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Protein

Sensor histidine kinase RcsC

Gene

rcsC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the Rcs signaling system, which controls transcription of numerous genes. RcsC functions as a membrane-associated protein kinase that phosphorylates RcsD in response to environmental signals. The phosphoryl group is then transferred to the response regulator RcsB. RcsC has also phosphatase activity. The system controls expression of genes involved in colanic acid capsule synthesis, biofilm formation and cell division.UniRule annotation6 Publications

Catalytic activityi

ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.UniRule annotation

Enzyme regulationi

The Rcs phosphorelay may be activated by RcsF. DjlA, LolA and OmpG might act as a regulator of the phosphorelay. Activity is probably up-regulated by YmgA/AriR, and possibly down-regulated by YcgZ, all 3 are connector proteins providing additional signal input into signaling system.3 Publications

GO - Molecular functioni

  • ATP binding Source: UniProtKB-HAMAP
  • phosphorelay sensor kinase activity Source: EcoCyc

GO - Biological processi

  • cellular response to osmotic stress Source: EcoCyc
  • phosphorelay signal transduction system Source: EcoCyc
  • protein autophosphorylation Source: EcoCyc
  • regulation of transcription, DNA-templated Source: InterPro
  • single-species biofilm formation Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Capsule biogenesis/degradation, Two-component regulatory system

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Sensor histidine kinase RcsCUniRule annotation (EC:2.7.13.3UniRule annotation)
Alternative name(s):
Capsular synthesis regulator component C
Gene namesi
Name:rcsCUniRule annotation
Ordered Locus Names:b2218, JW5917/JW5920
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10822. rcsC.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1919CytoplasmicSequence analysisAdd
BLAST
Transmembranei20 – 4122HelicalUniRule annotationAdd
BLAST
Topological domaini42 – 313272PeriplasmicSequence analysisAdd
BLAST
Transmembranei314 – 33522HelicalUniRule annotationAdd
BLAST
Topological domaini336 – 949614CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: UniProtKB-HAMAP
  • intracellular Source: GOC
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi479 – 4791H → Q: Does not induce cps operon expression. Retains phosphatase activity. 1 Publication
Mutagenesisi875 – 8751D → Q: Does not induce cps operon expression. Lack of phosphatase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 949949Sensor histidine kinase RcsCPRO_0000074856Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei479 – 4791Phosphohistidine; by autocatalysisCurated
Modified residuei875 – 87514-aspartylphosphateCurated

Post-translational modificationi

Autophosphorylated. Activation probably requires a transfer of a phosphate group from a His in the transmitter domain to an Asp in the receiver domain.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP0DMC5.

Interactioni

Subunit structurei

Interacts with RcsD.UniRule annotation2 Publications

Protein-protein interaction databases

IntActiP0DMC5. 1 interaction.
MINTiMINT-1267658.
STRINGi511145.b2218.

Structurei

Secondary structure

1
949
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni703 – 7064Combined sources
Beta strandi707 – 7126Combined sources
Helixi716 – 72611Combined sources
Turni727 – 7304Combined sources
Beta strandi731 – 7355Combined sources
Beta strandi746 – 7527Combined sources
Beta strandi759 – 7657Combined sources
Beta strandi770 – 7723Combined sources
Beta strandi780 – 7834Combined sources
Helixi790 – 79910Combined sources
Beta strandi826 – 8338Combined sources
Helixi834 – 84714Combined sources
Beta strandi849 – 8546Combined sources
Helixi858 – 8669Combined sources
Beta strandi870 – 8789Combined sources
Helixi884 – 89411Combined sources
Beta strandi899 – 90810Combined sources
Helixi909 – 9168Combined sources
Beta strandi920 – 9267Combined sources
Helixi929 – 94719Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AYXNMR-A700-949[»]
2AYYNMR-A700-816[»]
2AYZNMR-A817-949[»]
ProteinModelPortaliP0DMC5.
SMRiP0DMC5. Positions 455-689, 700-949.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini357 – 42569PASUniRule annotationAdd
BLAST
Domaini476 – 692217Histidine kinaseUniRule annotationAdd
BLAST
Domaini705 – 805101ABLUniRule annotationAdd
BLAST
Domaini826 – 940115Response regulatoryPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the RcsC family.UniRule annotation
Contains 1 ABL domain.UniRule annotation
Contains 1 histidine kinase domain.UniRule annotation
Contains 1 PAS (PER-ARNT-SIM) domain.UniRule annotation
Contains 1 response regulatory domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105BZU. Bacteria.
ENOG410XNMH. LUCA.
KOiK07677.
OMAiTRCWLAV.
PhylomeDBiP0DMC5.

Family and domain databases

Gene3Di1.10.287.130. 1 hit.
3.30.565.10. 1 hit.
HAMAPiMF_00979. RcsC. 1 hit.
InterProiIPR011006. CheY-like_superfamily.
IPR003594. HATPase_C.
IPR005467. His_kinase_dom.
IPR003661. HisK_dim/P.
IPR030856. RcsC.
IPR004358. Sig_transdc_His_kin-like_C.
IPR019017. Sig_transdc_His_kin_a/b-loop_C.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamiPF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
PF09456. RcsC. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF47384. SSF47384. 1 hit.
SSF52172. SSF52172. 2 hits.
SSF55874. SSF55874. 1 hit.
PROSITEiPS51426. ABL. 1 hit.
PS50109. HIS_KIN. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0DMC5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKYLASFRTT LKASRYMFRA LALVLWLLIA FSSVFYIVNA LHQRESEIRQ
60 70 80 90 100
EFNLSSDQAQ RFIQRTSDVM KELKYIAENR LSAENGVLSP RGRETQADVP
110 120 130 140 150
AFEPLFADSD CSAMSNTWRG SLESLAWFMR YWRDNFSAAY DLNRVFLIGS
160 170 180 190 200
DNLCMANFGL RDMPVERDTA LKALHERINK YRNAPQDDSG SNLYWISEGP
210 220 230 240 250
RPGVGYFYAL TPVYLANRLQ ALLGVEQTIR MENFFLPGTL PMGVTILDEN
260 270 280 290 300
GHTLISLTGP ESKIKGDPRW MQERSWFGYT EGFRELVLKK NLPPSSLSIV
310 320 330 340 350
YSVPVDKVLE RIRMLILNAI LLNVLAGAAL FTLARMYERR IFIPAESDAL
360 370 380 390 400
RLEEHEQFNR KIVASAPVGI CILRTADGVN ILSNELAHTY LNMLTHEDRQ
410 420 430 440 450
RLTQIICGQQ VNFVDVLTSN NTNLQISFVH SRYRNENVAI CVLVDVSSRV
460 470 480 490 500
KMEESLQEMA QAAEQASQSK SMFLATVSHE LRTPLYGIIG NLDLLQTKEL
510 520 530 540 550
PKGVDRLVTA MNNSSSLLLK IISDILDFSK IESEQLKIEP REFSPREVMN
560 570 580 590 600
HITANYLPLV VRKQLGLYCF IEPDVPVALN GDPMRLQQVI SNLLSNAIKF
610 620 630 640 650
TDTGCIVLHV RADGDYLSIR VRDTGVGIPA KEVVRLFDPF FQVGTGVQRN
660 670 680 690 700
FQGTGLGLAI CEKLISMMDG DISVDSEPGM GSQFTVRIPL YGAQYPQKKG
710 720 730 740 750
VEGLSGKRCW LAVRNASLCQ FLETSLQRSG IVVTTYEGQE PTPEDVLITD
760 770 780 790 800
EVVSKKWQGR AVVTFCRRHI GIPLEKAPGE WVHSVAAPHE LPALLARIYL
810 820 830 840 850
IEMESDDPAN ALPSTDKAVS DNDDMMILVV DDHPINRRLL ADQLGSLGYQ
860 870 880 890 900
CKTANDGVDA LNVLSKNHID IVLSDVNMPN MDGYRLTQRI RQLGLTLPVI
910 920 930 940
GVTANALAEE KQRCLESGMD SCLSKPVTLD VIKQTLTLYA ERVRKSRDS
Length:949
Mass (Da):106,506
Last modified:February 19, 2014 - v1
Checksum:iE37E9D70EC944A78
GO

Sequence cautioni

The sequence AAA24503 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA16001 differs from that shown. Reason: Frameshift at position 808. Curated
The sequence BAA16014 differs from that shown. Reason: Frameshift at position 808. Curated
The sequence BAA16014 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1302MR → IG in AAA24503 (PubMed:2404948).Curated
Sequence conflicti935 – 9351T → S in AAA24503 (PubMed:2404948).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28242 Genomic DNA. Translation: AAA24503.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75278.2.
AP009048 Genomic DNA. Translation: BAA16001.2. Frameshift.
AP009048 Genomic DNA. Translation: BAA16014.1. Sequence problems.
PIRiH64991. BVECCC.
RefSeqiNP_416722.2. NC_000913.3.
WP_000876011.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75278; AAC75278; b2218.
BAA16001; BAA16001; BAA16001.
BAA16014; BAA16014; BAA16014.
GeneIDi948993.
KEGGiecj:JW5917.
ecj:JW5920.
eco:b2218.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28242 Genomic DNA. Translation: AAA24503.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75278.2.
AP009048 Genomic DNA. Translation: BAA16001.2. Frameshift.
AP009048 Genomic DNA. Translation: BAA16014.1. Sequence problems.
PIRiH64991. BVECCC.
RefSeqiNP_416722.2. NC_000913.3.
WP_000876011.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AYXNMR-A700-949[»]
2AYYNMR-A700-816[»]
2AYZNMR-A817-949[»]
ProteinModelPortaliP0DMC5.
SMRiP0DMC5. Positions 455-689, 700-949.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0DMC5. 1 interaction.
MINTiMINT-1267658.
STRINGi511145.b2218.

Proteomic databases

PaxDbiP0DMC5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75278; AAC75278; b2218.
BAA16001; BAA16001; BAA16001.
BAA16014; BAA16014; BAA16014.
GeneIDi948993.
KEGGiecj:JW5917.
ecj:JW5920.
eco:b2218.

Organism-specific databases

EchoBASEiEB0815.
EcoGeneiEG10822. rcsC.

Phylogenomic databases

eggNOGiENOG4105BZU. Bacteria.
ENOG410XNMH. LUCA.
KOiK07677.
OMAiTRCWLAV.
PhylomeDBiP0DMC5.

Miscellaneous databases

PROiP0DMC5.

Family and domain databases

Gene3Di1.10.287.130. 1 hit.
3.30.565.10. 1 hit.
HAMAPiMF_00979. RcsC. 1 hit.
InterProiIPR011006. CheY-like_superfamily.
IPR003594. HATPase_C.
IPR005467. His_kinase_dom.
IPR003661. HisK_dim/P.
IPR030856. RcsC.
IPR004358. Sig_transdc_His_kin-like_C.
IPR019017. Sig_transdc_His_kin_a/b-loop_C.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamiPF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
PF09456. RcsC. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF47384. SSF47384. 1 hit.
SSF52172. SSF52172. 2 hits.
SSF55874. SSF55874. 1 hit.
PROSITEiPS51426. ABL. 1 hit.
PS50109. HIS_KIN. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRCSC_ECOLI
AccessioniPrimary (citable) accession number: P0DMC5
Secondary accession number(s): P14376
, P76457, P97170, P97202, Q47586
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 19, 2014
Last sequence update: February 19, 2014
Last modified: July 6, 2016
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

There is a close linkage between the Rcs and PhoQ/P signaling systems, and both signaling systems respond to certain external divalent cations (zinc and magnesium).1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.