(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 130.
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 / 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}.
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   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; BSU00850.
DR   GeneID; 936939; -.
DR   KEGG; bsu:BSU00850; -.
DR   PATRIC; fig|224308.179.peg.86; -.
DR   eggNOG; ENOG41066A3; Bacteria.
DR   eggNOG; COG3869; LUCA.
DR   HOGENOM; HOG000082112; -.
DR   InParanoid; P37570; -.
DR   KO; K19405; -.
DR   OMA; ACPTNVG; -.
DR   PhylomeDB; P37570; -.
DR   BioCyc; BSUB:BSU00850-MONOMER; -.
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   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;
DR   PRODOM; P37570.
DR   SWISS-2DPAGE; P37570.
KW   Allosteric enzyme; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   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   NP_BIND         27..31
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   NP_BIND         176..180
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   NP_BIND         207..212
FT                   /note="ATP"
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         92
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT   BINDING         125
FT                   /note="ATP"
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"
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
//

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