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 RcsC

Gene

rcsC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

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

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-KW
  • 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

Keywordsi

Molecular functionKinase, Transferase
Biological processCapsule biogenesis/degradation, Two-component regulatory system
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:RCSC-MONOMER

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10822 rcsC

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 19CytoplasmicSequence analysisAdd BLAST19
Transmembranei20 – 41HelicalUniRule annotationAdd BLAST22
Topological domaini42 – 313PeriplasmicSequence analysisAdd BLAST272
Transmembranei314 – 335HelicalUniRule annotationAdd BLAST22
Topological domaini336 – 949CytoplasmicSequence analysisAdd BLAST614

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • intracellular Source: GOC
  • plasma membrane Source: EcoCyc

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi479H → Q: Does not induce cps operon expression. Retains phosphatase activity. 1 Publication1
Mutagenesisi875D → Q: Does not induce cps operon expression. Lack of phosphatase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000748561 – 949Sensor histidine kinase RcsCAdd BLAST949

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei479Phosphohistidine; by autocatalysisCurated1
Modified residuei8754-aspartylphosphateCurated1

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
PRIDEiP0DMC5

PTM databases

iPTMnetiP0DMC5

Interactioni

Subunit structurei

Interacts with RcsD.UniRule annotation2 Publications

Protein-protein interaction databases

IntActiP0DMC5, 1 interactor
STRINGi316385.ECDH10B_2376

Structurei

Secondary structure

1949
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni703 – 706Combined sources4
Beta strandi707 – 712Combined sources6
Helixi716 – 726Combined sources11
Turni727 – 730Combined sources4
Beta strandi731 – 735Combined sources5
Beta strandi746 – 752Combined sources7
Beta strandi759 – 765Combined sources7
Beta strandi770 – 772Combined sources3
Beta strandi780 – 783Combined sources4
Helixi790 – 799Combined sources10
Beta strandi826 – 833Combined sources8
Helixi834 – 847Combined sources14
Beta strandi849 – 854Combined sources6
Helixi858 – 866Combined sources9
Beta strandi870 – 878Combined sources9
Helixi884 – 894Combined sources11
Beta strandi899 – 908Combined sources10
Helixi909 – 916Combined sources8
Beta strandi920 – 926Combined sources7
Helixi929 – 947Combined sources19

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini357 – 425PASUniRule annotationAdd BLAST69
Domaini476 – 692Histidine kinaseUniRule annotationAdd BLAST217
Domaini705 – 805ABLUniRule annotationAdd BLAST101
Domaini826 – 940Response regulatoryPROSITE-ProRule annotationAdd BLAST115

Sequence similaritiesi

Belongs to the RcsC family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105BZU Bacteria
ENOG410XNMH LUCA
KOiK07677
OMAiTRCWLAV
PhylomeDBiP0DMC5

Family and domain databases

CDDicd00075 HATPase_c, 1 hit
cd00082 HisKA, 1 hit
cd00156 REC, 1 hit
Gene3Di3.30.565.10, 1 hit
3.40.50.10970, 1 hit
HAMAPiMF_00979 RcsC, 1 hit
InterProiView protein in InterPro
IPR011006 CheY-like_superfamily
IPR003594 HATPase_C
IPR036890 HATPase_C_sf
IPR005467 His_kinase_dom
IPR003661 HisK_dim/P
IPR036097 HisK_dim/P_sf
IPR030856 RcsC
IPR038388 RcsC_C_sf
IPR004358 Sig_transdc_His_kin-like_C
IPR019017 Sig_transdc_His_kin_a/b-loop_C
IPR001789 Sig_transdc_resp-reg_receiver
PfamiView protein in Pfam
PF02518 HATPase_c, 1 hit
PF00512 HisKA, 1 hit
PF09456 RcsC, 1 hit
PF00072 Response_reg, 1 hit
PRINTSiPR00344 BCTRLSENSOR
SMARTiView protein in SMART
SM00387 HATPase_c, 1 hit
SM00388 HisKA, 1 hit
SM00448 REC, 1 hit
SUPFAMiSSF47384 SSF47384, 1 hit
SSF52172 SSF52172, 2 hits
SSF55874 SSF55874, 1 hit
PROSITEiView protein in PROSITE
PS51426 ABL, 1 hit
PS50109 HIS_KIN, 1 hit
PS50110 RESPONSE_REGULATORY, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti129 – 130MR → IG in AAA24503 (PubMed:2404948).Curated2
Sequence conflicti935T → S in AAA24503 (PubMed:2404948).Curated1

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
PATRICifig|511145.12.peg.2307

Similar proteinsi

Entry informationi

Entry nameiRCSC_ECOLI
AccessioniPrimary (citable) accession number: P0DMC5
Secondary accession number(s): P14376
, P76457, P97170, P97202, Q47586
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 19, 2014
Last sequence update: February 19, 2014
Last modified: March 28, 2018
This is version 33 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health