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Protein

Protein-arginine kinase

Gene

mcsB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the specific phosphorylation of arginine residues in a large number of proteins. Is part of the bacterial stress response system, where it is involved in regulating the global heat shock repressor CtsR; phosphorylates arginine residues in the winged helix-turn-helix domain of CtsR, thereby preventing its binding to DNA and consequently inducing the expression of repressed genes. The transcriptional repressor HrcA, the chaperone GroEL, the unfoldase ClpC, together with several ribosomal subunits, represent other physiological targets of McsB under stress conditions. Protein arginine phosphorylation has a physiologically important role and is involved in the regulation of many critical cellular processes, such as protein homeostasis, motility, competence, and stringent and stress responses, by regulating gene expression and protein activity. Functions as an adapter whose kinase activity is required for ClpCP-mediated degradation of CtsR during heat stress. Is required for the delocalization of competence proteins from the cell poles, probably via a role in the degradation of anchor proteins.4 Publications

Catalytic activityi

ATP + a [protein]-L-arginine = ADP + a [protein]-N(omega)-phospho-L-arginine.UniRule annotation

Enzyme regulationi

The McsB kinase is inhibited in nonstressed cells by direct interaction with ClpC; upon heat exposure, the interaction of McsB with ClpC is dramatically decreased, leading to McsB release and activation during heat stress. Its kinase activity is counteracted by the protein-arginine-phosphatase YwlE in vivo. Requires McsA for full kinase activity.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei92ATPUniRule annotation1
Binding sitei125ATPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi27 – 31ATPUniRule annotation5
Nucleotide bindingi176 – 180ATPUniRule annotation5
Nucleotide bindingi207 – 212ATPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU00850-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-arginine kinaseUniRule annotation (EC:2.7.14.1UniRule annotation)
Gene namesi
Name:mcsBUniRule annotation
Synonyms:yacI
Ordered Locus Names:BSU00850
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm Curated

  • Note: Localizes to the cell poles in competent cells, but not in non-competent cells.1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene show a defect in the delocalization of competence proteins that is not related to altered expression of the com genes on the levels of either transcription or translation. Inactivation of mcsB also decreases transformability.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002120171 – 363Protein-arginine kinaseAdd BLAST363

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei29Phosphoarginine; by autocatalysis1 Publication1
Modified residuei40Phosphoarginine; by autocatalysis1 Publication1
Modified residuei86Phosphoarginine; by autocatalysis1 Publication1
Modified residuei190Phosphoarginine; by autocatalysis1 Publication1
Modified residuei255Phosphoarginine; by autocatalysis2 Publications1
Modified residuei269Phosphoarginine; by autocatalysis1 Publication1
Modified residuei272Phosphoarginine; by autocatalysis1 Publication1
Modified residuei346Phosphoarginine; by autocatalysis1 Publication1

Post-translational modificationi

Autophosphorylated on Arg residues. Phosphorylation on Arg-40 and Arg-86 are up-regulated upon stress conditions.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP37570.
PRIDEiP37570.

Expressioni

Inductioni

Is repressed by the transcriptional regulator CtsR. Forms part of an operon with ctsR, mcsA and clpC.1 Publication

Interactioni

Subunit structurei

Interacts with CtsR in its autophosphorylated form. Interacts with McsA in nonstressed as well as in heat-stressed cells, whereas strongly interacts with ClpC only in nonstressed cells.2 Publications

Protein-protein interaction databases

IntActiP37570. 1 interactor.
MINTiMINT-4789055.
STRINGi224308.Bsubs1_010100000440.

Structurei

3D structure databases

ProteinModelPortaliP37570.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 254Phosphagen kinase C-terminalUniRule annotationAdd BLAST231

Sequence similaritiesi

Belongs to the ATP:guanido phosphotransferase family.UniRule annotation
Contains 1 phosphagen kinase C-terminal domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG41066A3. Bacteria.
COG3869. LUCA.
HOGENOMiHOG000082112.
InParanoidiP37570.
KOiK19405.
OMAiIIMQERV.
PhylomeDBiP37570.

Family and domain databases

CDDicd07930. bacterial_phosphagen_kinase. 1 hit.
Gene3Di3.30.590.10. 1 hit.
HAMAPiMF_00602. Prot_Arg_kinase. 1 hit.
InterProiIPR023660. Arg_Kinase.
IPR000749. ATP-guanido_PTrfase.
IPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
PANTHERiPTHR11547. PTHR11547. 2 hits.
PfamiPF00217. ATP-gua_Ptrans. 1 hit.
[Graphical view]
PROSITEiPS00112. PHOSPHAGEN_KINASE. 1 hit.
PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P37570-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLKHFIQDA LSSWMKQKGP ESDIVLSSRI RLARNFEHIR FPTRYSNEEA
60 70 80 90 100
SSIIQQFEDQ FSEQEIPGIG KFVLIRMNDA QPLEKRVLVE KHLISPNLTE
110 120 130 140 150
SPFGGCLLSE NEEVSVMLNE EDHIRIQCLF PGFQLLEAMK AANQVDDWIE
160 170 180 190 200
EKVDYAFNEQ RGYLTSCPTN VGTGLRASVM MHLPALVLTR QINRIIPAIN
210 220 230 240 250
QLGLVVRGIY GEGSEAVGNI FQISNQITLG KSEQDIVEDL NSVAAQLIEQ
260 270 280 290 300
ERSAREAIYQ TSKIELEDRV YRSYGVLSNC RMIESKETAK CLSDVRLGID
310 320 330 340 350
LGIIKGLSSN ILNELMILTQ PGFLQQYSGG ALRPNERDIR RAALIRERLH
360
LEMNGKRQED ESI
Length:363
Mass (Da):41,124
Last modified:October 1, 1994 - v1
Checksum:i923E4A6445A752EF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26185 Genomic DNA. Translation: BAA05319.1.
AL009126 Genomic DNA. Translation: CAB11861.1.
U02604 Unassigned DNA. Translation: AAA19232.1.
PIRiS66114.
RefSeqiNP_387966.1. NC_000964.3.
WP_003235007.1. NZ_JNCM01000029.1.

Genome annotation databases

EnsemblBacteriaiCAB11861; CAB11861; BSU00850.
GeneIDi936939.
KEGGibsu:BSU00850.
PATRICi18971675. VBIBacSub10457_0086.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26185 Genomic DNA. Translation: BAA05319.1.
AL009126 Genomic DNA. Translation: CAB11861.1.
U02604 Unassigned DNA. Translation: AAA19232.1.
PIRiS66114.
RefSeqiNP_387966.1. NC_000964.3.
WP_003235007.1. NZ_JNCM01000029.1.

3D structure databases

ProteinModelPortaliP37570.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP37570. 1 interactor.
MINTiMINT-4789055.
STRINGi224308.Bsubs1_010100000440.

Proteomic databases

PaxDbiP37570.
PRIDEiP37570.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB11861; CAB11861; BSU00850.
GeneIDi936939.
KEGGibsu:BSU00850.
PATRICi18971675. VBIBacSub10457_0086.

Phylogenomic databases

eggNOGiENOG41066A3. Bacteria.
COG3869. LUCA.
HOGENOMiHOG000082112.
InParanoidiP37570.
KOiK19405.
OMAiIIMQERV.
PhylomeDBiP37570.

Enzyme and pathway databases

BioCyciBSUB:BSU00850-MONOMER.

Family and domain databases

CDDicd07930. bacterial_phosphagen_kinase. 1 hit.
Gene3Di3.30.590.10. 1 hit.
HAMAPiMF_00602. Prot_Arg_kinase. 1 hit.
InterProiIPR023660. Arg_Kinase.
IPR000749. ATP-guanido_PTrfase.
IPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
PANTHERiPTHR11547. PTHR11547. 2 hits.
PfamiPF00217. ATP-gua_Ptrans. 1 hit.
[Graphical view]
PROSITEiPS00112. PHOSPHAGEN_KINASE. 1 hit.
PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMCSB_BACSU
AccessioniPrimary (citable) accession number: P37570
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: November 2, 2016
This is version 114 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

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  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.