MCSB_BACSU
ID MCSB_BACSU Reviewed; 363 AA.
AC P37570;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Protein-arginine kinase {ECO:0000255|HAMAP-Rule:MF_00602};
DE EC=2.7.14.1 {ECO:0000255|HAMAP-Rule:MF_00602, ECO:0000305|PubMed:30962626};
GN Name=mcsB {ECO:0000255|HAMAP-Rule:MF_00602}; Synonyms=yacI;
GN OrderedLocusNames=BSU00850;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 253-363.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8016066; DOI=10.1073/pnas.91.13.5788;
RA Msadek T., Kunst F., Rapoport G.;
RT "MecB of Bacillus subtilis, a member of the ClpC ATPase family, is a
RT pleiotropic regulator controlling competence gene expression and growth at
RT high temperature.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:5788-5792(1994).
RN [4]
RP REPRESSION BY CTSR.
RX PubMed=9987115; DOI=10.1046/j.1365-2958.1999.01152.x;
RA Derre I., Rapoport G., Msadek T.;
RT "CtsR, a novel regulator of stress and heat shock response, controls clp
RT and molecular chaperone gene expression in gram-positive bacteria.";
RL Mol. Microbiol. 31:117-131(1999).
RN [5]
RP GENE NAME.
RC STRAIN=168 / IS58;
RX PubMed=11179229; DOI=10.1093/emboj/20.4.852;
RA Kruger E., Zuhlke D., Witt E., Ludwig H., Hecker M.;
RT "Clp-mediated proteolysis in Gram-positive bacteria is autoregulated by the
RT stability of a repressor.";
RL EMBO J. 20:852-863(2001).
RN [6]
RP ACTIVITY REGULATION, AND INTERACTION WITH MCSA AND CTSR.
RC STRAIN=168;
RX PubMed=16163393; DOI=10.1038/sj.emboj.7600780;
RA Kirstein J., Zuhlke D., Gerth U., Turgay K., Hecker M.;
RT "A tyrosine kinase and its activator control the activity of the CtsR heat
RT shock repressor in B. subtilis.";
RL EMBO J. 24:3435-3445(2005).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=168 / BD630;
RX PubMed=19226326; DOI=10.1111/j.1365-2958.2009.06636.x;
RA Hahn J., Kramer N., Briley K. Jr., Dubnau D.;
RT "McsA and B mediate the delocalization of competence proteins from the cell
RT poles of Bacillus subtilis.";
RL Mol. Microbiol. 72:202-215(2009).
RN [8]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH CLPC AND MCSA, AND
RP PHOSPHORYLATION AT ARG-29; ARG-190; ARG-255; ARG-269 AND ARG-272.
RC STRAIN=168;
RX PubMed=21622759; DOI=10.1128/jb.00079-11;
RA Elsholz A.K., Hempel K., Michalik S., Gronau K., Becher D., Hecker M.,
RA Gerth U.;
RT "Activity control of the ClpC adaptor McsB in Bacillus subtilis.";
RL J. Bacteriol. 193:3887-3893(2011).
RN [9]
RP FUNCTION AS AN ARGININE KINASE, IDENTIFICATION OF SUBSTRATES, AND ACTIVITY
RP REGULATION.
RC STRAIN=168;
RX PubMed=22517742; DOI=10.1073/pnas.1117483109;
RA Elsholz A.K., Turgay K., Michalik S., Hessling B., Gronau K., Oertel D.,
RA Mader U., Bernhardt J., Becher D., Hecker M., Gerth U.;
RT "Global impact of protein arginine phosphorylation on the physiology of
RT Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:7451-7456(2012).
RN [10]
RP FUNCTION, IDENTIFICATION OF SUBSTRATES, ACTIVITY REGULATION, AND
RP PHOSPHORYLATION AT ARG-40; ARG-86; ARG-255 AND ARG-346.
RC STRAIN=168;
RX PubMed=24263382; DOI=10.1074/mcp.m113.032292;
RA Schmidt A., Trentini D.B., Spiess S., Fuhrmann J., Ammerer G., Mechtler K.,
RA Clausen T.;
RT "Quantitative phosphoproteomics reveals the role of protein arginine
RT phosphorylation in the bacterial stress response.";
RL Mol. Cell. Proteomics 13:537-550(2014).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-121; TYR-210 AND
RP ARG-272.
RC STRAIN=168;
RX PubMed=30962626; DOI=10.1038/s41589-019-0265-y;
RA Suskiewicz M.J., Hajdusits B., Beveridge R., Heuck A., Vu L.D.,
RA Kurzbauer R., Hauer K., Thoeny V., Rumpel K., Mechtler K., Meinhart A.,
RA Clausen T.;
RT "Structure of McsB, a protein kinase for regulated arginine
RT phosphorylation.";
RL Nat. Chem. Biol. 15:510-518(2019).
CC -!- FUNCTION: Catalyzes the specific phosphorylation of arginine residues
CC in a large number of proteins. Is part of the bacterial stress response
CC system, where it is involved in regulating the global heat shock
CC repressor CtsR; phosphorylates arginine residues in the winged helix-
CC turn-helix domain of CtsR, thereby preventing its binding to DNA and
CC consequently inducing the expression of repressed genes. The
CC transcriptional repressor HrcA, the chaperone GroEL, the unfoldase
CC ClpC, together with several ribosomal subunits, represent other
CC physiological targets of McsB under stress conditions. Protein arginine
CC phosphorylation has a physiologically important role and is involved in
CC the regulation of many critical cellular processes, such as protein
CC homeostasis, motility, competence, and stringent and stress responses,
CC by regulating gene expression and protein activity. Functions as an
CC adapter whose kinase activity is required for ClpCP-mediated
CC degradation of CtsR during heat stress. Is required for the
CC delocalization of competence proteins from the cell poles, probably via
CC a role in the degradation of anchor proteins.
CC {ECO:0000269|PubMed:19226326, ECO:0000269|PubMed:21622759,
CC ECO:0000269|PubMed:22517742, ECO:0000269|PubMed:24263382,
CC ECO:0000269|PubMed:30962626}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-phospho-L-
CC arginyl-[protein]; Xref=Rhea:RHEA:43384, Rhea:RHEA-COMP:10532,
CC Rhea:RHEA-COMP:10533, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83226, ChEBI:CHEBI:456216;
CC EC=2.7.14.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00602,
CC ECO:0000305|PubMed:30962626};
CC -!- ACTIVITY REGULATION: Appears to be allosterically activated by the
CC binding of pArg-containing polypeptides to the pArg-binding pocket
CC localized in the C-terminal domain of McsB (By similarity). The McsB
CC kinase is inhibited in nonstressed cells by direct interaction with
CC ClpC; upon heat exposure, the interaction of McsB with ClpC is
CC dramatically decreased, leading to McsB release and activation during
CC heat stress. Its kinase activity is counteracted by the protein-
CC arginine-phosphatase YwlE in vivo. Requires McsA for full kinase
CC activity. {ECO:0000255|HAMAP-Rule:MF_00602,
CC ECO:0000269|PubMed:16163393, ECO:0000269|PubMed:21622759,
CC ECO:0000269|PubMed:22517742, ECO:0000269|PubMed:24263382}.
CC -!- SUBUNIT: Interacts with CtsR in its autophosphorylated form. Interacts
CC with McsA in nonstressed as well as in heat-stressed cells, whereas
CC strongly interacts with ClpC only in nonstressed cells.
CC {ECO:0000269|PubMed:16163393, ECO:0000269|PubMed:21622759}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Note=Localizes to the
CC cell poles in competent cells, but not in non-competent cells.
CC {ECO:0000269|PubMed:19226326}.
CC -!- INDUCTION: Is repressed by the transcriptional regulator CtsR. Forms
CC part of an operon with ctsR, mcsA and clpC.
CC {ECO:0000269|PubMed:9987115}.
CC -!- PTM: Autophosphorylated on Arg residues. Phosphorylation on Arg-40 and
CC Arg-86 are up-regulated upon stress conditions.
CC {ECO:0000269|PubMed:21622759, ECO:0000269|PubMed:24263382}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a defect in the
CC delocalization of competence proteins that is not related to altered
CC expression of the com genes on the levels of either transcription or
CC translation. Inactivation of mcsB also decreases transformability
CC (PubMed:19226326). CtsR is no more degraded (PubMed:30962626).
CC {ECO:0000269|PubMed:19226326, ECO:0000269|PubMed:30962626}.
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_00602}.
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DR EMBL; D26185; BAA05319.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11861.1; -; Genomic_DNA.
DR EMBL; U02604; AAA19232.1; -; Unassigned_DNA.
DR PIR; S66114; S66114.
DR RefSeq; NP_387966.1; NC_000964.3.
DR RefSeq; WP_003235007.1; NZ_JNCM01000029.1.
DR PDB; 6TV6; X-ray; 2.50 A; A/B/C/D=1-363.
DR PDBsum; 6TV6; -.
DR AlphaFoldDB; P37570; -.
DR SMR; P37570; -.
DR IntAct; P37570; 1.
DR MINT; P37570; -.
DR STRING; 224308.BSU00850; -.
DR iPTMnet; P37570; -.
DR jPOST; P37570; -.
DR PaxDb; P37570; -.
DR PRIDE; P37570; -.
DR EnsemblBacteria; CAB11861; CAB11861; BSU_00850.
DR GeneID; 936939; -.
DR KEGG; bsu:BSU00850; -.
DR PATRIC; fig|224308.179.peg.86; -.
DR eggNOG; COG3869; Bacteria.
DR InParanoid; P37570; -.
DR OMA; IIMQERV; -.
DR PhylomeDB; P37570; -.
DR BioCyc; BSUB:BSU00850-MON; -.
DR BRENDA; 2.7.14.1; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004111; F:creatine kinase activity; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd07930; bacterial_phosphagen_kinase; 1.
DR HAMAP; MF_00602; Prot_Arg_kinase; 1.
DR InterPro; IPR023660; Arg_Kinase.
DR InterPro; IPR000749; ATP-guanido_PTrfase.
DR InterPro; IPR022415; ATP-guanido_PTrfase_AS.
DR InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR PANTHER; PTHR11547; PTHR11547; 1.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..363
FT /note="Protein-arginine kinase"
FT /id="PRO_0000212017"
FT DOMAIN 24..254
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT MOTIF 337..342
FT /note="RDXXRA motif of the pArg binding pocket involved in
FT allosteric regulation"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT BINDING 27..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT BINDING 125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT BINDING 176..180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT BINDING 207..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT MOD_RES 29
FT /note="Phosphoarginine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:21622759"
FT MOD_RES 40
FT /note="Phosphoarginine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:24263382"
FT MOD_RES 86
FT /note="Phosphoarginine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:24263382"
FT MOD_RES 190
FT /note="Phosphoarginine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:21622759"
FT MOD_RES 255
FT /note="Phosphoarginine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:21622759,
FT ECO:0000269|PubMed:24263382"
FT MOD_RES 269
FT /note="Phosphoarginine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:21622759"
FT MOD_RES 272
FT /note="Phosphoarginine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:21622759"
FT MOD_RES 346
FT /note="Phosphoarginine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:24263382"
FT MUTAGEN 121
FT /note="E->A: Stabilizes quantity of CtsR to an extent
FT comparable to that observed for the mcsB deletion,
FT indicating a loss of protein phosphorylation activity of
FT McsB in vivo."
FT /evidence="ECO:0000269|PubMed:30962626"
FT MUTAGEN 210
FT /note="Y->A: Stabilizes quantity of CtsR to an extent a
FT little lower to that observed for the mcsB deletion,
FT indicating a decrease of protein phosphorylation activity
FT of McsB in vivo."
FT /evidence="ECO:0000269|PubMed:30962626"
FT MUTAGEN 272
FT /note="R->A: Stabilizes quantity of CtsR to an extent a
FT little lower to that observed for the mcsB deletion,
FT indicating a decrease of protein phosphorylation activity
FT of McsB in vivo."
FT /evidence="ECO:0000269|PubMed:30962626"
FT HELIX 1..8
FT /evidence="ECO:0007829|PDB:6TV6"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:6TV6"
FT TURN 20..24
FT /evidence="ECO:0007829|PDB:6TV6"
FT STRAND 25..34
FT /evidence="ECO:0007829|PDB:6TV6"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:6TV6"
FT HELIX 47..60
FT /evidence="ECO:0007829|PDB:6TV6"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:6TV6"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:6TV6"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:6TV6"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:6TV6"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:6TV6"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:6TV6"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:6TV6"
FT STRAND 112..133
FT /evidence="ECO:0007829|PDB:6TV6"
FT HELIX 135..150
FT /evidence="ECO:0007829|PDB:6TV6"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:6TV6"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:6TV6"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:6TV6"
FT HELIX 184..188
FT /evidence="ECO:0007829|PDB:6TV6"
FT HELIX 196..201
FT /evidence="ECO:0007829|PDB:6TV6"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:6TV6"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:6TV6"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:6TV6"
FT HELIX 233..261
FT /evidence="ECO:0007829|PDB:6TV6"
FT HELIX 263..279
FT /evidence="ECO:0007829|PDB:6TV6"
FT HELIX 285..300
FT /evidence="ECO:0007829|PDB:6TV6"
FT HELIX 309..318
FT /evidence="ECO:0007829|PDB:6TV6"
FT HELIX 321..328
FT /evidence="ECO:0007829|PDB:6TV6"
FT HELIX 334..362
FT /evidence="ECO:0007829|PDB:6TV6"
SQ SEQUENCE 363 AA; 41124 MW; 923E4A6445A752EF CRC64;
MSLKHFIQDA LSSWMKQKGP ESDIVLSSRI RLARNFEHIR FPTRYSNEEA SSIIQQFEDQ
FSEQEIPGIG KFVLIRMNDA QPLEKRVLVE KHLISPNLTE SPFGGCLLSE NEEVSVMLNE
EDHIRIQCLF PGFQLLEAMK AANQVDDWIE EKVDYAFNEQ RGYLTSCPTN VGTGLRASVM
MHLPALVLTR QINRIIPAIN QLGLVVRGIY GEGSEAVGNI FQISNQITLG KSEQDIVEDL
NSVAAQLIEQ ERSAREAIYQ TSKIELEDRV YRSYGVLSNC RMIESKETAK CLSDVRLGID
LGIIKGLSSN ILNELMILTQ PGFLQQYSGG ALRPNERDIR RAALIRERLH LEMNGKRQED
ESI
