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Protein

Phosphotransferase RcsD

Gene

rcsD

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. RcsD is a phosphotransfer intermediate between the sensor kinase RcsC and the response regulator RcsB. It acquires a phosphoryl group from RcsC and transfers it to RcsB. The system controls expression of genes involved in colanic acid capsule synthesis, biofilm formation and cell division.UniRule annotation5 Publications

GO - Molecular functioni

  • ATP binding Source: UniProtKB-HAMAP
  • histidine phosphotransfer kinase activity Source: EcoCyc
  • phosphotransferase activity, carboxyl group as acceptor Source: UniProtKB-HAMAP

GO - Biological processi

  • phosphorelay signal transduction system Source: EcoCyc
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

BioCyciEcoCyc:EG12385-MONOMER.
ECOL316407:JW2204-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphotransferase RcsDUniRule annotation (EC:2.7.2.-UniRule annotation)
Alternative name(s):
Phosphotransfer intermediate RcsDUniRule annotation
Gene namesi
Name:rcsDUniRule annotation
Synonyms:yojN, yojP, yojQ
Ordered Locus Names:b2216, JW2204
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12385. rcsD.

Subcellular locationi

  • Cell inner membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2121CytoplasmicSequence analysisAdd
BLAST
Transmembranei22 – 4221HelicalUniRule annotationAdd
BLAST
Topological domaini43 – 308266PeriplasmicSequence analysisAdd
BLAST
Transmembranei309 – 32921HelicalUniRule annotationAdd
BLAST
Topological domaini330 – 890561CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: EcoCyc
  • 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
Mutagenesisi842 – 8421H → R: Lack of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 890890Phosphotransferase RcsDPRO_0000074916Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei842 – 8421PhosphohistidineUniRule annotation1 Publication

Post-translational modificationi

Phosphorylated by RcsC.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP39838.
PRIDEiP39838.

PTM databases

iPTMnetiP39838.

Interactioni

Subunit structurei

Interacts with RcsC and RcsB. Has a higher affinity for RcsB than for RcsC.UniRule annotation1 Publication

Protein-protein interaction databases

DIPiDIP-12815N.
IntActiP39838. 4 interactions.
MINTiMINT-1304951.
STRINGi511145.b2216.

Structurei

Secondary structure

1
890
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi690 – 69910Combined sources
Helixi703 – 71513Combined sources
Beta strandi718 – 7214Combined sources
Beta strandi725 – 7284Combined sources
Beta strandi733 – 7397Combined sources
Helixi740 – 7423Combined sources
Beta strandi744 – 7507Combined sources
Beta strandi755 – 7617Combined sources
Beta strandi764 – 7674Combined sources
Beta strandi784 – 7874Combined sources
Helixi801 – 8088Combined sources
Helixi811 – 8144Combined sources
Turni815 – 8173Combined sources
Helixi818 – 83114Combined sources
Helixi834 – 85118Combined sources
Helixi854 – 86815Combined sources
Helixi872 – 88918Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SR2NMR-A775-890[»]
2KX7NMR-A688-795[»]
ProteinModelPortaliP39838.
SMRiP39838. Positions 688-890.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39838.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini803 – 89088HPtUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni468 – 678211Histidine-like kinaseAdd
BLAST

Sequence similaritiesi

Belongs to the RcsD family.UniRule annotation
Contains 1 histidine kinase domain.Curated
Contains 1 HPt domain.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105E3G. Bacteria.
COG2198. LUCA.
HOGENOMiHOG000122289.
KOiK07676.
OMAiTWRYATW.

Family and domain databases

Gene3Di1.20.120.160. 1 hit.
3.30.565.10. 1 hit.
HAMAPiMF_00980. RcsD. 1 hit.
InterProiIPR003594. HATPase_C.
IPR005467. His_kinase_dom.
IPR030861. Ptransferase_RcsD.
IPR032306. RcsD_ABL.
IPR008207. Sig_transdc_His_kin_Hpt_dom.
[Graphical view]
PfamiPF02518. HATPase_c. 1 hit.
PF01627. Hpt. 1 hit.
PF16359. RcsD_ABL. 1 hit.
[Graphical view]
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF47226. SSF47226. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiPS50109. HIS_KIN. 1 hit.
PS50894. HPT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39838-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRQKETTATT RFSLLPGSIT RFFLLLIIVL LVTMGVMVQS AVNAWLKDKS
60 70 80 90 100
YQIVDITHAI QKRVDNWRYV TWQIYDNIAA TTSPSSGEGL QETRLKQDVY
110 120 130 140 150
YLEKPRRKTE ALIFGSHDNS TLEMTQRMST YLDTLWGAEN VPWSMYYLNG
160 170 180 190 200
QDNSLVLIST LPLKDLTSGF KESTVSDIVD SRRAEMLQQA NALDERESFS
210 220 230 240 250
NMRRLAWQNG HYFTLRTTFN QPGHLATVVA FDLPINDLIP PGMPLDSFRL
260 270 280 290 300
EPDATATGNN DNEKEGTDSV SIHFNSTKIE ISSALNSTDM RLVWQVPYGT
310 320 330 340 350
LLLDTLQNIL LPLLLNIGLL ALALFGYTTF RHFSSRSTEN VPSTAVNNEL
360 370 380 390 400
RILRAINEEI VSLLPLGLLV HDQESNRTVI SNKIADHLLP HLNLQNITTM
410 420 430 440 450
AEQHQGIIQA TINNELYEIR MFRSQVAPRT QIFIIRDQDR EVLVNKKLKQ
460 470 480 490 500
AQRLYEKNQQ GRMIFMKNIG DALKEPAQSL AESAAKLNAP ESKQLANQAD
510 520 530 540 550
VLVRLVDEIQ LANMLADDSW KSETVLFSVQ DLIDEVVPSV LPAIKRKGLQ
560 570 580 590 600
LLINNHLKAH DMRRGDRDAL RRILLLLMQY AVTSTQLGKI TLEVDQDESS
610 620 630 640 650
EDRLTFRILD TGEGVSIHEM DNLHFPFINQ TQNDRYGKAD PLAFWLSDQL
660 670 680 690 700
ARKLGGHLNI KTRDGLGTRY SVHIKMLAAD PEVEEEEERL LDDVCVMVDV
710 720 730 740 750
TSAEIRNIVT RQLENWGATC ITPDERLISQ DYDIFLTDNP SNLTASGLLL
760 770 780 790 800
SDDESGVREI GPGQLCVNFN MSNAMQEAVL QLIEVQLAQE EVTESPLGGD
810 820 830 840 850
ENAQLHASGY YALFVDTVPD DVKRLYTEAA TSDFAALAQT AHRLKGVFAM
860 870 880 890
LNLVPGKQLC ETLEHLIREK DVPGIEKYIS DIDSYVKSLL
Length:890
Mass (Da):100,372
Last modified:November 1, 1997 - v3
Checksum:iAE26E2E70E363830
GO

Sequence cautioni

The sequence AAA81025 differs from that shown. Reason: Frameshift at positions 145 and 488. Curated
The sequence AAA81026 differs from that shown. Reason: Frameshift at positions 145 and 488. Curated
The sequence AAA81027 differs from that shown. Reason: Frameshift at positions 145 and 488. Curated
The sequence M28242 differs from that shown. Reason: Frameshift at positions 597 and 702. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611Q → L in AAA81025 (Ref. 4) Curated
Sequence conflicti164 – 1641K → E in AAA81026 (Ref. 4) Curated
Sequence conflicti174 – 1741T → A in AAA81026 (Ref. 4) Curated
Sequence conflicti176 – 1761S → N in AAA81026 (Ref. 4) Curated
Sequence conflicti179 – 1791V → G in AAA81026 (Ref. 4) Curated
Sequence conflicti184 – 1841A → T in AAA81026 (Ref. 4) Curated
Sequence conflicti267 – 2671T → A in AAA81026 (Ref. 4) Curated
Sequence conflicti598 – 5992ES → DA in M28242 (PubMed:2404948).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75276.1.
AP009048 Genomic DNA. Translation: BAA15999.1.
U38659 Genomic DNA. Translation: AAA81025.1. Frameshift.
U38659 Genomic DNA. Translation: AAA81026.1. Frameshift.
U38659 Genomic DNA. Translation: AAA81027.1. Frameshift.
M28242 Genomic DNA. No translation available.
PIRiF64991.
RefSeqiNP_416720.1. NC_000913.3.
WP_001249081.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75276; AAC75276; b2216.
BAA15999; BAA15999; BAA15999.
GeneIDi946717.
KEGGiecj:JW2204.
eco:b2216.
PATRICi32119791. VBIEscCol129921_2305.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75276.1.
AP009048 Genomic DNA. Translation: BAA15999.1.
U38659 Genomic DNA. Translation: AAA81025.1. Frameshift.
U38659 Genomic DNA. Translation: AAA81026.1. Frameshift.
U38659 Genomic DNA. Translation: AAA81027.1. Frameshift.
M28242 Genomic DNA. No translation available.
PIRiF64991.
RefSeqiNP_416720.1. NC_000913.3.
WP_001249081.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SR2NMR-A775-890[»]
2KX7NMR-A688-795[»]
ProteinModelPortaliP39838.
SMRiP39838. Positions 688-890.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-12815N.
IntActiP39838. 4 interactions.
MINTiMINT-1304951.
STRINGi511145.b2216.

PTM databases

iPTMnetiP39838.

Proteomic databases

PaxDbiP39838.
PRIDEiP39838.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75276; AAC75276; b2216.
BAA15999; BAA15999; BAA15999.
GeneIDi946717.
KEGGiecj:JW2204.
eco:b2216.
PATRICi32119791. VBIEscCol129921_2305.

Organism-specific databases

EchoBASEiEB2286.
EcoGeneiEG12385. rcsD.

Phylogenomic databases

eggNOGiENOG4105E3G. Bacteria.
COG2198. LUCA.
HOGENOMiHOG000122289.
KOiK07676.
OMAiTWRYATW.

Enzyme and pathway databases

BioCyciEcoCyc:EG12385-MONOMER.
ECOL316407:JW2204-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP39838.
PROiP39838.

Family and domain databases

Gene3Di1.20.120.160. 1 hit.
3.30.565.10. 1 hit.
HAMAPiMF_00980. RcsD. 1 hit.
InterProiIPR003594. HATPase_C.
IPR005467. His_kinase_dom.
IPR030861. Ptransferase_RcsD.
IPR032306. RcsD_ABL.
IPR008207. Sig_transdc_His_kin_Hpt_dom.
[Graphical view]
PfamiPF02518. HATPase_c. 1 hit.
PF01627. Hpt. 1 hit.
PF16359. RcsD_ABL. 1 hit.
[Graphical view]
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF47226. SSF47226. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiPS50109. HIS_KIN. 1 hit.
PS50894. HPT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRCSD_ECOLI
AccessioniPrimary (citable) accession number: P39838
Secondary accession number(s): P47725, P47726, P76456
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 1, 1997
Last modified: September 7, 2016
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Contains a histidine kinase domain, but it seems to be non-functional as the highly conserved histidine residue is missing.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.