O31602 (SPX_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Regulatory protein spx

Gene names

Name:	spxA
Ordered Locus Names:	BSU11500

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	131 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.2 Ref.3
Subcellular location	Cytoplasm Probable HAMAP MF_01132.
Induction	By heat, salt, ethanol and disulfide stress and also by phosphate limitation. HAMAP MF_01132
Sequence similarities	Belongs to the ArsC family. Spx subfamily.

Ontologies

Keywords
Biological process	Stress response Transcription Transcription regulation
Cellular component	Cytoplasm
Domain	Redox-active center
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro response to stress Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 131

131

Regulatory protein spx HAMAP MF_01132

PRO_0000162551

Amino acid modifications

Disulfide bond

10 ↔ 13

Redox-active Potential

Experimental info

Mutagenesis

130 – 131

2

AN → DD: Resistant to degradation by ClpXP. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

131

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Helix

11 – 22

12

Beta strand

27 – 31

5

Turn

32 – 34

3

Helix

39 – 47

9

Helix

53 – 55

3

Helix

62 – 67

6

Helix

71 – 73

3

Helix

76 – 85

10

Helix

87 – 89

3

Beta strand

94 – 96

3

Beta strand

101 – 104

4

Helix

109 – 113

5

Sequences

	Sequence		Length	Mass (Da)
	O31602 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: E296B3B7A90397D7	FASTA	131	15,529
	10 20 30 40 50 60 MVTLYTSPSC TSCRKARAWL EEHEIPFVER NIFSEPLSID EIKQILRMTE DGTDEIISTR 70 80 90 100 110 120 SKVFQKLNVN VESMPLQDLY RLINEHPGLL RRPIIIDEKR LQVGYNEDEI RRFLPRKVRS 130 FQLREAQRLA N

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9384377] [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: 11703662] [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: 12642660] [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: 12028382] [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: 14597697] [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: 12057962] [Abstract] Cited for: DEGRADATION BY CLPXP. Strain: 168 / JH642.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AL009126 Genomic DNA. Translation: CAB13007.1.

PIR

D69843.

RefSeq

NP_389032.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Z3E	X-ray	1.50	A	1-131	[»]
3GFK	X-ray	2.30	A	1-131	[»]
3IHQ	X-ray	1.90	A	1-131	[»]

ProteinModelPortal

O31602.

SMR

O31602. Positions 1-118.

ModBase

Search...

Protein-protein interaction databases

IntAct

O31602. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000003128; EBBACP00000003128; EBBACG00000003121.

GeneID

936407.

GenomeReviews

Gene locus BSU11500 in contig AL009126_GR.

KEGG

bsu:BSU11500.

NMPDR

fig|224308.1.peg.1151.

PATRIC

18974015. VBIBacSub10457_1201.

Organism-specific databases

GenoList

BSU11500. [Micado]

Phylogenomic databases

GeneTree

EBGT00050000001358.

HOGENOM

HBG734370.

OMA

FTERNIF.

PhylomeDB

O31602.

ProtClustDB

PRK01655.

Enzyme and pathway databases

BioCyc

BSUB:BSU11500-MONOMER.

Family and domain databases

HAMAP

MF_01132. SpxA.
[Tree]

InterPro

IPR006660. Arsenate_reductase-like.
IPR012336. Thioredoxin-like_fold.
IPR023731. Tscrpt_reg_Spx.
IPR006504. Tscrpt_reg_Spx/MgsR.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

Pfam

PF03960. ArsC. 1 hit.
[Graphical view]

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

TIGRFAMs

TIGR01617. ArsC_related. 1 hit.

PROSITE

PS51353. ARSC. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SPX_BACSU

Accession

Primary (citable) accession number: O31602

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	January 1, 1998
Last modified:	January 25, 2012
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program