(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 114.
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}.
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   STRING; 224308.BSU00840; -.
DR   iPTMnet; P37569; -.
DR   PaxDb; P37569; -.
DR   PRIDE; P37569; -.
DR   EnsemblBacteria; CAB11860; CAB11860; BSU00840.
DR   GeneID; 936845; -.
DR   KEGG; bsu:BSU00840; -.
DR   PATRIC; fig|224308.179.peg.85; -.
DR   eggNOG; ENOG4108Z0C; Bacteria.
DR   eggNOG; COG3880; LUCA.
DR   HOGENOM; HOG000218089; -.
DR   InParanoid; P37569; -.
DR   KO; K19411; -.
DR   OMA; CGKRPAT; -.
DR   PhylomeDB; P37569; -.
DR   BioCyc; BSUB:BSU00840-MONOMER; -.
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: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;
DR   PRODOM; P37569.
DR   SWISS-2DPAGE; P37569.
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
//

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