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Conserved domains on  [gi|754574566|ref|WP_041967776|]
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MULTISPECIES: STAS domain-containing protein [Bacillaceae]

Protein Classification

STAS domain-containing protein( domain architecture ID 10162406)

STAS (Sulphate Transporter and Anti-Sigma factor antagonist) domain-containing protein similar to Bacillus subtilis stressosome complex proteins RsbS, RsbRB, and RsbRC, which function in the environmental signaling branch of the general stress response

CATH:  3.30.750.24
Gene Ontology:  GO:0043856|GO:0006355
PubMed:  10662676|22116355
SCOP:  4003567

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
STAS_RsbR_RsbS_like cd07041
Sulphate Transporter and Anti-Sigma factor antagonist domain of the "stressosome" complex ...
 2-109 2.42e-35

Sulphate Transporter and Anti-Sigma factor antagonist domain of the "stressosome" complex proteins RsbS and RsbR, regulators of the bacterial stress activated alternative sigma factor sigma-B by phosphorylation; The STAS (Sulphate Transporter and Anti-Sigma factor antagonist) domain of proteins related to RsbS and RsbR which are part of the "stressosome" complex that plays an important role in the regulation of the bacterial stress activated alternative sigma factor sigma-B. During stress conditions RsbS and RsbR are phosphorylated which leads to the release of RsbT, an activator of of the RsbU phosphatase, which in turn activates RsbV which leads to the release and activation of sigma factor B. RsbS is a single domain protein (STAS domain), while RsbR-like proteins have a well-conserved C-terminal STATS domain and a variable N-terminal domain. The STAS domain is also found in the C- terminal region of sulphate transporters and anti-anti-sigma factors.


:

Pssm-ID: 132912  Cd Length: 109  Bit Score: 117.17  E-value: 2.42e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754574566   2 RIPILKL-DDCLLVSIQWELDDQTALQFQEDLLHKIHETSANGVVIDLTSIDFIDSFIAKVLGDVINMSKLMGAIVVITG 80
Cdd:cd07041    1 STPIIPVwDGVLVLPLIGDLDDERAEQLQERLLEAISRRRARGVIIDLTGVPVIDSAVARHLLRLARALRLLGARTILTG 80

                         90       100
                 ....*....|....*....|....*....
gi 754574566  81 IQPAVAITLIELGIGLDDVLTALDLEKGL 109
Cdd:cd07041   81 IRPEVAQTLVELGIDLSGIRTAATLQQAL 109
 
Name Accession Description Interval E-value
STAS_RsbR_RsbS_like cd07041
Sulphate Transporter and Anti-Sigma factor antagonist domain of the "stressosome" complex ...
 2-109 2.42e-35

Sulphate Transporter and Anti-Sigma factor antagonist domain of the "stressosome" complex proteins RsbS and RsbR, regulators of the bacterial stress activated alternative sigma factor sigma-B by phosphorylation; The STAS (Sulphate Transporter and Anti-Sigma factor antagonist) domain of proteins related to RsbS and RsbR which are part of the "stressosome" complex that plays an important role in the regulation of the bacterial stress activated alternative sigma factor sigma-B. During stress conditions RsbS and RsbR are phosphorylated which leads to the release of RsbT, an activator of of the RsbU phosphatase, which in turn activates RsbV which leads to the release and activation of sigma factor B. RsbS is a single domain protein (STAS domain), while RsbR-like proteins have a well-conserved C-terminal STATS domain and a variable N-terminal domain. The STAS domain is also found in the C- terminal region of sulphate transporters and anti-anti-sigma factors.


Pssm-ID: 132912  Cd Length: 109  Bit Score: 117.17  E-value: 2.42e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754574566   2 RIPILKL-DDCLLVSIQWELDDQTALQFQEDLLHKIHETSANGVVIDLTSIDFIDSFIAKVLGDVINMSKLMGAIVVITG 80
Cdd:cd07041    1 STPIIPVwDGVLVLPLIGDLDDERAEQLQERLLEAISRRRARGVIIDLTGVPVIDSAVARHLLRLARALRLLGARTILTG 80

                         90       100
                 ....*....|....*....|....*....
gi 754574566  81 IQPAVAITLIELGIGLDDVLTALDLEKGL 109
Cdd:cd07041   81 IRPEVAQTLVELGIDLSGIRTAATLQQAL 109
SpoIIAA COG1366
Anti-anti-sigma regulatory factor (antagonist of anti-sigma factor) [Signal transduction ...
 2-94 7.37e-17

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


Pssm-ID: 440977 [Multi-domain]  Cd Length: 93  Bit Score: 69.50  E-value: 7.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754574566   2 RIPILKLDDCLLVSIQWELDDQTALQFQEDLLHKIhETSANGVVIDLTSIDFIDSFIAKVLGDVINMSKLMGAIVVITGI 81
Cdd:COG1366    1 SIPVEVRDGVLVLPLIGELDAARAPELREALLEAL-ETGARRVVLDLSGVTFIDSSGLGALLSLAKAARLLGGRLVLVGV 79

                         90
                 ....*....|...
gi 754574566  82 QPAVAITLIELGI 94
Cdd:COG1366   80 SPAVARVLELTGL 92
STAS pfam01740
STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is ...
 2-89 5.02e-14

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: 62.63  E-value: 5.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754574566    2 RIPILKLDDCLLVSIQWELDDQTALQFQEDLLHKIHETSANGVVIDLTSIDFIDSFIAKVLGDVINMSKLMGAIVVITGI 81
Cdd:pfam01740   1 YPEAEEIPGILILRLDGPLDFANAESLRERLLRALEEGEIKHVVLDLSAVPFIDSSGLGALEELYKELRRRGVELVLVGP 80


                  ....*...
gi 754574566   82 QPAVAITL 89
Cdd:pfam01740  81 SPEVARTL 88
ant_ant_sig TIGR00377
anti-anti-sigma factor; This superfamily includes small (105-125 residue) proteins related to ...
 1-101 3.51e-05

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: 39.89  E-value: 3.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754574566    1 MRIPILKLDDCLLVSIQWELDDQTALQFQEDLLHKIHETSANGVVIDLTSIDFIDSFIAKVLGDVINMSKLMGAIVVITG 80
Cdd:TIGR00377   3 LNIETEVQEGVVVVRLSGELDAHTAPLLREKVTPAAERTGIRPIVLDLEDLEFMDSSGLGVLLGRYKQVRRVGGQLVLVS 82

                          90       100
                  ....*....|....*....|.
gi 754574566   81 IQPAVAiTLIELGiGLDDVLT 101
Cdd:TIGR00377  83 VSPRVA-RLLDIT-GLLRIIP 101
 
Name Accession Description Interval E-value
STAS_RsbR_RsbS_like cd07041
Sulphate Transporter and Anti-Sigma factor antagonist domain of the "stressosome" complex ...
 2-109 2.42e-35

Sulphate Transporter and Anti-Sigma factor antagonist domain of the "stressosome" complex proteins RsbS and RsbR, regulators of the bacterial stress activated alternative sigma factor sigma-B by phosphorylation; The STAS (Sulphate Transporter and Anti-Sigma factor antagonist) domain of proteins related to RsbS and RsbR which are part of the "stressosome" complex that plays an important role in the regulation of the bacterial stress activated alternative sigma factor sigma-B. During stress conditions RsbS and RsbR are phosphorylated which leads to the release of RsbT, an activator of of the RsbU phosphatase, which in turn activates RsbV which leads to the release and activation of sigma factor B. RsbS is a single domain protein (STAS domain), while RsbR-like proteins have a well-conserved C-terminal STATS domain and a variable N-terminal domain. The STAS domain is also found in the C- terminal region of sulphate transporters and anti-anti-sigma factors.


Pssm-ID: 132912  Cd Length: 109  Bit Score: 117.17  E-value: 2.42e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754574566   2 RIPILKL-DDCLLVSIQWELDDQTALQFQEDLLHKIHETSANGVVIDLTSIDFIDSFIAKVLGDVINMSKLMGAIVVITG 80
Cdd:cd07041    1 STPIIPVwDGVLVLPLIGDLDDERAEQLQERLLEAISRRRARGVIIDLTGVPVIDSAVARHLLRLARALRLLGARTILTG 80

                         90       100
                 ....*....|....*....|....*....
gi 754574566  81 IQPAVAITLIELGIGLDDVLTALDLEKGL 109
Cdd:cd07041   81 IRPEVAQTLVELGIDLSGIRTAATLQQAL 109
SpoIIAA COG1366
Anti-anti-sigma regulatory factor (antagonist of anti-sigma factor) [Signal transduction ...
 2-94 7.37e-17

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


Pssm-ID: 440977 [Multi-domain]  Cd Length: 93  Bit Score: 69.50  E-value: 7.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754574566   2 RIPILKLDDCLLVSIQWELDDQTALQFQEDLLHKIhETSANGVVIDLTSIDFIDSFIAKVLGDVINMSKLMGAIVVITGI 81
Cdd:COG1366    1 SIPVEVRDGVLVLPLIGELDAARAPELREALLEAL-ETGARRVVLDLSGVTFIDSSGLGALLSLAKAARLLGGRLVLVGV 79

                         90
                 ....*....|...
gi 754574566  82 QPAVAITLIELGI 94
Cdd:COG1366   80 SPAVARVLELTGL 92
STAS cd06844
Sulphate Transporter and Anti-Sigma factor antagonist domain found in the C-terminal region of ...
 3-96 4.38e-14

Sulphate Transporter and Anti-Sigma factor antagonist domain found in the C-terminal region of sulphate transporters as well as in bacterial and archaeal proteins involved in the regulation of sigma factors; The STAS (Sulphate Transporter and Anti-Sigma factor antagonist) domain is found in the C-terminal region of sulphate transporters as well as in bacterial and archaeal proteins involved in the regulation of sigma factors, like anti-anti-sigma factors and "stressosome" components. The sigma factor regulators are involved in protein-protein interaction which is regulated by phosphorylation.


Pssm-ID: 132911 [Multi-domain]  Cd Length: 100  Bit Score: 62.88  E-value: 4.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754574566   3 IPILKLDDCLLVSIQWELDDQTALQFQEDLLHKIHETSANGVVIDLTSIDFIDSFIAKVLGDVINMSKLMGAIVVITGIQ 82
Cdd:cd06844    1 VPLEKVDDYWVVRLEGELDHHSVEQFKEELLHNITNVAGKTIVIDISALEFMDSSGTGVLLERSRLAEAVGGQFVLTGIS 80

                         90
                 ....*....|....
gi 754574566  83 PAVAITLIELGIGL 96
Cdd:cd06844   81 PAVRITLTESGLDK 94
STAS pfam01740
STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is ...
 2-89 5.02e-14

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: 62.63  E-value: 5.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754574566    2 RIPILKLDDCLLVSIQWELDDQTALQFQEDLLHKIHETSANGVVIDLTSIDFIDSFIAKVLGDVINMSKLMGAIVVITGI 81
Cdd:pfam01740   1 YPEAEEIPGILILRLDGPLDFANAESLRERLLRALEEGEIKHVVLDLSAVPFIDSSGLGALEELYKELRRRGVELVLVGP 80


                  ....*...
gi 754574566   82 QPAVAITL 89
Cdd:pfam01740  81 SPEVARTL 88
STAS_anti-anti-sigma_factors cd07043
Sulphate Transporter and Anti-Sigma factor antagonist) domain of anti-anti-sigma factors, key ...
 9-101 2.65e-05

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: 39.81  E-value: 2.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754574566   9 DDCLLVSIQWELDDQTALQFQEDLLHKIHETSANgVVIDLTSIDFIDSFIAKVLGDVINMSKLMGAIVVITGIQPAVAiT 88
Cdd:cd07043    7 GGVLVVRLSGELDAATAPELREALEELLAEGPRR-LVLDLSGVTFIDSSGLGVLLGAYKRARAAGGRLVLVNVSPAVR-R 84

                         90
                 ....*....|...
gi 754574566  89 LIELgIGLDDVLT 101
Cdd:cd07043   85 VLEL-TGLDRLFP 96
ant_ant_sig TIGR00377
anti-anti-sigma factor; This superfamily includes small (105-125 residue) proteins related to ...
 1-101 3.51e-05

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: 39.89  E-value: 3.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754574566    1 MRIPILKLDDCLLVSIQWELDDQTALQFQEDLLHKIHETSANGVVIDLTSIDFIDSFIAKVLGDVINMSKLMGAIVVITG 80
Cdd:TIGR00377   3 LNIETEVQEGVVVVRLSGELDAHTAPLLREKVTPAAERTGIRPIVLDLEDLEFMDSSGLGVLLGRYKQVRRVGGQLVLVS 82

                          90       100
                  ....*....|....*....|.
gi 754574566   81 IQPAVAiTLIELGiGLDDVLT 101
Cdd:TIGR00377  83 VSPRVA-RLLDIT-GLLRIIP 101
SpoIIAA COG5815
Stage II sporulation protein SpoIIAA (antagonist of anti-sigma F factor) [Cell cycle control, ...
 1-85 6.26e-05

Stage II sporulation protein SpoIIAA (antagonist of anti-sigma F factor) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444517  Cd Length: 110  Bit Score: 38.96  E-value: 6.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754574566   1 MRIPILKLDDCLLVSIQWELDDQTALQFQEDLLHKIHETSANGVVIDLTSIDFIDS-FIAKVLGDVINMSKLmGAIVVIT 79
Cdd:COG5815    1 MEVDFEKKGDTLIVRLEGELDHHTAEELREKIDRAIEKGGVKHLILNLEGVSFMDSsGLGVILGRYKKIKAL-GGKVAVI 79


                 ....*.
gi 754574566  80 GIQPAV 85
Cdd:COG5815   80 NVSPQV 85
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
73-107 1.65e-03

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 36.38  E-value: 1.65e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 754574566  73 GAIVVITGIQPAVAITLIELGIG-LDDVLTALDLEK 107
Cdd:COG1148  244 GAIVLATGFKPYDPTKLGEYGYGkYPNVITNLELER 279
SUL1 COG0659
Sulfate permease or related transporter, MFS superfamily [Inorganic ion transport and ...
 24-115 3.57e-03

Sulfate permease or related transporter, MFS superfamily [Inorganic ion transport and metabolism];


Pssm-ID: 440424 [Multi-domain]  Cd Length: 529  Bit Score: 35.47  E-value: 3.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754574566  24 TALQFQEDLLHKIHETSAngVVIDLTSIDFIDSFIAKVLGDVINMSKLMGAIVVITGIQPAVAITLIELGIG--LDDVLT 101
Cdd:COG0659  436 NAERLKERLDALAPDPRV--VILDLSAVPFIDATALEALEELAERLRARGITLELAGLKPPVRDLLERAGLLdeLGEERV 513

                         90
                 ....*....|....
gi 754574566 102 ALDLEKGLEKLQQE 115
Cdd:COG0659  514 FPDLDEALEAAEER 527
spore_II_AA TIGR02886
anti-sigma F factor antagonist; The anti-sigma F factor antagonist, also called stage II ...
 7-85 3.76e-03

anti-sigma F factor antagonist; The anti-sigma F factor antagonist, also called stage II sporulation protein AA, is a protein universal among endospore-forming bacteria, all of which belong to the Firmcutes [Regulatory functions, Protein interactions, Cellular processes, Sporulation and germination]


Pssm-ID: 131932  Cd Length: 106  Bit Score: 34.16  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754574566    7 KLDDCLLVSIQWELDDQTALQFQEDLLHKIHETSANGVVIDLTSIDFIDS-FIAKVLGDVINMSKLMGAIVVItGIQPAV 85
Cdd:TIGR02886   5 VKGDVLIVRLSGELDHHTAERVRRKIDDAIERRPIKHLILNLKNVTFMDSsGLGVILGRYKKIKNEGGEVIVC-NVSPAV 83
 
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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