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Protein

Regulatory protein Spx

Gene

spxA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Interferes with activator-stimulated transcription by interaction with the RNA polymerase alpha-CTD. May function to globally reduce transcription of genes involved in growth- and development-promoting processes and to increase transcription of genes involved in thiol homeostasis, during periods of extreme stress. Negatively affects competence and sporulation. Its degradation by the MecA/ClpXP complex is needed for competence development.UniRule annotation2 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Stress response, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciBSUB:BSU11500-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulatory protein SpxUniRule annotation
Gene namesi
Name:spxAUniRule annotation
Synonyms:yjbD
Ordered Locus Names:BSU11500
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi130 – 1312AN → DD: Resistant to degradation by ClpXP. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 131131Regulatory protein SpxPRO_0000162551Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi10 ↔ 13Redox-activeUniRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiO31602.

Expressioni

Inductioni

By heat, salt, ethanol and disulfide stress and also by phosphate limitation. Transcribed under partial control of SigM ECF sigma factor (PubMed:17434969).1 Publication

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
rpoCP378712EBI-5248631,EBI-5244361
yjbHO316063EBI-5248631,EBI-6406036

Protein-protein interaction databases

IntActiO31602. 3 interactions.
STRINGi224308.Bsubs1_010100006356.

Structurei

Secondary structure

1
131
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi11 – 2212Combined sources
Beta strandi27 – 315Combined sources
Turni32 – 343Combined sources
Helixi39 – 479Combined sources
Helixi53 – 553Combined sources
Helixi62 – 676Combined sources
Helixi71 – 733Combined sources
Helixi76 – 8510Combined sources
Helixi87 – 893Combined sources
Beta strandi94 – 963Combined sources
Beta strandi101 – 1044Combined sources
Helixi109 – 1135Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z3EX-ray1.50A1-131[»]
3GFKX-ray2.30A1-131[»]
3IHQX-ray1.90A1-131[»]
ProteinModelPortaliO31602.
SMRiO31602. Positions 1-118.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO31602.

Family & Domainsi

Sequence similaritiesi

Belongs to the ArsC family. Spx subfamily.UniRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG41090SU. Bacteria.
COG1393. LUCA.
HOGENOMiHOG000059715.
InParanoidiO31602.
KOiK16509.
OMAiLKRPIIM.
OrthoDBiEOG6WQDCS.
PhylomeDBiO31602.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
HAMAPiMF_01132. SpxA.
InterProiIPR006660. Arsenate_reductase-like.
IPR023731. Spx.
IPR012336. Thioredoxin-like_fold.
IPR006504. Tscrpt_reg_Spx/MgsR.
[Graphical view]
PfamiPF03960. ArsC. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR01617. arsC_related. 1 hit.
PROSITEiPS51353. ARSC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O31602-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTLYTSPSC TSCRKARAWL EEHEIPFVER NIFSEPLSID EIKQILRMTE
60 70 80 90 100
DGTDEIISTR SKVFQKLNVN VESMPLQDLY RLINEHPGLL RRPIIIDEKR
110 120 130
LQVGYNEDEI RRFLPRKVRS FQLREAQRLA N
Length:131
Mass (Da):15,529
Last modified:January 1, 1998 - v1
Checksum:iE296B3B7A90397D7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13007.1.
PIRiD69843.
RefSeqiNP_389032.1. NC_000964.3.
WP_003245483.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13007; CAB13007; BSU11500.
GeneIDi936407.
KEGGibsu:BSU11500.
PATRICi18974015. VBIBacSub10457_1201.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13007.1.
PIRiD69843.
RefSeqiNP_389032.1. NC_000964.3.
WP_003245483.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z3EX-ray1.50A1-131[»]
3GFKX-ray2.30A1-131[»]
3IHQX-ray1.90A1-131[»]
ProteinModelPortaliO31602.
SMRiO31602. Positions 1-118.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO31602. 3 interactions.
STRINGi224308.Bsubs1_010100006356.

Proteomic databases

PaxDbiO31602.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13007; CAB13007; BSU11500.
GeneIDi936407.
KEGGibsu:BSU11500.
PATRICi18974015. VBIBacSub10457_1201.

Phylogenomic databases

eggNOGiENOG41090SU. Bacteria.
COG1393. LUCA.
HOGENOMiHOG000059715.
InParanoidiO31602.
KOiK16509.
OMAiLKRPIIM.
OrthoDBiEOG6WQDCS.
PhylomeDBiO31602.

Enzyme and pathway databases

BioCyciBSUB:BSU11500-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO31602.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
HAMAPiMF_01132. SpxA.
InterProiIPR006660. Arsenate_reductase-like.
IPR023731. Spx.
IPR012336. Thioredoxin-like_fold.
IPR006504. Tscrpt_reg_Spx/MgsR.
[Graphical view]
PfamiPF03960. ArsC. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR01617. arsC_related. 1 hit.
PROSITEiPS51353. ARSC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  2. "Loss-of-function mutations in yjbD result in ClpX- and ClpP-independent competence development of Bacillus subtilis."
    Nakano M.M., Hajarizadeh F., Zhu Y., Zuber P.
    Mol. Microbiol. 42:383-394(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: 168 / JH642.
  3. "A regulatory protein that interferes with activator-stimulated transcription in bacteria."
    Nakano S., Nakano M.M., Zhang Y., Leelakriangsak M., Zuber P.
    Proc. Natl. Acad. Sci. U.S.A. 100:4233-4238(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: 168 / JH642.
  4. "Spx (YjbD), a negative effector of competence in Bacillus subtilis, enhances ClpC-MecA-ComK interaction."
    Nakano M.M., Nakano S., Zuber P.
    Mol. Microbiol. 44:1341-1349(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: 168 / JH642.
  5. "Spx-dependent global transcriptional control is induced by thiol-specific oxidative stress in Bacillus subtilis."
    Nakano S., Kuester-Schoeck E., Grossman A.D., Zuber P.
    Proc. Natl. Acad. Sci. U.S.A. 100:13603-13608(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MUTAGENESIS OF 130-ALA-ASN-131.
    Strain: 168 / JH642.
  6. "Multiple pathways of Spx (YjbD) proteolysis in Bacillus subtilis."
    Nakano S., Zheng G., Nakano M.M., Zuber P.
    J. Bacteriol. 184:3664-3670(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEGRADATION BY CLPXP.
    Strain: 168 / JH642.
  7. "SigM-responsive genes of Bacillus subtilis and their promoters."
    Jervis A.J., Thackray P.D., Houston C.W., Horsburgh M.J., Moir A.
    J. Bacteriol. 189:4534-4538(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: 168 / 1604.

Entry informationi

Entry nameiSPX_BACSU
AccessioniPrimary (citable) accession number: O31602
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 1, 1998
Last modified: April 13, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.