ID   MCSA_STAA8              Reviewed;         188 AA.
AC   Q2G0P7;
DT   24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 2.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Protein-arginine kinase activator protein {ECO:0000250|UniProtKB:P37569};
GN   Name=mcsA {ECO:0000303|PubMed:22126623};
GN   OrderedLocusNames=SAOUHSC_00503 {ECO:0000312|EMBL:ABD29652.1};
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [2]
RP   FUNCTION, INDUCTION, INTERACTION WITH MCSB AND CTSR, AND MUTAGENESIS.
RC   STRAIN=SH1000;
RX   PubMed=22126623; DOI=10.1111/j.1574-6968.2011.02468.x;
RA   Sitthisak S., Kitti T., Boonyonying K., Wozniak D., Mongkolsuk S.,
RA   Jayaswal R.K.;
RT   "McsA and the roles of metal-binding motif in Staphylococcus aureus.";
RL   FEMS Microbiol. Lett. 327:126-133(2012).
CC   -!- FUNCTION: Activates the phosphorylation activity of the protein-
CC       arginine kinase McsB (By similarity). May function as an important
CC       molecule for oxidative tolerance in various types of stress including
CC       that of heavy metals. Binds to Cu(2+), Zn(2+), Co(2+) and Cd(2+) via
CC       its CXXC metal binding motifs (PubMed:22126623).
CC       {ECO:0000250|UniProtKB:P37569, ECO:0000269|PubMed:22126623}.
CC   -!- SUBUNIT: Interacts with McsB and CtsR; the CXXC motifs are needed for
CC       the binding. {ECO:0000269|PubMed:22126623}.
CC   -!- INDUCTION: Up-regulated by heavy metals such as Cu(2+) and Cd(2+), but
CC       Zn(2+) and Co(2+) have no effect. Forms part of an operon with ctsR,
CC       mcsB and clpC, which is repressed by CtsR.
CC       {ECO:0000269|PubMed:22126623}.
CC   -!- MISCELLANEOUS: The mutant where Cys residues of three CXXC motifs are
CC       mutated to Ala (Cys-3, Cys-6, Cys-29, Cys-32, Cys-105 and Cys-108) is
CC       still able to bind Cu(2+), probably via its fourth CXXC motif, but
CC       loses the ability to bind Zn(2+), Co(2+) and Cd(2+).
CC       {ECO:0000269|PubMed:22126623}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABD29652.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000253; ABD29652.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000882069.1; NZ_LS483365.1.
DR   RefSeq; YP_499076.1; NC_007795.1.
DR   AlphaFoldDB; Q2G0P7; -.
DR   SMR; Q2G0P7; -.
DR   STRING; 1280.SAXN108_0576; -.
DR   EnsemblBacteria; ABD29652; ABD29652; SAOUHSC_00503.
DR   GeneID; 3920415; -.
DR   KEGG; sao:SAOUHSC_00503; -.
DR   PATRIC; fig|93061.5.peg.450; -.
DR   eggNOG; COG3880; Bacteria.
DR   HOGENOM; CLU_102553_0_0_9; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0046870; F:cadmium ion binding; IDA:UniProtKB.
DR   GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB.
DR   GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:1990170; P:stress response to cadmium ion; IDA:UniProtKB.
DR   GO; GO:1990169; P:stress response to copper ion; IDA:UniProtKB.
DR   InterPro; IPR001943; UVR_dom.
DR   InterPro; IPR025542; YacH.
DR   InterPro; IPR001510; Znf_PARP.
DR   PANTHER; PTHR38430; PTHR38430; 1.
DR   Pfam; PF02151; UVR; 1.
DR   PIRSF; PIRSF015034; YacH; 1.
DR   PROSITE; PS50064; PARP_ZN_FINGER_2; 1.
DR   PROSITE; PS50151; UVR; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Reference proteome; Stress response; Zinc; Zinc-finger.
FT   CHAIN           1..188
FT                   /note="Protein-arginine kinase activator protein"
FT                   /id="PRO_0000433303"
FT   DOMAIN          145..180
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00217"
FT   ZN_FING         96..166
FT                   /note="PARP-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT   MOTIF           3..6
FT                   /note="CXXC metal binding motif 1"
FT                   /evidence="ECO:0000305|PubMed:22126623"
FT   MOTIF           29..32
FT                   /note="CXXC metal binding motif 2"
FT                   /evidence="ECO:0000305|PubMed:22126623"
FT   MOTIF           87..90
FT                   /note="CXXC metal binding motif 3"
FT                   /evidence="ECO:0000305|PubMed:22126623"
FT   MOTIF           105..108
FT                   /note="CXXC metal binding motif 4"
FT                   /evidence="ECO:0000305|PubMed:22126623"
SQ   SEQUENCE   188 AA;  21703 MW;  4A557AA77C01B306 CRC64;
     MLCENCQLNE AELKVKVTSK NKTEEKMVCQ TCAEGHHPWN QANEQPEYQE HQDNFEEAFV
     VKQILQHLAT KHGINFQEVA FKEEKRCPSC HMTLKDIAHV GKFGCANCYA TFKDDIIDIV
     RRVQGGQFEH VGKTPHSSHK KIALKRKIEE KNEYLKKLIE IQDFEEAAIV RDEIKALKAE
     SEVQHDDA