[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; PubMed=8282725 [NCBI, ExPASy, EBI, Israel, Japan] Nagasawa S., Ishige K., Mizuno T.; "Novel members of the two-component signal transduction genes in Escherichia coli."; J. Biochem. 114:350-357(1993).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1093/dnares/3.6.379; PubMed=9097040 [NCBI, ExPASy, EBI, Israel, Japan] Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.; "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."; DNA Res. 3:379-392(1996).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[5]	SUBCELLULAR LOCATION. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.1109730; PubMed=15919996 [NCBI, ExPASy, EBI, Israel, Japan] Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.; "Global topology analysis of the Escherichia coli inner membrane proteome."; Science 308:1321-1323(2005).

Comments

FUNCTION: Member of the two-component regulatory system baeS/baeR. May activate baeR by phosphorylation.
CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
SIMILARITY: Contains 1 HAMP domain.
SIMILARITY: Contains 1 histidine kinase domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D14054; BAA03140.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75139.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA15934.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

E64974; E64974.

RefSeq

AP_002678.1; -.
NP_416582.1; -.

3D structure databases

ModBase

P30847.

Protein-protein interaction databases

DIP

DIP:9199N; -.

Enzyme and pathway databases

BioCyc

EcoCyc:BAES-MON; -.

Organism-specific databases

EchoBASE

EB1574; -.

EcoGene

EG11617; baeS.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0000155;	Molecular function: two-component sensor activity (inferred from electronic annotation from InterPro).
GO:0018106;	Biological process: peptidyl-histidine phosphorylation (inferred from electronic annotation from InterPro).
GO:0000160;	Biological process: two-component signal transduction system (phosphorelay) (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR003594; ATP_bd_ATPase.
IPR004358; Sig_transdc_His_kin-like_C.
IPR008358; Sig_transdc_His_kin/Pase_MprB.
IPR003661; Sig_transdc_His_kin_sub1_dim/P.
IPR005467; Sig_transdc_His_kinase_core.
IPR003660; Sig_transdc_His_kinase_HAMP.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.565.10; ATP_bd_ATPase; 1.

Pfam

PF00672; HAMP; 1.
PF02518; HATPase_c; 1.
PF00512; HisKA; 1.
Pfam graphical view of domain structure.

PRINTS

PR00344; BCTRLSENSOR.
PR01780; LANTIREGPROT.

SMART

SM00304; HAMP; 1.
SM00387; HATPase_c; 1.
SM00388; HisKA; 1.
SMART graphical view of domain structure.

PROSITE

PS50885; HAMP; 1.
PS50109; HIS_KIN; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

946611; -.

GenomeReviews

U00096_GR; b2078.
AP009048_GR; JW2063.

KEGG

ecj:JW2063; -.
eco:b2078; -.

Phylogenomic databases

HOGENOM

P30847; -.

Genome annotation databases

CMR

P30847; b2078.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cell inner membrane; Cell membrane; Complete proteome; Kinase; Membrane; Phosphoprotein; Transferase; Transmembrane; Two-component regulatory system.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 467`	`467`	`Signal transduction histidine-protein kinase baeS.`	`PRO_0000074696`
`TOPO_DOM`	`1 11`	`11`	`Cytoplasmic (Potential).`
`TRANSMEM`	`12 32`	`21`	`Potential.`
`TOPO_DOM`	`33 167`	`135`	`Periplasmic (Potential).`
`TRANSMEM`	`168 186`	`19`	`Potential.`
`TOPO_DOM`	`187 467`	`281`	`Cytoplasmic (Potential).`
`DOMAIN`	`187 239`	`53`	`HAMP.`
`DOMAIN`	`247 461`	`215`	`Histidine kinase.`
`MOD_RES`	`250 250`		`Phosphohistidine; by autocatalysis (By similarity).`
`CONFLICT`	`414 421`		`GSRNRASG -> VPATVPA (in Ref. 1; BAA03140).`

Sequence information

Length: 467 AA [This is the length of the unprocessed precursor]

Molecular weight: 51991 Da [This is the MW of the unprocessed precursor]

CRC64: 024D76950012FFE0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKFWRPGITG KLFLAIFATC IVLLISMHWA VRISFERGFI DYIKHGNEQR LQLLSDALGE 

        70         80         90        100        110        120 
QYAQHGNWRF LRNNDRFVFQ ILRSFEHDNS EDKPGPGMPP HGWRTQFWVV DQNNKVLVGP 

       130        140        150        160        170        180 
RAPIPPDGTR RPILVNGAEV GAVIASPVER LTRNTDINFD KQQRQTSWLI VALATLLAAL 

       190        200        210        220        230        240 
ATFLLARGLL APVKRLVDGT HKLAAGDFTT RVTPTSEDEL GKLAQDFNQL ASTLEKNQQM 

       250        260        270        280        290        300 
RRDFMADISH ELRTPLAVLR GELEAIQDGV RKFTPETVAS LQAEVGTLTK LVDDLHQLSM 

       310        320        330        340        350        360 
SDEGALAYQK APVDLIPLLE VAGGAFRERF ASRGLKLQFS LPDSITVFGD RDRLMQLFNN 

       370        380        390        400        410        420 
LLENSLRYTD SGGSLQISAG QRDKTVRLTF ADSAPGVSDD QLQKLFERFY RTEGSRNRAS 

       430        440        450        460 
GGSGLGLAIC LNIVEAHNGR IIAAHSPFGG VSITVELPLE RDLQREV

P30847 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools