Skip Header

Contribute Send feedback
Read comments (?) or add your own

O32193 (CSSS_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sensor histidine kinase CssS

EC=2.7.13.3
Gene names
Name:cssS
Synonyms:yvqB
Ordered Locus Names:BSU33020
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length451 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Member of the two-component regulatory system CssS/CssR required to control the cellular response to secretion stress. Required for the transcription of htrA. Could detect misfolded proteins at the membrane-cell wall interface and then activate CssR by phosphorylation. Ref.5

Catalytic activity

ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.

Subcellular location

Cell membrane; Multi-pass membrane protein Potential.

Sequence similarities

Contains 1 HAMP domain.

Contains 1 histidine kinase domain.

Sequence caution

The sequence CAB07976.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTwo-component regulatory system
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processpeptidyl-histidine phosphorylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

two-component sensor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 451451Sensor histidine kinase CssS
PRO_0000074743

Regions

Topological domain1 – 99Cytoplasmic Potential
Transmembrane10 – 3021Helical; Potential
Topological domain31 – 165135Extracellular Potential
Transmembrane166 – 18621Helical; Potential
Topological domain187 – 451265Cytoplasmic Potential
Domain187 – 23953HAMP
Domain247 – 451205Histidine kinase

Amino acid modifications

Modified residue2501Phosphohistidine; by autocatalysis By similarity

Experimental info

Sequence conflict4441T → S in CAA11751. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O32193 [UniParc].

Last modified July 28, 2009. Version 2.
Checksum: DCC269B9038176F0

FASTA45152,097
        10         20         30         40         50         60 
MKNKPLAFQI WVVISGILLA ISILLLVLFS NTLRDFFTNE TYTTIENEQH VLTEYRLPGS 

        70         80         90        100        110        120 
IERRYYSEEA TAPTTVRSVQ HVLLPENEEA SSDKDLSILS SSFIHKVYKL ADKQEAKKKR 

       130        140        150        160        170        180 
YSADVNGEKV FFVIKKGLSV NGQSAMMLSY ALDSYRDDLA YTLFKQLLFI IAVVILLSWI 

       190        200        210        220        230        240 
PAIWLAKYLS RPLVSFEKHV KRISEQDWDD PVKVDRKDEI GKLGHTIEEM RQKLVQKDET 

       250        260        270        280        290        300 
ERTLLQNISH DLKTPVMVIR GYTQSIKDGI FPKGDLENTV DVIECEALKL EKKIKDLLYL 

       310        320        330        340        350        360 
TKLDYLAKQK VQHDMFSIVE VTEEVIERLK WARKELSWEI DVEEDILMPG DPEQWNKLLE 

       370        380        390        400        410        420 
NILENQIRYA ETKIEISMKQ DDRNIVITIK NDGPHIEDEM LSSLYEPFNK GKKGEFGIGL 

       430        440        450 
SIVKRILTLH KASISIENDK TGVTYRIAVP K 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of regions downstream of addA (98 degrees) and citG (289 degrees) in Bacillus subtilis."
Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J.
Microbiology 143:3305-3308(1997) [PubMed: 9353931] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The yvsA-yvqA (293 degrees - 289 degrees) region of the Bacillus subtilis chromosome containing genes involved in metal ion uptake and a putative sigma factor."
Wipat A., Brignell C.S., Guy J.B., Rose M., Emmerson P.T., Harwood C.R.
Microbiology 144:1593-1600(1998) [PubMed: 9639930] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"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. expand/collapse author list , 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.
[4]"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract]
Cited for: SEQUENCE REVISION TO 444.
[5]"Comprehensive DNA microarray analysis of Bacillus subtilis two-component regulatory systems."
Kobayashi K., Ogura M., Yamaguchi H., Yoshida K., Ogasawara N., Tanaka T., Fujita Y.
J. Bacteriol. 183:7365-7370(2001) [PubMed: 11717295] [Abstract]
Cited for: FUNCTION.
[6]"A novel two-component regulatory system in Bacillus subtilis for the survival of severe secretion stress."
Hyyrylaeinen H.-L., Bolhuis A., Darmon E., Muukkonen L., Koski P., Vitikainen M., Sarvas M., Pragai Z., Bron S., van Dijl J.M., Kontinen V.P.
Mol. Microbiol. 41:1159-1172(2001) [PubMed: 11555295] [Abstract]
Cited for: CHARACTERIZATION.
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z93941 Genomic DNA. Translation: CAB07976.1. Different initiation.
AJ223978 Genomic DNA. Translation: CAA11751.1.
AL009126 Genomic DNA. Translation: CAB15292.2.
PIRD70045.
RefSeqNP_391182.2. NC_000964.3.

3D structure databases

ProteinModelPortalO32193.
SMRO32193. Positions 203-451.
ModBaseSearch...

Protein-protein interaction databases

IntActO32193. 16 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000001884; EBBACP00000001884; EBBACG00000001881.
GeneID935936.
GenomeReviewsGene locus BSU33020 in contig AL009126_GR.
KEGGbsu:BSU33020.
NMPDRfig|224308.1.peg.3308.
PATRIC18978588. VBIBacSub10457_3457.

Organism-specific databases

GenoListBSU33020. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000000010.
HOGENOMHBG338303.
PhylomeDBO32193.
ProtClustDBCLSK872951.

Enzyme and pathway databases

BioCycBSUB:BSU33020-MONOMER.
BRENDA2.7.13.3. 700.

Family and domain databases

InterProIPR003594. ATPase-like_ATP-bd.
IPR003660. HAMP_linker_domain.
IPR004358. Sig_transdc_His_kin-like_C.
IPR003661. Sig_transdc_His_kin_sub1_dim/P.
IPR005467. Sig_transdc_His_kinase_core.
IPR009082. Sig_transdc_His_kinase_dimeric.
[Graphical view]
Gene3DG3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.
KOK07650.
PfamPF00672. HAMP. 1 hit.
PF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
[Graphical view]
PRINTSPR00344. BCTRLSENSOR.
SMARTSM00304. HAMP. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
[Graphical view]
SUPFAMSSF55874. ATP_bd_ATPase. 1 hit.
SSF47384. His_kin_homodim. 1 hit.
PROSITEPS50885. HAMP. 1 hit.
PS50109. HIS_KIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCSSS_BACSU
AccessionPrimary (citable) accession number: O32193
Secondary accession number(s): O32303
Entry history
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: July 28, 2009
Last modified: January 25, 2012
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families