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Protein

Sensor histidine kinase CitA

Gene

citA

Organism
Klebsiella pneumoniae
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei109 – 1091Citrate1 Publication
Binding sitei112 – 1121Citrate1 Publication
Binding sitei150 – 1501Citrate1 Publication
Binding sitei152 – 1521Citrate1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Two-component regulatory system

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.13.3. 2814.

Names & Taxonomyi

Protein namesi
Recommended name:
Sensor histidine kinase CitA (EC:2.7.13.3)
Gene namesi
Name:citA
OrganismiKlebsiella pneumoniae
Taxonomic identifieri573 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2323CytoplasmicSequence analysisAdd
BLAST
Transmembranei24 – 4421HelicalSequence analysisAdd
BLAST
Topological domaini45 – 180136PeriplasmicAdd
BLAST
Transmembranei181 – 20121HelicalSequence analysisAdd
BLAST
Topological domaini202 – 547346CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi109 – 1091R → A: Reduces strongly citrate binding. 1 Publication
Mutagenesisi112 – 1121H → A: Reduces strongly citrate binding. 1 Publication
Mutagenesisi141 – 1411R → A: Increases citrate binding. 1 Publication
Mutagenesisi150 – 1501R → A: Reduces citrate binding. 1 Publication
Mutagenesisi152 – 1521K → A: Reduces strongly citrate binding. 1 Publication
Mutagenesisi350 – 3501H → L: Loss of autophosphorylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 547547Sensor histidine kinase CitAPRO_0000074733Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei350 – 3501Phosphohistidine; by autocatalysisCurated

Post-translational modificationi

Autophosphorylated.

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Homodimer. In vitro CitB and the CitA kinase domain form a complex, formation of which is enhanced by ATP.1 Publication

Protein-protein interaction databases

STRINGi272620.KPN_00029.

Structurei

Secondary structure

1
547
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni49 – 513Combined sources
Helixi53 – 6715Combined sources
Helixi70 – 778Combined sources
Helixi81 – 9414Combined sources
Beta strandi98 – 1047Combined sources
Beta strandi107 – 1115Combined sources
Helixi115 – 1173Combined sources
Beta strandi123 – 1253Combined sources
Helixi128 – 1336Combined sources
Beta strandi137 – 1437Combined sources
Beta strandi146 – 15611Combined sources
Beta strandi162 – 17110Combined sources
Helixi172 – 1743Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P0ZX-ray1.60A/B/C/D/E/F/G/H/I/J48-176[»]
2J80X-ray1.60A/B45-176[»]
2V9AX-ray2.00A/B45-176[»]
ProteinModelPortaliP52687.
SMRiP52687. Positions 47-175.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52687.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini225 – 26440PASAdd
BLAST
Domaini347 – 542196Histidine kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi194 – 1985Poly-Leu

Sequence similaritiesi

Contains 1 histidine kinase domain.PROSITE-ProRule annotation
Contains 1 PAS (PER-ARNT-SIM) domain.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CEQ. Bacteria.
COG3290. LUCA.

Family and domain databases

Gene3Di1.10.287.130. 1 hit.
3.30.565.10. 1 hit.
InterProiIPR003594. HATPase_C.
IPR005467. His_kinase_dom.
IPR003661. HisK_dim/P.
IPR000014. PAS.
IPR033463. sCache_3.
IPR029151. Sensor-like.
IPR004358. Sig_transdc_His_kin-like_C.
IPR016120. Sig_transdc_His_kin_SpoOB.
[Graphical view]
PfamiPF02518. HATPase_c. 1 hit.
PF17203. sCache_3_2. 1 hit.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF103190. SSF103190. 1 hit.
SSF55785. SSF55785. 1 hit.
SSF55874. SSF55874. 1 hit.
SSF55890. SSF55890. 1 hit.
PROSITEiPS50109. HIS_KIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P52687-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIYPMYTRK ITHWFARRSF QNRIFLLILF TSTIVMLAMS WYLTDITEER
60 70 80 90 100
LHYQVGQRAL IQAMQISAMP ELVEAVQKRD LARIKALIDP MRSFSDATYI
110 120 130 140 150
TVGDASGQRL YHVNPDEIGK SMEGGDSDEA LINAKSYVSV RKGSLGSSLR
160 170 180 190 200
GKSPIQDATG KVIGIVSVGY TIEQLENWLS LQISSLLIPM AIMLLLLLFC
210 220 230 240 250
ARRFSLHIKK QMLNMEPQQL SQLLIQQSVL FESVFEGLIA IDSDYKITAI
260 270 280 290 300
NQTARRLLNL SQPEPTLIGK RISSVISQEV FFYDAPQTNK KDEIVTFNQI
310 320 330 340 350
KVIASRMAVI LNNEPQGWVI SFRSKDDINT LSLQLSQVQQ YADNLRAVQH
360 370 380 390 400
EHRNLISTIA GLLFLKRYNQ ALELIQQQSE SHQKVIDFIA RNFQDNHLAG
410 420 430 440 450
LLIGKYYRAK ELGLELIFDP ACFVDRLPTA LSHNEWISIV GNLLDNAYNA
460 470 480 490 500
SLRQPQGSKQ IECLINSDGQ EVIIEIADQG CGIDEALRDR IFERGVTSSA
510 520 530 540
SKDHGIGLWL VRSYVEQAGG SIVVENNIPF GTIFTLYIPL TRDEHHG
Length:547
Mass (Da):61,780
Last modified:October 1, 1996 - v1
Checksum:i84D261862F9DE8C7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31464 Genomic DNA. Translation: AAC44733.1.
PIRiS70538.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31464 Genomic DNA. Translation: AAC44733.1.
PIRiS70538.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P0ZX-ray1.60A/B/C/D/E/F/G/H/I/J48-176[»]
2J80X-ray1.60A/B45-176[»]
2V9AX-ray2.00A/B45-176[»]
ProteinModelPortaliP52687.
SMRiP52687. Positions 47-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272620.KPN_00029.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CEQ. Bacteria.
COG3290. LUCA.

Enzyme and pathway databases

BRENDAi2.7.13.3. 2814.

Miscellaneous databases

EvolutionaryTraceiP52687.

Family and domain databases

Gene3Di1.10.287.130. 1 hit.
3.30.565.10. 1 hit.
InterProiIPR003594. HATPase_C.
IPR005467. His_kinase_dom.
IPR003661. HisK_dim/P.
IPR000014. PAS.
IPR033463. sCache_3.
IPR029151. Sensor-like.
IPR004358. Sig_transdc_His_kin-like_C.
IPR016120. Sig_transdc_His_kin_SpoOB.
[Graphical view]
PfamiPF02518. HATPase_c. 1 hit.
PF17203. sCache_3_2. 1 hit.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF103190. SSF103190. 1 hit.
SSF55785. SSF55785. 1 hit.
SSF55874. SSF55874. 1 hit.
SSF55890. SSF55890. 1 hit.
PROSITEiPS50109. HIS_KIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCITA_KLEPN
AccessioniPrimary (citable) accession number: P52687
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.