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Conserved domains on  [gi|505182401|ref|WP_015369503|]
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MULTISPECIES: lipid asymmetry maintenance protein MlaB [Klebsiella]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
mlaB_1 NF033618
lipid asymmetry maintenance protein MlaB; MlaB belongs to a system that maintains asymmetry in ...
3-96 1.98e-48

lipid asymmetry maintenance protein MlaB; MlaB belongs to a system that maintains asymmetry in the outer membrane of Gram-negative bacteria, with LPS in the outer leaflet and phospholipids in the inner leaflet. Several components of the system share homology with typical ABC transporters.


:

Pssm-ID: 411237  Cd Length: 94  Bit Score: 148.81  E-value: 1.98e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182401  3 EQLSWNRDGERLALRGELDQEFILPLWNARAQATDGVSTIDLSDVSRVDSAGVALLVHFVALVRRQGKTAQVVGKSENLQ 82
Cdd:NF033618  1 EALSWEREGDTLALSGELDRDTLLPLWQQREELLAGVTCIDVSGLERVDSAGLALLVHLRAEARQQGRELKISGVSDRLR 80
                        90
                ....*....|....
gi 505182401 83 TLVSLYNLPADMIP 96
Cdd:NF033618 81 TLITLYNLPEIILP 94
 
Name Accession Description Interval E-value
mlaB_1 NF033618
lipid asymmetry maintenance protein MlaB; MlaB belongs to a system that maintains asymmetry in ...
3-96 1.98e-48

lipid asymmetry maintenance protein MlaB; MlaB belongs to a system that maintains asymmetry in the outer membrane of Gram-negative bacteria, with LPS in the outer leaflet and phospholipids in the inner leaflet. Several components of the system share homology with typical ABC transporters.


Pssm-ID: 411237  Cd Length: 94  Bit Score: 148.81  E-value: 1.98e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182401  3 EQLSWNRDGERLALRGELDQEFILPLWNARAQATDGVSTIDLSDVSRVDSAGVALLVHFVALVRRQGKTAQVVGKSENLQ 82
Cdd:NF033618  1 EALSWEREGDTLALSGELDRDTLLPLWQQREELLAGVTCIDVSGLERVDSAGLALLVHLRAEARQQGRELKISGVSDRLR 80
                        90
                ....*....|....
gi 505182401 83 TLVSLYNLPADMIP 96
Cdd:NF033618 81 TLITLYNLPEIILP 94
MlaB COG3113
Binding protein subunit MlaB of the ABC-type intermembrane phospholipid transporter Mla, ...
1-94 6.39e-29

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: 99.55  E-value: 6.39e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182401  1 MSEQLSWNRDGERLALRGELDQEFILPLWNARAQ--ATDGVSTIDLSDVSRVDSAGVALLVHFVALVRRQGKTAQVVGKS 78
Cdd:COG3113   1 MSEALLWNAEGGTLRLSGELTRDTVLALWAQLLAllAAGGAVEIDLSGVTRVDSAGLALLLELLREARAQGKTLRLTGVP 80
                        90
                ....*....|....*.
gi 505182401 79 ENLQTLVSLYNLPADM 94
Cdd:COG3113  81 EQLRTLAALYGLDELL 96
STAS_2 pfam13466
STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is ...
14-90 3.04e-10

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: 51.46  E-value: 3.04e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505182401  14 LALRGELDQEFILPLWNARAQA--TDGVSTIDLSDVSRVDSAGVALLVHFVALVRRQGKTAQVVGKSENLQTLVSLYNL 90
Cdd:pfam13466  1 LSLSGELDADTAPALREALLAAlaAGSPVVVDLSGVERVDSAGLALLLALARRARARGKRLVLRGLPPALLRLLRLLGL 79
STAS_anti-anti-sigma_factors cd07043
Sulphate Transporter and Anti-Sigma factor antagonist) domain of anti-anti-sigma factors, key ...
4-90 1.00e-07

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: 45.59  E-value: 1.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182401  4 QLSWNRDGERLALRGELDQEFILPLWNARAQATDGVST---IDLSDVSRVDSAGVALLVHFVALVRRQGKTAQVVGKSEN 80
Cdd:cd07043   2 TVEERGGVLVVRLSGELDAATAPELREALEELLAEGPRrlvLDLSGVTFIDSSGLGVLLGAYKRARAAGGRLVLVNVSPA 81
                        90
                ....*....|
gi 505182401 81 LQTLVSLYNL 90
Cdd:cd07043  82 VRRVLELTGL 91
ant_ant_sig TIGR00377
anti-anti-sigma factor; This superfamily includes small (105-125 residue) proteins related to ...
14-79 4.95e-04

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: 36.04  E-value: 4.95e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505182401   14 LALRGELD-------QEFILPlWNARAQATDGVstIDLSDVSRVDSAGVALLVHFVALVRRQGKTAQVVGKSE 79
Cdd:TIGR00377  16 VRLSGELDahtapllREKVTP-AAERTGIRPIV--LDLEDLEFMDSSGLGVLLGRYKQVRRVGGQLVLVSVSP 85
 
Name Accession Description Interval E-value
mlaB_1 NF033618
lipid asymmetry maintenance protein MlaB; MlaB belongs to a system that maintains asymmetry in ...
3-96 1.98e-48

lipid asymmetry maintenance protein MlaB; MlaB belongs to a system that maintains asymmetry in the outer membrane of Gram-negative bacteria, with LPS in the outer leaflet and phospholipids in the inner leaflet. Several components of the system share homology with typical ABC transporters.


Pssm-ID: 411237  Cd Length: 94  Bit Score: 148.81  E-value: 1.98e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182401  3 EQLSWNRDGERLALRGELDQEFILPLWNARAQATDGVSTIDLSDVSRVDSAGVALLVHFVALVRRQGKTAQVVGKSENLQ 82
Cdd:NF033618  1 EALSWEREGDTLALSGELDRDTLLPLWQQREELLAGVTCIDVSGLERVDSAGLALLVHLRAEARQQGRELKISGVSDRLR 80
                        90
                ....*....|....
gi 505182401 83 TLVSLYNLPADMIP 96
Cdd:NF033618 81 TLITLYNLPEIILP 94
MlaB COG3113
Binding protein subunit MlaB of the ABC-type intermembrane phospholipid transporter Mla, ...
1-94 6.39e-29

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: 99.55  E-value: 6.39e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182401  1 MSEQLSWNRDGERLALRGELDQEFILPLWNARAQ--ATDGVSTIDLSDVSRVDSAGVALLVHFVALVRRQGKTAQVVGKS 78
Cdd:COG3113   1 MSEALLWNAEGGTLRLSGELTRDTVLALWAQLLAllAAGGAVEIDLSGVTRVDSAGLALLLELLREARAQGKTLRLTGVP 80
                        90
                ....*....|....*.
gi 505182401 79 ENLQTLVSLYNLPADM 94
Cdd:COG3113  81 EQLRTLAALYGLDELL 96
STAS_2 pfam13466
STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is ...
14-90 3.04e-10

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: 51.46  E-value: 3.04e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505182401  14 LALRGELDQEFILPLWNARAQA--TDGVSTIDLSDVSRVDSAGVALLVHFVALVRRQGKTAQVVGKSENLQTLVSLYNL 90
Cdd:pfam13466  1 LSLSGELDADTAPALREALLAAlaAGSPVVVDLSGVERVDSAGLALLLALARRARARGKRLVLRGLPPALLRLLRLLGL 79
STAS_anti-anti-sigma_factors cd07043
Sulphate Transporter and Anti-Sigma factor antagonist) domain of anti-anti-sigma factors, key ...
4-90 1.00e-07

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: 45.59  E-value: 1.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182401  4 QLSWNRDGERLALRGELDQEFILPLWNARAQATDGVST---IDLSDVSRVDSAGVALLVHFVALVRRQGKTAQVVGKSEN 80
Cdd:cd07043   2 TVEERGGVLVVRLSGELDAATAPELREALEELLAEGPRrlvLDLSGVTFIDSSGLGVLLGAYKRARAAGGRLVLVNVSPA 81
                        90
                ....*....|
gi 505182401 81 LQTLVSLYNL 90
Cdd:cd07043  82 VRRVLELTGL 91
SpoIIAA COG1366
Anti-anti-sigma regulatory factor (antagonist of anti-sigma factor) [Signal transduction ...
14-90 6.96e-06

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


Pssm-ID: 440977 [Multi-domain]  Cd Length: 93  Bit Score: 40.61  E-value: 6.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182401 14 LALRGELD----QEFILPLWNARAQATDGVsTIDLSDVSRVDSAGVALLVHFVALVRRQGKTAQVVGKSENLQTLVSLYN 89
Cdd:COG1366  13 LPLIGELDaaraPELREALLEALETGARRV-VLDLSGVTFIDSSGLGALLSLAKAARLLGGRLVLVGVSPAVARVLELTG 91

                .
gi 505182401 90 L 90
Cdd:COG1366  92 L 92
ant_ant_sig TIGR00377
anti-anti-sigma factor; This superfamily includes small (105-125 residue) proteins related to ...
14-79 4.95e-04

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: 36.04  E-value: 4.95e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505182401   14 LALRGELD-------QEFILPlWNARAQATDGVstIDLSDVSRVDSAGVALLVHFVALVRRQGKTAQVVGKSE 79
Cdd:TIGR00377  16 VRLSGELDahtapllREKVTP-AAERTGIRPIV--LDLEDLEFMDSSGLGVLLGRYKQVRRVGGQLVLVSVSP 85
STAS pfam01740
STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is ...
14-69 1.03e-03

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: 35.28  E-value: 1.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182401   14 LALRGELD----QEFILPLWNARAQATDGVSTIDLSDVSRVDSAGVALLVHFVALVRRQG 69
Cdd:pfam01740  13 LRLDGPLDfanaESLRERLLRALEEGEIKHVVLDLSAVPFIDSSGLGALEELYKELRRRG 72
 
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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