P52687 (CITA_KLEPN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sensor histidine kinase CitA
EC=2.7.13.3

Gene names

Name:

citA

Organism

Klebsiella pneumoniae

Taxonomic identifier

573 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Klebsiella

Protein attributes

Sequence length	547 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Member of the two-component regulatory system CitA/CitB. Probably activates CitB by phosphorylation. The periplasmic domain binds H-citrate2-, which is essential for induction of the citrate-fermentation genes. Ref.2
Catalytic activity	ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. Ref.2
Subunit structure	Homodimer. In vitro CitB and the CitA kinase domain form a complex, formation of which is enhanced by ATP.
Subcellular location	Cell inner membrane; Multi-pass membrane protein Probable.
Post-translational modification	Autophosphorylated. Ref.2
Sequence similarities	Contains 1 histidine kinase domain. Contains 1 PAS (PER-ARNT-SIM) domain.

Ontologies

Keywords
Biological process	Two-component regulatory system
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	peptidyl-histidine phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 547

547

Sensor histidine kinase CitA

PRO_0000074733

Regions

Topological domain

1 – 23

23

Cytoplasmic Potential

Transmembrane

24 – 44

21

Helical; Potential

Topological domain

45 – 180

136

Periplasmic

Transmembrane

181 – 201

21

Helical; Potential

Topological domain

202 – 547

346

Cytoplasmic Potential

Domain

225 – 264

40

PAS

Domain

347 – 542

196

Histidine kinase

Compositional bias

194 – 198

5

Poly-Leu

Sites

Binding site

109

1

Citrate

Binding site

112

1

Citrate

Binding site

150

1

Citrate

Binding site

152

1

Citrate

Amino acid modifications

Modified residue

350

1

Phosphohistidine; by autocatalysis Probable

Experimental info

Mutagenesis

109

1

R → A: Reduces strongly citrate binding. Ref.3

Mutagenesis

112

1

H → A: Reduces strongly citrate binding. Ref.3

Mutagenesis

141

1

R → A: Increases citrate binding. Ref.3

Mutagenesis

150

1

R → A: Reduces citrate binding. Ref.3

Mutagenesis

152

1

K → A: Reduces strongly citrate binding. Ref.3

Mutagenesis

350

1

H → L: Loss of autophosphorylation. Ref.2

Secondary structure

1

.

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.

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547

Helix Strand Turn

Details...

Helix

50 – 67

18

Helix

70 – 77

8

Helix

81 – 93

13

Beta strand

98 – 104

7

Beta strand

107 – 111

5

Helix

115 – 117

3

Beta strand

123 – 125

3

Helix

128 – 131

4

Beta strand

137 – 143

7

Beta strand

146 – 156

11

Beta strand

162 – 171

10

Helix

172 – 174

3

Sequences

	Sequence		Length	Mass (Da)
	P52687 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 84D261862F9DE8C7	FASTA	547	61,780
	10 20 30 40 50 60 MSIYPMYTRK ITHWFARRSF QNRIFLLILF TSTIVMLAMS WYLTDITEER LHYQVGQRAL 70 80 90 100 110 120 IQAMQISAMP ELVEAVQKRD LARIKALIDP MRSFSDATYI TVGDASGQRL YHVNPDEIGK 130 140 150 160 170 180 SMEGGDSDEA LINAKSYVSV RKGSLGSSLR GKSPIQDATG KVIGIVSVGY TIEQLENWLS 190 200 210 220 230 240 LQISSLLIPM AIMLLLLLFC ARRFSLHIKK QMLNMEPQQL SQLLIQQSVL FESVFEGLIA 250 260 270 280 290 300 IDSDYKITAI NQTARRLLNL SQPEPTLIGK RISSVISQEV FFYDAPQTNK KDEIVTFNQI 310 320 330 340 350 360 KVIASRMAVI LNNEPQGWVI SFRSKDDINT LSLQLSQVQQ YADNLRAVQH EHRNLISTIA 370 380 390 400 410 420 GLLFLKRYNQ ALELIQQQSE SHQKVIDFIA RNFQDNHLAG LLIGKYYRAK ELGLELIFDP 430 440 450 460 470 480 ACFVDRLPTA LSHNEWISIV GNLLDNAYNA SLRQPQGSKQ IECLINSDGQ EVIIEIADQG 490 500 510 520 530 540 CGIDEALRDR IFERGVTSSA SKDHGIGLWL VRSYVEQAGG SIVVENNIPF GTIFTLYIPL TRDEHHG

References

[1]	"Regulation of anaerobic citrate metabolism in Klebsiella pneumoniae." Bott M., Meyer M., Dimroth P. Mol. Microbiol. 18:533-546(1995) [PubMed: 8748036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 13882 / NBRC 13541 / NCTC 8172.
[2]	"The periplasmic domain of the histidine autokinase CitA functions as a highly specific citrate receptor." Kaspar S., Perozzo R., Reinelt S., Meyer M., Pfister K., Scapozza L., Bott M. Mol. Microbiol. 33:858-872(1999) [PubMed: 10447894] [Abstract] Cited for: FUNCTION, CITRATE-BINDING, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, CHARACTERIZATION, MUTAGENESIS OF HIS-350. Strain: ATCC 13882 / NBRC 13541 / NCTC 8172.
[3]	"Identification of basic amino acid residues important for citrate binding by the periplasmic receptor domain of the sensor kinase CitA." Gerharz T., Reinelt S., Kaspar S., Scapozza L., Bott M. Biochemistry 42:5917-5924(2003) [PubMed: 12741850] [Abstract] Cited for: MUTAGENESIS OF ARG-109; HIS-112; ARG-141; ARG-150 AND LYS-152.
[4]	"The structure of the periplasmic ligand-binding domain of the sensor kinase CitA reveals the first extracellular PAS domain." Reinelt S., Hofmann E., Gerharz T., Bott M., Madden D.R. J. Biol. Chem. 278:39189-39196(2003) [PubMed: 12867417] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH CITRATE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U31464 Genomic DNA. Translation: AAC44733.1.

PIR

S70538.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P0Z	X-ray	1.60	A/B/C/D/E/F/G/H/I/J	48-176	[»]
2J80	X-ray	1.60	A/B	45-176	[»]
2V9A	X-ray	2.00	A/B	45-176	[»]

ProteinModelPortal

P52687.

SMR

P52687. Positions 47-175.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

2.7.13.3. 2814.

Family and domain databases

InterPro

IPR003594. ATPase-like_ATP-bd.
IPR000014. PAS.
IPR004358. Sig_transdc_His_kin-like_C.
IPR005467. Sig_transdc_His_kinase_core.
IPR016121. Spore_sensor_kin_SpoOB_hlx.
[Graphical view]

Gene3D

G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.
G3DSA:1.10.287.130. Sensor_kinase_SpoOB-type_hlx. 1 hit.

Pfam

PF02518. HATPase_c. 1 hit.
[Graphical view]

PRINTS

PR00344. BCTRLSENSOR.

SMART

SM00387. HATPase_c. 1 hit.
SM00091. PAS. 1 hit.
[Graphical view]

SUPFAM

SSF55874. ATP_bd_ATPase. 1 hit.

PROSITE

PS50109. HIS_KIN. 1 hit.
PS50112. PAS. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CITA_KLEPN

Accession

Primary (citable) accession number: P52687

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	September 21, 2011
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program