MCSB_GEOSE
ID MCSB_GEOSE Reviewed; 363 AA.
AC P0DMM5;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Protein-arginine kinase {ECO:0000255|HAMAP-Rule:MF_00602};
DE EC=2.7.14.1 {ECO:0000269|PubMed:19498169, ECO:0000269|PubMed:30962626};
GN Name=mcsB {ECO:0000303|PubMed:19498169, ECO:0000303|PubMed:30962626};
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 12980 / DSM 22 / CCM 2062 / JCM 2501 / NBRC 12550 / NCIMB 8923
RC / NCTC 10339 / R-35646 / VKM B-510;
RA Fuhrmann J.;
RL Submitted (MAY-2014) to UniProtKB.
RN [2]
RP FUNCTION AS AN ARGININE KINASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP AND MUTAGENESIS OF GLU-122 AND GLU-213.
RC STRAIN=ATCC 12980 / DSM 22 / CCM 2062 / JCM 2501 / NBRC 12550 / NCIMB 8923
RC / NCTC 10339 / R-35646 / VKM B-510;
RX PubMed=19498169; DOI=10.1126/science.1170088;
RA Fuhrmann J., Schmidt A., Spiess S., Lehner A., Turgay K., Mechtler K.,
RA Charpentier E., Clausen T.;
RT "McsB is a protein arginine kinase that phosphorylates and inhibits the
RT heat-shock regulator CtsR.";
RL Science 324:1323-1327(2009).
RN [3] {ECO:0007744|PDB:6FH1, ECO:0007744|PDB:6FH2, ECO:0007744|PDB:6FH3}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-355 OF APOENZYME AND IN
RP COMPLEXES WITH ATP ANALOG AND PHOSPHOARGININE, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, DOMAIN, SUBUNIT, AND MUTAGENESIS OF HIS-92;
RP GLU-122; CYS-168; ARG-208; TYR-211; GLU-213; ARG-273 AND ARG-282.
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. Protein
CC arginine phosphorylation has a physiologically important role and is
CC involved in the regulation of many critical cellular processes, such as
CC protein homeostasis, motility, competence, and stringent and stress
CC responses, by regulating gene expression and protein activity. Acts
CC exclusively on Arg residues, since it cannot phosphorylate Tyr, Ser,
CC Thr, His, Asp and Lys. Has no free arginine kinase activity.
CC {ECO:0000269|PubMed:19498169, 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:0000269|PubMed:19498169,
CC ECO:0000269|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.
CC {ECO:0000269|PubMed:30962626}.
CC -!- SUBUNIT: Homodimer. Dimerization is important for full catalytic
CC activity. {ECO:0000269|PubMed:30962626}.
CC -!- DOMAIN: In the 3D-structure the McsB dimer adopts a flat 'domino tile'
CC shape, with the two active sites opening on the same side. Individual
CC subunits are composed of the N-terminal catalytic, ATP:guanido
CC phosphotransferase domain (PD, residues 1-263) and the C-terminal
CC dimerization domain (DD, residues 264-355), which are linearly
CC organized in a PD-DD-DD*-PD* manner (asterisk denotes the partner
CC protomer). The PhK-like catalytic phosphotransferase domain is
CC structurally adapted to target protein substrates. The C-terminal DD of
CC McsB contains a pArg-binding pocket that allows pArg-carrying proteins
CC to allosterically enhance McsB kinase activity.
CC {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 RefSeq; WP_033017267.1; NZ_RCTK01000011.1.
DR PDB; 6FH1; X-ray; 1.70 A; A/B=1-355.
DR PDB; 6FH2; X-ray; 2.70 A; A/B=1-355.
DR PDB; 6FH3; X-ray; 1.85 A; A/B=1-355.
DR PDBsum; 6FH1; -.
DR PDBsum; 6FH2; -.
DR PDBsum; 6FH3; -.
DR AlphaFoldDB; P0DMM5; -.
DR SMR; P0DMM5; -.
DR GeneID; 58573133; -.
DR BRENDA; 2.7.14.1; 623.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004111; F:creatine kinase activity; IEA:InterPro.
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; Kinase; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..363
FT /note="Protein-arginine kinase"
FT /id="PRO_0000430097"
FT DOMAIN 24..255
FT /note="Phosphagen kinase C-terminal"
FT MOTIF 338..343
FT /note="RDXXRA motif of the pArg binding pocket involved in
FT allosteric regulation"
FT /evidence="ECO:0000269|PubMed:30962626"
FT BINDING 27..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:30962626"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:30962626"
FT BINDING 177..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602,
FT ECO:0000305|PubMed:30962626"
FT BINDING 208..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT MUTAGEN 92
FT /note="H->A: Loss of protein kinase activity."
FT /evidence="ECO:0000269|PubMed:30962626"
FT MUTAGEN 122
FT /note="E->A: Loss of protein kinase activity."
FT /evidence="ECO:0000269|PubMed:19498169,
FT ECO:0000269|PubMed:30962626"
FT MUTAGEN 168
FT /note="C->A: Loss of protein kinase activity."
FT /evidence="ECO:0000269|PubMed:30962626"
FT MUTAGEN 208
FT /note="R->A: Loss of protein kinase activity."
FT /evidence="ECO:0000269|PubMed:30962626"
FT MUTAGEN 211
FT /note="Y->A: Loss of protein kinase activity."
FT /evidence="ECO:0000269|PubMed:30962626"
FT MUTAGEN 213
FT /note="E->A,D: Loss of protein kinase activity."
FT /evidence="ECO:0000269|PubMed:19498169,
FT ECO:0000269|PubMed:30962626"
FT MUTAGEN 273
FT /note="R->E: Abolishes dimerization. Large decrease in
FT protein kinase activity."
FT /evidence="ECO:0000269|PubMed:30962626"
FT MUTAGEN 282
FT /note="R->E: Abolishes dimerization. Large decrease in
FT protein kinase activity."
FT /evidence="ECO:0000269|PubMed:30962626"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:6FH1"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:6FH1"
FT TURN 20..24
FT /evidence="ECO:0007829|PDB:6FH1"
FT STRAND 25..34
FT /evidence="ECO:0007829|PDB:6FH1"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:6FH1"
FT HELIX 47..61
FT /evidence="ECO:0007829|PDB:6FH1"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:6FH1"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:6FH1"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:6FH1"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:6FH1"
FT HELIX 96..101
FT /evidence="ECO:0007829|PDB:6FH1"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:6FH1"
FT STRAND 113..134
FT /evidence="ECO:0007829|PDB:6FH1"
FT HELIX 136..151
FT /evidence="ECO:0007829|PDB:6FH1"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:6FH1"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:6FH1"
FT STRAND 176..183
FT /evidence="ECO:0007829|PDB:6FH1"
FT HELIX 185..189
FT /evidence="ECO:0007829|PDB:6FH1"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:6FH2"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:6FH1"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:6FH1"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:6FH1"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:6FH1"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:6FH1"
FT HELIX 234..263
FT /evidence="ECO:0007829|PDB:6FH1"
FT HELIX 265..280
FT /evidence="ECO:0007829|PDB:6FH1"
FT HELIX 286..301
FT /evidence="ECO:0007829|PDB:6FH1"
FT HELIX 311..319
FT /evidence="ECO:0007829|PDB:6FH1"
FT HELIX 322..329
FT /evidence="ECO:0007829|PDB:6FH1"
FT HELIX 335..355
FT /evidence="ECO:0007829|PDB:6FH1"
SQ SEQUENCE 363 AA; 40853 MW; DE55B7DE22920D45 CRC64;
MSFGKFFNTA VSAWMSQEGP NSDIVLSSRI RLARNIVDFR FPTLFSSEEA KQIVALFERA
FVHRPYGEAG RFELLKMSEL QPIEKRVLVE KHLISPHLAE DSPFGACLLS ENEEISIMIN
EEDHIRIQCL FPGLQLAEAL EAASELDDWI EGHVNYAFDE RLGYLTSCPT NVGTGLRASV
MMHLPALVLT QQINRIIPAI NQLGLVVRGT YGEGSEALGN IFQISNQITL GKSEEDIVAD
LHTIVEQLIA QERAARQALV KTLGIQLEDK VFRSYGILAN CRVIDSKEAA QCLSDVRLGI
DLGYIKNVSR NILNELMILT QPGFLQQYAG GVLRPEERDV RRAALIRERL RMETRRKMEG
DER
