[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 / MG1655 / ATCC 47076; DOI=10.1093/nar/23.12.2105; PubMed=7610040 [NCBI, ExPASy, EBI, Israel, Japan] Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.; "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."; Nucleic Acids Res. 23:2105-2119(1995).
[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]	TOPOLOGY [LARGE SCALE ANALYSIS]. 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 basS/basR. May activate basR 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

D14055; BAA03144.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U14003; AAA97011.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC77073.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE78114.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JX0285; JX0285.

RefSeq

AP_004613.1; -.
NP_418536.1; -.

3D structure databases

HSSP

P02933; 1BXD. [HSSP ENTRY / PDB]

ModBase

P30844.

Protein-protein interaction databases

DIP

DIP:9202N; -.

Enzyme and pathway databases

BioCyc

EcoCyc:BASS-MON; -.

Organism-specific databases

EchoBASE

EB1571; -.

EcoGene

EG11614; basS.

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 UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR003594; ATP_bd_ATPase.
IPR004358; Sig_transdc_His_kin-like_C.
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.

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

948632; -.

GenomeReviews

U00096_GR; b4112.
AP009048_GR; JW4073.

KEGG

ecj:JW4073; -.
eco:b4112; -.

Phylogenomic databases

HOGENOM

P30844; -.

Genome annotation databases

CMR

P30844; b4112.

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`	`1 363`	`363`	`Sensor protein basS/pmrB.`	`PRO_0000074701`
`TOPO_DOM`	`1 13`	`13`	`Cytoplasmic (Potential).`
`TRANSMEM`	`14 34`	`21`	`Potential.`
`TOPO_DOM`	`35 64`	`30`	`Periplasmic (Potential).`
`TRANSMEM`	`65 88`	`24`	`Potential.`
`TOPO_DOM`	`89 363`	`275`	`Cytoplasmic (Potential).`
`DOMAIN`	`89 141`	`53`	`HAMP.`
`DOMAIN`	`149 357`	`209`	`Histidine kinase.`
`MOD_RES`	`152 152`		`Phosphohistidine; by autocatalysis (By similarity).`

Sequence information

Length: 363 AA [This is the length of the unprocessed precursor]

Molecular weight: 41029 Da [This is the MW of the unprocessed precursor]

CRC64: A390AAB9EB425750 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MHFLRRPISL RQRLILTIGA ILLVFELISV FWLWHESTEQ IQLFEQALRD NRNNDRHIMR 

        70         80         90        100        110        120 
EIREAVASLI VPGVFMVSLT LFICYQAVRR ITRPLAELQK ELEARTADNL TPIAIHSATL 

       130        140        150        160        170        180 
EIEAVVSALN DLVSRLTSTL DNERLFTADV AHELRTPLAG VRLHLELLAK THHIDVAPLV 

       190        200        210        220        230        240 
ARLDQMMESV SQLLQLARAG QSFSSGNYQH VKLLEDVILP SYDELSTMLD QRQQTLLLPE 

       250        260        270        280        290        300 
SAADITVQGD ATLLRMLLRN LVENAHRYSP QGSNIMIKLQ EDDGAVMAVE DEGPGIDESK 

       310        320        330        340        350        360 
CGELSKAFVR MDSRYGGIGL GLSIVSRITQ LHHGQFFLQN RQETSGTRAW VRLKKDQYVA 


NQI

P30844 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