SPX_BACSU
ID SPX_BACSU Reviewed; 131 AA.
AC O31602;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Global transcriptional regulator Spx {ECO:0000255|HAMAP-Rule:MF_01132, ECO:0000303|PubMed:17908206};
DE AltName: Full=Redox-responsive transcription factor Spx;
DE AltName: Full=Suppressor of clpP and clpX {ECO:0000303|PubMed:12028382};
DE Short=Spx {ECO:0000303|PubMed:12028382};
GN Name=spx {ECO:0000303|PubMed:12028382};
GN Synonyms=spxA {ECO:0000312|EMBL:CAB13007.1}, yjbD;
GN OrderedLocusNames=BSU11500;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP INDUCTION.
RX PubMed=11544224; DOI=10.1128/jb.183.19.5617-5631.2001;
RA Petersohn A., Brigulla M., Haas S., Hoheisel J.D., Voelker U., Hecker M.;
RT "Global analysis of the general stress response of Bacillus subtilis.";
RL J. Bacteriol. 183:5617-5631(2001).
RN [3]
RP FUNCTION IN REGULATION OF COMPETENCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / JH642;
RX PubMed=11703662; DOI=10.1046/j.1365-2958.2001.02639.x;
RA Nakano M.M., Hajarizadeh F., Zhu Y., Zuber P.;
RT "Loss-of-function mutations in yjbD result in ClpX- and ClpP-independent
RT competence development of Bacillus subtilis.";
RL Mol. Microbiol. 42:383-394(2001).
RN [4]
RP FUNCTION IN REGULATION OF COMPETENCE.
RC STRAIN=168 / JH642;
RX PubMed=12028382; DOI=10.1046/j.1365-2958.2002.02963.x;
RA Nakano M.M., Nakano S., Zuber P.;
RT "Spx (YjbD), a negative effector of competence in Bacillus subtilis,
RT enhances ClpC-MecA-ComK interaction.";
RL Mol. Microbiol. 44:1341-1349(2002).
RN [5]
RP ACTIVITY REGULATION, AND DEGRADATION BY CLPXP AND CLPCP.
RC STRAIN=168 / JH642;
RX PubMed=12057962; DOI=10.1128/jb.184.13.3664-3670.2002;
RA Nakano S., Zheng G., Nakano M.M., Zuber P.;
RT "Multiple pathways of Spx (YjbD) proteolysis in Bacillus subtilis.";
RL J. Bacteriol. 184:3664-3670(2002).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH RNAP.
RC STRAIN=168 / JH642;
RX PubMed=12642660; DOI=10.1073/pnas.0637648100;
RA Nakano S., Nakano M.M., Zhang Y., Leelakriangsak M., Zuber P.;
RT "A regulatory protein that interferes with activator-stimulated
RT transcription in bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4233-4238(2003).
RN [7]
RP FUNCTION IN DISULFIDE STRESS, INDUCTION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF 130-ALA-ASN-131.
RC STRAIN=168 / JH642;
RX PubMed=14597697; DOI=10.1073/pnas.2235180100;
RA Nakano S., Kuester-Schoeck E., Grossman A.D., Zuber P.;
RT "Spx-dependent global transcriptional control is induced by thiol-specific
RT oxidative stress in Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13603-13608(2003).
RN [8]
RP FUNCTION IN DISULFIDE STRESS, ACTIVITY REGULATION, DISULFIDE BOND, AND
RP MUTAGENESIS OF CYS-10 AND CYS-13.
RX PubMed=15659166; DOI=10.1111/j.1365-2958.2004.04395.x;
RA Nakano S., Erwin K.N., Ralle M., Zuber P.;
RT "Redox-sensitive transcriptional control by a thiol/disulphide switch in
RT the global regulator, Spx.";
RL Mol. Microbiol. 55:498-510(2005).
RN [9]
RP FUNCTION IN ORGANOSULFUR METABOLISM.
RX PubMed=16885442; DOI=10.1128/jb.00443-06;
RA Choi S.Y., Reyes D., Leelakriangsak M., Zuber P.;
RT "The global regulator Spx functions in the control of organosulfur
RT metabolism in Bacillus subtilis.";
RL J. Bacteriol. 188:5741-5751(2006).
RN [10]
RP INDUCTION.
RC STRAIN=168 / JH642;
RX PubMed=17158660; DOI=10.1128/jb.01520-06;
RA Leelakriangsak M., Kobayashi K., Zuber P.;
RT "Dual negative control of spx transcription initiation from the P3 promoter
RT by repressors PerR and YodB in Bacillus subtilis.";
RL J. Bacteriol. 189:1736-1744(2007).
RN [11]
RP INDUCTION.
RC STRAIN=168 / 1604;
RX PubMed=17434969; DOI=10.1128/jb.00130-07;
RA Jervis A.J., Thackray P.D., Houston C.W., Horsburgh M.J., Moir A.;
RT "SigM-responsive genes of Bacillus subtilis and their promoters.";
RL J. Bacteriol. 189:4534-4538(2007).
RN [12]
RP ACTIVITY REGULATION.
RX PubMed=17908206; DOI=10.1111/j.1365-2958.2007.05949.x;
RA Larsson J.T., Rogstam A., von Wachenfeldt C.;
RT "YjbH is a novel negative effector of the disulphide stress regulator, Spx,
RT in Bacillus subtilis.";
RL Mol. Microbiol. 66:669-684(2007).
RN [13]
RP FUNCTION IN OXIDATIVE STRESS, ACTIVITY REGULATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168;
RX PubMed=18662407; DOI=10.1186/1471-2180-8-128;
RA You C., Sekowska A., Francetic O., Martin-Verstraete I., Wang Y.,
RA Danchin A.;
RT "Spx mediates oxidative stress regulation of the methionine sulfoxide
RT reductases operon in Bacillus subtilis.";
RL BMC Microbiol. 8:128-128(2008).
RN [14]
RP FUNCTION.
RX PubMed=18687074; DOI=10.1111/j.1365-2958.2008.06330.x;
RA Reyes D.Y., Zuber P.;
RT "Activation of transcription initiation by Spx: formation of transcription
RT complex and identification of a Cis-acting element required for
RT transcriptional activation.";
RL Mol. Microbiol. 69:765-779(2008).
RN [15]
RP ACTIVITY REGULATION, DEGRADATION BY CLPXP, AND INTERACTION WITH SPXH/YJBH.
RC STRAIN=168 / JH642;
RX PubMed=19074380; DOI=10.1128/jb.01289-08;
RA Garg S.K., Kommineni S., Henslee L., Zhang Y., Zuber P.;
RT "The YjbH protein of Bacillus subtilis enhances ClpXP-catalyzed proteolysis
RT of Spx.";
RL J. Bacteriol. 191:1268-1277(2009).
RN [16]
RP SUBUNIT, AND INTERACTION WITH RNAP.
RC STRAIN=168 / JH642;
RX PubMed=22307755; DOI=10.1128/jb.06660-11;
RA Lin A.A., Zuber P.;
RT "Evidence that a single monomer of Spx can productively interact with RNA
RT polymerase in Bacillus subtilis.";
RL J. Bacteriol. 194:1697-1707(2012).
RN [17]
RP FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=168 / CU1065;
RX PubMed=23894131; DOI=10.1099/mic.0.070482-0;
RA Gaballa A., Antelmann H., Hamilton C.J., Helmann J.D.;
RT "Regulation of Bacillus subtilis bacillithiol biosynthesis operons by
RT Spx.";
RL Microbiology 159:2025-2035(2013).
RN [18]
RP FUNCTION IN HEAT STRESS RESPONSE, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24417481; DOI=10.1111/mmi.12521;
RA Runde S., Moliere N., Heinz A., Maisonneuve E., Janczikowski A.,
RA Elsholz A.K., Gerth U., Hecker M., Turgay K.;
RT "The role of thiol oxidative stress response in heat-induced protein
RT aggregate formation during thermotolerance in Bacillus subtilis.";
RL Mol. Microbiol. 91:1036-1052(2014).
RN [19]
RP INTERACTION WITH SPXH/YJBH, DOMAIN, AND MUTAGENESIS OF GLY-52; ARG-60;
RP ARG-91; ARG-92; ILE-110; ARG-111; ARG-112; PHE-113; LEU-114 AND PRO-115.
RX PubMed=24942655; DOI=10.1111/mmi.12671;
RA Chan C.M., Hahn E., Zuber P.;
RT "Adaptor bypass mutations of Bacillus subtilis spx suggest a mechanism for
RT YjbH-enhanced proteolysis of the regulator Spx by ClpXP.";
RL Mol. Microbiol. 93:426-438(2014).
RN [20]
RP FUNCTION IN CELL WALL STRESS, ACTIVITY REGULATION, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=29271514; DOI=10.1111/mmi.13906;
RA Rojas-Tapias D.F., Helmann J.D.;
RT "Induction of the Spx regulon by cell wall stress reveals novel regulatory
RT mechanisms in Bacillus subtilis.";
RL Mol. Microbiol. 107:659-674(2018).
RN [21]
RP ACTIVITY REGULATION.
RX PubMed=30001325; DOI=10.1371/journal.pgen.1007531;
RA Rojas-Tapias D.F., Helmann J.D.;
RT "Stabilization of Bacillus subtilis Spx under cell wall stress requires the
RT anti-adaptor protein YirB.";
RL PLoS Genet. 14:e1007531-e1007531(2018).
RN [22]
RP FUNCTION.
RX PubMed=30718304; DOI=10.1128/jb.00712-18;
RA Kobayashi K.;
RT "Inactivation of cysL inhibits biofilm formation by activating the
RT disulfide stress regulator Spx in Bacillus subtilis.";
RL J. Bacteriol. 201:0-0(2019).
RN [23]
RP REVIEW.
RX PubMed=30830258; DOI=10.1007/s00294-019-00950-6;
RA Schaefer H., Turgay K.;
RT "Spx, a versatile regulator of the Bacillus subtilis stress response.";
RL Curr. Genet. 65:871-876(2019).
RN [24]
RP REVIEW.
RX PubMed=31655740; DOI=10.1016/bs.ampbs.2019.05.003;
RA Rojas-Tapias D.F., Helmann J.D.;
RT "Roles and regulation of Spx family transcription factors in Bacillus
RT subtilis and related species.";
RL Adv. Microb. Physiol. 75:279-323(2019).
RN [25] {ECO:0007744|PDB:1Z3E}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH THE C-TERMINAL
RP DOMAIN OF THE RNAP ALPHA SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=16249335; DOI=10.1073/pnas.0506592102;
RA Newberry K.J., Nakano S., Zuber P., Brennan R.G.;
RT "Crystal structure of the Bacillus subtilis anti-alpha, global
RT transcriptional regulator, Spx, in complex with the alpha C-terminal domain
RT of RNA polymerase.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:15839-15844(2005).
RN [26] {ECO:0007744|PDB:3GFK}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH THE C-TERMINAL
RP DOMAIN OF THE RNAP ALPHA SUBUNIT, AND DISULFIDE BONDS.
RC STRAIN=168;
RX PubMed=19580872; DOI=10.1016/j.jsb.2009.07.001;
RA Lamour V., Westblade L.F., Campbell E.A., Darst S.A.;
RT "Crystal structure of the in vivo-assembled Bacillus subtilis Spx/RNA
RT polymerase alpha subunit C-terminal domain complex.";
RL J. Struct. Biol. 168:352-356(2009).
RN [27] {ECO:0007744|PDB:3IHQ}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF REDUCED SER-10 MUTANT IN COMPLEX
RP WITH THE C-TERMINAL DOMAIN OF THE RNAP ALPHA SUBUNIT, FUNCTION, DOMAIN, AND
RP MUTAGENESIS OF ARG-60; LYS-62 AND LYS-66.
RX PubMed=20084284; DOI=10.1371/journal.pone.0008664;
RA Nakano M.M., Lin A., Zuber C.S., Newberry K.J., Brennan R.G., Zuber P.;
RT "Promoter recognition by a complex of Spx and the C-terminal domain of the
RT RNA polymerase alpha subunit.";
RL PLoS ONE 5:e8664-e8664(2010).
RN [28] {ECO:0007744|PDB:6GHB, ECO:0007744|PDB:6GHO}
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) IN COMPLEXES WITH G.KAUSTOPHILUS
RP SPXH/YJBH, ACTIVITY REGULATION, INTERACTION WITH SPXH/YJBH, AND DISULFIDE
RP BONDS.
RX PubMed=30982633; DOI=10.1016/j.str.2019.03.009;
RA Awad W., Al-Eryani Y., Ekstrom S., Logan D.T., von Wachenfeldt C.;
RT "Structural basis for YjbH adaptor-mediated recognition of transcription
RT factor Spx.";
RL Structure 27:923-936.e6(2019).
CC -!- FUNCTION: Global transcriptional regulator that plays a key role in
CC stress response and exerts either positive or negative regulation of
CC genes (PubMed:12642660, PubMed:15659166, PubMed:16885442,
CC PubMed:18662407, PubMed:18687074, PubMed:29271514). Acts by interacting
CC with the C-terminal domain of the alpha subunit of the RNA polymerase
CC (RNAP) (PubMed:12642660, PubMed:15659166, PubMed:18687074,
CC PubMed:20084284). This interaction can enhance binding of RNAP to the
CC promoter region of target genes and stimulate their transcription, or
CC block interaction of RNAP with activator proteins and repress
CC transcription (PubMed:12642660, PubMed:15659166, PubMed:18687074,
CC PubMed:20084284). Exhibits no DNA-binding activity (PubMed:15659166,
CC PubMed:18687074). {ECO:0000269|PubMed:12642660,
CC ECO:0000269|PubMed:15659166, ECO:0000269|PubMed:16885442,
CC ECO:0000269|PubMed:18662407, ECO:0000269|PubMed:18687074,
CC ECO:0000269|PubMed:20084284, ECO:0000269|PubMed:29271514}.
CC -!- FUNCTION: Induces the expression of a large number of genes in response
CC to a variety of stress conditions, such as disulfide, heat and cell
CC wall stress, while concurrently repressing transcription of genes
CC involved in various developmental and growth-related pathways during
CC periods of extreme stress (PubMed:12642660, PubMed:14597697). Functions
CC in the oxidative stress response via induction of the transcription of
CC thioredoxin (trxA) and thioredoxin reductase (trxB) during thiol-
CC specific oxidative (disulfide) stress (PubMed:14597697,
CC PubMed:15659166, PubMed:18687074). Mediates response to oxidative
CC stress caused by paraquat (PQ) via induction of the methionine
CC sulfoxide reductase genes, msrA and msrB (PubMed:18662407). Also acts
CC as a transcriptional activator of the bacillithiol (BSH) biosynthesis
CC genes in response to oxidizing conditions and thio-reactive compounds
CC (PubMed:23894131). Involved in heat stress response and thermotolerance
CC development, which results in diminished cellular protein aggregates
CC (PubMed:24417481). Plays an important adaptive role in the cell wall
CC stress response (PubMed:29271514). Participates in sulfate-dependent
CC control of organosulfur metabolism. Negatively controls, via CymR, the
CC expression of the organosulfur utilization operons ytmI, yxeI and ssu,
CC and directly activates yrrT operon expression during growth in medium
CC containing methionine as sole sulfur source (PubMed:16885442).
CC Negatively affects competence and sporulation (PubMed:11703662,
CC PubMed:12028382). Inhibits biofilm formation in response to disulfide
CC stress by repressing biofilm matrix genes (PubMed:30718304).
CC {ECO:0000269|PubMed:11703662, ECO:0000269|PubMed:12028382,
CC ECO:0000269|PubMed:12642660, ECO:0000269|PubMed:14597697,
CC ECO:0000269|PubMed:15659166, ECO:0000269|PubMed:16885442,
CC ECO:0000269|PubMed:18662407, ECO:0000269|PubMed:18687074,
CC ECO:0000269|PubMed:23894131, ECO:0000269|PubMed:24417481,
CC ECO:0000269|PubMed:29271514, ECO:0000269|PubMed:30718304}.
CC -!- ACTIVITY REGULATION: Under non-stress conditions, Spx is degraded by
CC ClpXP and, to a lesser extent, by ClpCP (PubMed:12057962,
CC PubMed:12642660, PubMed:19074380). Efficient dedradation by ClpXP
CC requires the adapter protein SpxH/YjbH (PubMed:17908206,
CC PubMed:19074380). Binding to SpxH/YjbH reduces the overall
CC conformational flexibility of Spx and stabilizes the C-terminal ClpX
CC recognition region of Spx (PubMed:30982633). In addition, activity is
CC modulated by the formation of a disulfide bound within the N-terminal
CC Cys-X-X-Cys (CXXC) motif, which is required for the transcriptional
CC activation of trxA and trxB, or for the activation of msrAB operon
CC expression following paraquat oxidative stress (PubMed:15659166,
CC PubMed:18662407). However, it seems that formation of the disulfide
CC bound is not essential for induction of all Spx-controlled genes, as
CC for example the case of BSH biosynthesis genes (PubMed:23894131).
CC Similarly, induction of the Spx regulon during cell wall stress is not
CC accompanied by oxidation of the disulfide switch, but requires Spx
CC stabilization by the anti-adapter protein SpxO/YirB (PubMed:29271514,
CC PubMed:30001325). {ECO:0000269|PubMed:12057962,
CC ECO:0000269|PubMed:12642660, ECO:0000269|PubMed:15659166,
CC ECO:0000269|PubMed:17908206, ECO:0000269|PubMed:18662407,
CC ECO:0000269|PubMed:19074380, ECO:0000269|PubMed:23894131,
CC ECO:0000269|PubMed:29271514, ECO:0000269|PubMed:30001325,
CC ECO:0000269|PubMed:30982633}.
CC -!- SUBUNIT: Interacts with the C-terminal domain of the alpha subunit of
CC the RNAP (PubMed:12642660, PubMed:16249335, PubMed:19580872,
CC PubMed:20084284, PubMed:22307755). A single Spx monomer interacts with
CC RNAP to form the transcription activation complex (PubMed:22307755).
CC Interacts with the adapter protein SpxH/YjbH (PubMed:19074380,
CC PubMed:24942655, PubMed:30982633). {ECO:0000269|PubMed:12642660,
CC ECO:0000269|PubMed:16249335, ECO:0000269|PubMed:19074380,
CC ECO:0000269|PubMed:19580872, ECO:0000269|PubMed:20084284,
CC ECO:0000269|PubMed:22307755, ECO:0000269|PubMed:24942655,
CC ECO:0000269|PubMed:30982633}.
CC -!- INTERACTION:
CC O31602; P37871: rpoC; NbExp=2; IntAct=EBI-5248631, EBI-5244361;
CC O31602; O31606: spxH; NbExp=3; IntAct=EBI-5248631, EBI-6406036;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Transcribed from at least five promoters located in the yjbC
CC regulatory region or in the yjbC-spx intergenic region
CC (PubMed:17158660, PubMed:29271514). Induced by heat, salt, ethanol and
CC disulfide stress and also by phosphate limitation (PubMed:11544224,
CC PubMed:14597697, PubMed:24417481). Induced by cell wall stress but not
CC by membrane stress (PubMed:29271514). Transcribed under partial control
CC of SigM ECF sigma factor (PubMed:17434969, PubMed:29271514). Repressed
CC by YodB and PerR. YodB protects a region that includes the P3 -10 and
CC -35 regions, while PerR binds to a region downstream of the P3
CC transcriptional start site (PubMed:17158660).
CC {ECO:0000269|PubMed:11544224, ECO:0000269|PubMed:14597697,
CC ECO:0000269|PubMed:17158660, ECO:0000269|PubMed:17434969,
CC ECO:0000269|PubMed:24417481, ECO:0000269|PubMed:29271514}.
CC -!- DOMAIN: The C-terminal region is essential for structural folding and
CC for interaction with SpxH/YjbH (PubMed:24942655). A conformational
CC change during oxidation of Spx to the disulfide form likely alters the
CC structure of Spx alpha helix alpha4, which contains residues that
CC function in transcriptional activation and Spx/RNAP-promoter
CC interaction (PubMed:20084284). {ECO:0000269|PubMed:20084284,
CC ECO:0000269|PubMed:24942655}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene results in ClpP-
CC independent competence development as well as partial suppression of
CC the sporulation defect conferred by clpP mutation (PubMed:11703662).
CC Null mutant shows hypersensitivity to disulfide stress and to paraquat
CC (PubMed:14597697, PubMed:18662407). Mutants have increased sensitivity
CC toward cell wall active antibiotics inhibiting both early and late
CC steps in peptidoglycan synthesis (PubMed:29271514). Cells lacking the
CC gene are defective in thermotolerance (PubMed:24417481).
CC {ECO:0000269|PubMed:11703662, ECO:0000269|PubMed:14597697,
CC ECO:0000269|PubMed:18662407, ECO:0000269|PubMed:24417481,
CC ECO:0000269|PubMed:29271514}.
CC -!- SIMILARITY: Belongs to the ArsC family. Spx subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01132, ECO:0000305}.
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DR EMBL; AL009126; CAB13007.1; -; Genomic_DNA.
DR PIR; D69843; D69843.
DR RefSeq; NP_389032.1; NC_000964.3.
DR RefSeq; WP_003245483.1; NZ_JNCM01000035.1.
DR PDB; 1Z3E; X-ray; 1.50 A; A=1-131.
DR PDB; 3GFK; X-ray; 2.30 A; A=1-131.
DR PDB; 3IHQ; X-ray; 1.90 A; A=1-131.
DR PDB; 6GHB; X-ray; 3.10 A; A/C=1-131.
DR PDB; 6GHO; X-ray; 1.79 A; A=1-131.
DR PDBsum; 1Z3E; -.
DR PDBsum; 3GFK; -.
DR PDBsum; 3IHQ; -.
DR PDBsum; 6GHB; -.
DR PDBsum; 6GHO; -.
DR AlphaFoldDB; O31602; -.
DR SMR; O31602; -.
DR IntAct; O31602; 3.
DR STRING; 224308.BSU11500; -.
DR PaxDb; O31602; -.
DR PRIDE; O31602; -.
DR EnsemblBacteria; CAB13007; CAB13007; BSU_11500.
DR GeneID; 936407; -.
DR KEGG; bsu:BSU11500; -.
DR PATRIC; fig|224308.179.peg.1237; -.
DR eggNOG; COG1393; Bacteria.
DR InParanoid; O31602; -.
DR OMA; IMIDDKR; -.
DR PhylomeDB; O31602; -.
DR BioCyc; BSUB:BSU11500-MON; -.
DR EvolutionaryTrace; O31602; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR HAMAP; MF_01132; Spx; 1.
DR InterPro; IPR006660; Arsenate_reductase-like.
DR InterPro; IPR023731; Spx.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR006504; Tscrpt_reg_Spx/MgsR.
DR PANTHER; PTHR30041; PTHR30041; 1.
DR Pfam; PF03960; ArsC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01617; arsC_related; 1.
DR PROSITE; PS51353; ARSC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disulfide bond; Redox-active center;
KW Reference proteome; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..131
FT /note="Global transcriptional regulator Spx"
FT /id="PRO_0000162551"
FT MOTIF 10..13
FT /note="CXXC"
FT /evidence="ECO:0000305"
FT DISULFID 10..13
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01282,
FT ECO:0000269|PubMed:15659166, ECO:0000269|PubMed:16249335,
FT ECO:0000269|PubMed:19580872, ECO:0000269|PubMed:30982633,
FT ECO:0007744|PDB:1Z3E, ECO:0007744|PDB:3GFK,
FT ECO:0007744|PDB:6GHB, ECO:0007744|PDB:6GHO"
FT MUTAGEN 10
FT /note="C->A: Cannot induce expression of trxA and trxB.
FT Does not affect stability."
FT /evidence="ECO:0000269|PubMed:15659166"
FT MUTAGEN 13
FT /note="C->A: Cannot induce expression of trxA and trxB.
FT Does not affect stability."
FT /evidence="ECO:0000269|PubMed:15659166"
FT MUTAGEN 52
FT /note="G->R: Does not affect binding to SpxH/YjbH."
FT /evidence="ECO:0000269|PubMed:24942655"
FT MUTAGEN 60
FT /note="R->E: Confers defects in Spx-activated transcription
FT but not in Spx-dependent repression. Does not affect
FT binding to SpxH/YjbH."
FT /evidence="ECO:0000269|PubMed:20084284,
FT ECO:0000269|PubMed:24942655"
FT MUTAGEN 62
FT /note="K->E: Confers defects in Spx-activated transcription
FT but not in Spx-dependent repression."
FT /evidence="ECO:0000269|PubMed:20084284"
FT MUTAGEN 66
FT /note="K->E: Does not affect trxB expression."
FT /evidence="ECO:0000269|PubMed:20084284"
FT MUTAGEN 91
FT /note="R->A: Does not affect binding to SpxH/YjbH."
FT /evidence="ECO:0000269|PubMed:24942655"
FT MUTAGEN 92
FT /note="R->A: Does not affect binding to SpxH/YjbH."
FT /evidence="ECO:0000269|PubMed:24942655"
FT MUTAGEN 110
FT /note="I->A: Decreases activity. 90% decrease in binding to
FT SpxH/YjbH."
FT /evidence="ECO:0000269|PubMed:24942655"
FT MUTAGEN 111
FT /note="R->A: Decreases activity."
FT /evidence="ECO:0000269|PubMed:24942655"
FT MUTAGEN 112
FT /note="R->A: 80% decrease in binding to SpxH/YjbH."
FT /evidence="ECO:0000269|PubMed:24942655"
FT MUTAGEN 113
FT /note="F->A: Decreases activity. 80% decrease in binding to
FT SpxH/YjbH. Enhanced proteolysis by ClpXP in the absence of
FT SpxH/YjbH."
FT /evidence="ECO:0000269|PubMed:24942655"
FT MUTAGEN 114
FT /note="L->A: Decreases activity. 50% decrease in binding to
FT SpxH/YjbH. Enhanced proteolysis by ClpXP in the absence of
FT SpxH/YjbH."
FT /evidence="ECO:0000269|PubMed:24942655"
FT MUTAGEN 115
FT /note="P->A: Decreases activity. 90% decrease in binding to
FT SpxH/YjbH."
FT /evidence="ECO:0000269|PubMed:24942655"
FT MUTAGEN 130..131
FT /note="AN->DD: Retains activity. Resistant to degradation
FT by ClpXP."
FT /evidence="ECO:0000269|PubMed:14597697"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1Z3E"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:1Z3E"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:1Z3E"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:1Z3E"
FT HELIX 39..47
FT /evidence="ECO:0007829|PDB:1Z3E"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:1Z3E"
FT HELIX 62..67
FT /evidence="ECO:0007829|PDB:1Z3E"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:1Z3E"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:1Z3E"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:1Z3E"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1Z3E"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:1Z3E"
FT HELIX 109..113
FT /evidence="ECO:0007829|PDB:1Z3E"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:6GHO"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:6GHB"
SQ SEQUENCE 131 AA; 15529 MW; E296B3B7A90397D7 CRC64;
MVTLYTSPSC TSCRKARAWL EEHEIPFVER NIFSEPLSID EIKQILRMTE DGTDEIISTR
SKVFQKLNVN VESMPLQDLY RLINEHPGLL RRPIIIDEKR LQVGYNEDEI RRFLPRKVRS
FQLREAQRLA N
