Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Binding sitei109Citrate1 Publication1
Binding sitei112Citrate1 Publication1
Binding sitei150Citrate1 Publication1
Binding sitei152Citrate1 Publication1

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeKlebsiella

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 23CytoplasmicSequence analysisAdd BLAST23
Transmembranei24 – 44HelicalSequence analysisAdd BLAST21
Topological domaini45 – 180PeriplasmicAdd BLAST136
Transmembranei181 – 201HelicalSequence analysisAdd BLAST21
Topological domaini202 – 547CytoplasmicSequence analysisAdd BLAST346

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi109R → A: Reduces strongly citrate binding. 1 Publication1
Mutagenesisi112H → A: Reduces strongly citrate binding. 1 Publication1
Mutagenesisi141R → A: Increases citrate binding. 1 Publication1
Mutagenesisi150R → A: Reduces citrate binding. 1 Publication1
Mutagenesisi152K → A: Reduces strongly citrate binding. 1 Publication1
Mutagenesisi350H → L: Loss of autophosphorylation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000747331 – 547Sensor histidine kinase CitAAdd BLAST547

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei350Phosphohistidine; by autocatalysisCurated1

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

1547
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni49 – 51Combined sources3
Helixi53 – 67Combined sources15
Helixi70 – 77Combined sources8
Helixi81 – 94Combined sources14
Beta strandi98 – 104Combined sources7
Beta strandi107 – 111Combined sources5
Helixi115 – 117Combined sources3
Beta strandi123 – 125Combined sources3
Helixi128 – 133Combined sources6
Beta strandi137 – 143Combined sources7
Beta strandi146 – 156Combined sources11
Beta strandi162 – 171Combined sources10
Helixi172 – 174Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52687.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini225 – 264PASAdd BLAST40
Domaini347 – 542Histidine kinasePROSITE-ProRule annotationAdd BLAST196

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi194 – 198Poly-Leu5

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
PDB 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.
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: November 2, 2016
This is version 107 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.