Skip Header

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

P08401 (CREC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 122. 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 protein CreC

EC=2.7.13.3
Gene names
Name:creC
Synonyms:phoM
Ordered Locus Names:b4399, JW4362
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Member of the two-component regulatory system CreC/CreB involved in catabolic regulation. CreC may function as a membrane-associated protein kinase that phosphorylates CreB in response to environmental signals. CreC can also phosphorylate PhoB. Ref.6 Ref.7

Catalytic activity

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

Subcellular location

Cell inner membrane; Multi-pass membrane protein.

Post-translational modification

Autophosphorylated. Ref.7

Sequence similarities

Contains 1 HAMP domain.

Contains 1 histidine kinase domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 474474Sensor protein CreC
PRO_0000074742

Regions

Topological domain1 – 66Periplasmic Potential
Transmembrane7 – 2721Helical; Potential
Topological domain28 – 146119Cytoplasmic Potential
Transmembrane147 – 16721Helical; Potential
Topological domain168 – 18316Periplasmic Potential
Transmembrane184 – 20421Helical; Potential
Topological domain205 – 474270Cytoplasmic Potential
Domain205 – 25551HAMP
Domain262 – 473212Histidine kinase

Amino acid modifications

Modified residue2651Phosphohistidine; by autocatalysis By similarity

Experimental info

Sequence conflict771R → P in AAA24375. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P08401 [UniParc].

Last modified July 19, 2003. Version 2.
Checksum: 9CEB8CCE406E3163

FASTA47452,176
        10         20         30         40         50         60 
MRIGMRLLLG YFLLVAVAAW FVLAIFVKEV KPGVRRATEG TLIDTATLLA ELARPDLLSG 

        70         80         90        100        110        120 
DPTHGQLAQA FNQLQHRPFR ANIGGINKVR NEYHVYMTDA QGKVLFDSAN KAVGQDYSRW 

       130        140        150        160        170        180 
NDVWLTLRGQ YGARSTLQNP ADPESSVMYV AAPIMDGSRL IGVLSVGKPN AAMAPVIKRS 

       190        200        210        220        230        240 
ERRILWASAI LLGIALVIGA GMVWWINRSI ARLTRYADSV TDNKPVPLPD LGSSELRKLA 

       250        260        270        280        290        300 
QALESMRVKL EGKNYIEQYV YALTHELKSP LAAIRGAAEI LREGPPPEVV ARFTDNILTQ 

       310        320        330        340        350        360 
NARMQALVET LLRQARLENR QEVVLTAVDV AALFRRVSEA RTVQLAEKKI TLHVTPTEVN 

       370        380        390        400        410        420 
VAAEPALLEQ ALGNLLDNAI DFTPESGCIT LSAEVDQEHV TLKVLDTGSG IPDYALSRIF 

       430        440        450        460        470 
ERFYSLPRAN GQKSSGLGLA FVSEVARLFN GEVTLRNVQE GGVLASLRLH RHFT 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the phoM region of Escherichia coli: four open reading frames may constitute an operon."
Amemura M., Makino K., Shinagawa H., Nakata A.
J. Bacteriol. 168:294-302(1986) [PubMed: 3531171] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 23:2105-2119(1995) [PubMed: 7610040] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Identification and sequencing of the Escherichia coli cet gene which codes for an inner membrane protein, mutation of which causes tolerance to colicin E2."
Drury L.S., Buxton R.S.
Mol. Microbiol. 2:109-119(1988) [PubMed: 2835585] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 381-474.
Strain: K12.
[6]"Cross talk to the phosphate regulon of Escherichia coli by PhoM protein: PhoM is a histidine protein kinase and catalyzes phosphorylation of PhoB and PhoM-open reading frame 2."
Amemura M., Makino K., Shinagawa H., Nakata A.
J. Bacteriol. 172:6300-6307(1990) [PubMed: 2228961] [Abstract]
Cited for: FUNCTION.
[7]"Functional characterization in vitro of all two-component signal transduction systems from Escherichia coli."
Yamamoto K., Hirao K., Oshima T., Aiba H., Utsumi R., Ishihama A.
J. Biol. Chem. 280:1448-1456(2005) [PubMed: 15522865] [Abstract]
Cited for: FUNCTION, AUTOPHOSPHORYLATION.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]"Global topology analysis of the Escherichia coli inner membrane proteome."
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
Science 308:1321-1323(2005) [PubMed: 15919996] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: K12 / MG1655 / ATCC 47076.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13608 Genomic DNA. Translation: AAA24375.1.
U14003 Genomic DNA. Translation: AAA97295.1.
U00096 Genomic DNA. Translation: AAC77352.1.
AP009048 Genomic DNA. Translation: BAE78388.1.
Y00538 Genomic DNA. Translation: CAA68601.1.
PIRRGECFM. S56623.
RefSeqNP_418816.1. NC_000913.2.

3D structure databases

ProteinModelPortalP08401.
SMRP08401. Positions 204-472.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-9319N.
IntActP08401. 4 interactions.
MINTMINT-1307740.

Proteomic databases

PRIDEP08401.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000003217; EBESCP00000003217; EBESCG00000002642.
EBESCT00000014937; EBESCP00000014228; EBESCG00000013997.
GeneID948609.
GenomeReviewsGene locus JW4362 in contig AP009048_GR.
Gene locus b4399 in contig U00096_GR.
KEGGecj:JW4362.
eco:b4399.
PATRIC32124416. VBIEscCol129921_4548.

Organism-specific databases

EchoBASEEB0723.
EcoGeneEG10730. creC.

Phylogenomic databases

eggNOGCOG0642.
GeneTreeEBGT00050000008662.
HOGENOMHBG530303.
OMAMPTEINV.
PhylomeDBP08401.
ProtClustDBPRK11100.

Enzyme and pathway databases

BioCycEcoCyc:CREC-MONOMER.
BRENDA2.7.13.3. 2026.

Gene expression databases

GenevestigatorP08401.

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.
KOK07641.
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 nameCREC_ECOLI
AccessionPrimary (citable) accession number: P08401
Secondary accession number(s): Q2M5R8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 19, 2003
Last modified: January 25, 2012
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families