLFKIQKIDTSCLQILLSFKKVALTKYEQVRFVNFSNNVLSLID 94
Cdd:pfam01740  10 ILILRLDGPLDFANAESLRERLlRALEEGEIKHVVLDLSAVPFIDSSGLGALEELYKELRRRGVELVLVGPSPEVARTLE 89

                  ....*....
gi 490890582   95 LYNLSDFFR 103
Cdd:pfam01740  90 KTGLDDIIK 98
 
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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