MCSA_BACSU
ID MCSA_BACSU Reviewed; 185 AA.
AC P37569;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Protein-arginine kinase activator protein;
GN Name=mcsA; Synonyms=yacH; OrderedLocusNames=BSU00840;
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 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 [4]
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 [5]
RP FUNCTION, AND INTERACTION WITH MCSB.
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION AT ARG-169.
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION AT ARG-115.
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).
CC -!- FUNCTION: Activates the phosphorylation activity of the protein-
CC arginine kinase McsB. Is required for the delocalization of competence
CC proteins from the cell poles. {ECO:0000269|PubMed:16163393,
CC ECO:0000269|PubMed:19226326}.
CC -!- SUBUNIT: Interacts with McsB. {ECO:0000269|PubMed:16163393}.
CC -!- INDUCTION: Is repressed by the transcriptional regulator CtsR. Forms
CC part of an operon with ctsR, mcsB and clpC.
CC {ECO:0000269|PubMed:9987115}.
CC -!- PTM: Phosphorylated on Arg residues by McsB.
CC {ECO:0000269|PubMed:22517742, ECO:0000269|PubMed:24263382}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a defect in the
CC delocalization of competence proteins. {ECO:0000269|PubMed:19226326}.
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DR EMBL; D26185; BAA05318.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11860.1; -; Genomic_DNA.
DR PIR; S66113; S66113.
DR RefSeq; NP_387965.1; NC_000964.3.
DR RefSeq; WP_009966297.1; NZ_JNCM01000029.1.
DR AlphaFoldDB; P37569; -.
DR SMR; P37569; -.
DR STRING; 224308.BSU00840; -.
DR iPTMnet; P37569; -.
DR PaxDb; P37569; -.
DR PRIDE; P37569; -.
DR EnsemblBacteria; CAB11860; CAB11860; BSU_00840.
DR GeneID; 936845; -.
DR KEGG; bsu:BSU00840; -.
DR PATRIC; fig|224308.179.peg.85; -.
DR eggNOG; COG3880; Bacteria.
DR InParanoid; P37569; -.
DR OMA; CGKRPAT; -.
DR PhylomeDB; P37569; -.
DR BioCyc; BSUB:BSU00840-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0046870; F:cadmium ion binding; IBA:GO_Central.
DR GO; GO:0050897; F:cobalt ion binding; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IMP:CACAO.
DR GO; GO:1990170; P:stress response to cadmium ion; IBA:GO_Central.
DR GO; GO:1990169; P:stress response to copper ion; IBA:GO_Central.
DR InterPro; IPR001943; UVR_dom.
DR InterPro; IPR036876; UVR_dom_sf.
DR InterPro; IPR025542; YacH.
DR PANTHER; PTHR38430; PTHR38430; 1.
DR Pfam; PF02151; UVR; 1.
DR PIRSF; PIRSF015034; YacH; 1.
DR SUPFAM; SSF46600; SSF46600; 1.
DR PROSITE; PS50151; UVR; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..185
FT /note="Protein-arginine kinase activator protein"
FT /id="PRO_0000049449"
FT DOMAIN 139..174
FT /note="UVR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00217"
FT MOD_RES 115
FT /note="Phosphoarginine"
FT /evidence="ECO:0000269|PubMed:24263382"
FT MOD_RES 169
FT /note="Phosphoarginine"
FT /evidence="ECO:0000269|PubMed:22517742"
SQ SEQUENCE 185 AA; 21023 MW; A6388713A1A6ADBB CRC64;
MICQECHERP ATFHFTKVVN GEKIEVHICE QCAKENSDSY GISANQGFSI HNLLSGLLNM
DSSFQNAGTQ MFSHSEQISA CPKCGMTFQQ FRKIGRFGCS ECYKTFHSNI TPILRKVHSG
NTVHAGKIPK RIGGNLHVRR QIDMLKKELE SLIHQEEFEN AAHVRDQIRL LEQSLKSTDS
EEEQE
