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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995559670   2 RIPILKLYD-YLLVSIQWELDDQTAIQFQEDLLSKIHQTGAKGVVIDLTSIDMIDSFIAKVLGDVVSMSNLMGARVVLTG 80
Cdd:cd07041     1 STPIIPVWDgVLVLPLIGDLDDERAEQLQERLLEAISRRRARGVIIDLTGVPVIDSAVARHLLRLARALRLLGARTILTG 80

                          90       100
                  ....*....|....*....|....*....
gi 1995559670  81 IQPAVAITLVELGIGLNDVLTALDLEKGL 109
Cdd:cd07041    81 IRPEVAQTLVELGIDLSGIRTAATLQQAL 109

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995559670   2 RIPILKLYD-YLLVSIQWELDDQTAIQFQEDLLSKIHQTGAKGVVIDLTSIDMIDSFIAKVLGDVVSMSNLMGARVVLTG 80
Cdd:cd07041     1 STPIIPVWDgVLVLPLIGDLDDERAEQLQERLLEAISRRRARGVIIDLTGVPVIDSAVARHLLRLARALRLLGARTILTG 80

                          90       100
                  ....*....|....*....|....*....
gi 1995559670  81 IQPAVAITLVELGIGLNDVLTALDLEKGL 109
Cdd:cd07041    81 IRPEVAQTLVELGIDLSGIRTAATLQQAL 109

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995559670  12 LLVSIQWELDDQTAIQFQEDLLSKIHQTGAKGVVIDLTSIDMIDSFIAKVLGDVVSMSNLMGARVVLTGIQPAVAITLVE 91
Cdd:pfam01740  11 LILRLDGPLDFANAESLRERLLRALEEGEIKHVVLDLSAVPFIDSSGLGALEELYKELRRRGVELVLVGPSPEVARTLEK 90

                  ...
gi 1995559670  92 LGI 94
Cdd:pfam01740  91 TGL 93

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995559670   2 RIPILKLYD-YLLVSIQWELDDQTAIQFQEDLLSKIHQTGAKGVVIDLTSIDMIDSFIAKVLGDVVSMSNLMGARVVLTG 80
Cdd:cd07041     1 STPIIPVWDgVLVLPLIGDLDDERAEQLQERLLEAISRRRARGVIIDLTGVPVIDSAVARHLLRLARALRLLGARTILTG 80

                          90       100
                  ....*....|....*....|....*....
gi 1995559670  81 IQPAVAITLVELGIGLNDVLTALDLEKGL 109
Cdd:cd07041    81 IRPEVAQTLVELGIDLSGIRTAATLQQAL 109

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995559670   3 IPILKLYDYLLVSIQWELDDQTAIQFQEDLLSKIHQTGAKGVVIDLTSIDMIDSFIAKVLGDVVSMSNLMGARVVLTGIQ 82
Cdd:cd06844     1 VPLEKVDDYWVVRLEGELDHHSVEQFKEELLHNITNVAGKTIVIDISALEFMDSSGTGVLLERSRLAEAVGGQFVLTGIS 80

                          90
                  ....*....|....
gi 1995559670  83 PAVAITLVELGIGL 96
Cdd:cd06844    81 PAVRITLTESGLDK 94

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995559670   1 MRIPILKLYDYLLVSIQWELDDQTAIQFQEDLLSKIHQTGAKGVVIDLTSIDMIDSFIAKVLGDVVSMSNLMGARVVLTG 80
Cdd:TIGR00377   3 LNIETEVQEGVVVVRLSGELDAHTAPLLREKVTPAAERTGIRPIVLDLEDLEFMDSSGLGVLLGRYKQVRRVGGQLVLVS 82

                  ....*....
gi 1995559670  81 IQPAVAITL 89
Cdd:TIGR00377  83 VSPRVARLL 91

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995559670  10 DYLLVSIQWELDDQTAIQFQEDLLSKIHQtGAKGVVIDLTSIDMIDSFiakVLGDVVSMSNLM---GARVVLTGIQPAVA 86
Cdd:cd07043     8 GVLVVRLSGELDAATAPELREALEELLAE-GPRRLVLDLSGVTFIDSS---GLGVLLGAYKRAraaGGRLVLVNVSPAVR 83

                          90
                  ....*....|....*
gi 1995559670  87 ITLvELgIGLNDVLT 101
Cdd:cd07043    84 RVL-EL-TGLDRLFP 96

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995559670  24 TAIQFQEDLLSkiHQTGAKGVVIDLTSIDMIDSFIAKVLGDVVSMSNLMGARVVLTGIQPAVAITLVELGIG--LNDVLT 101
Cdd:COG0659   436 NAERLKERLDA--LAPDPRVVILDLSAVPFIDATALEALEELAERLRARGITLELAGLKPPVRDLLERAGLLdeLGEERV 513

                          90
                  ....*....|....
gi 1995559670 102 ALDLEKGLEKLQSE 115
Cdd:COG0659   514 FPDLDEALEAAEER 527