(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BHN6_GEOS0

ID   A0A0F6BHN6_GEOS0        Unreviewed;       360 AA.
AC   A0A0F6BHN6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 30.
DE   RecName: Full=Protein-arginine kinase {ECO:0000256|HAMAP-Rule:MF_00602, ECO:0000256|SAAS:SAAS00894317};
DE            EC=2.7.14.1 {ECO:0000256|HAMAP-Rule:MF_00602, ECO:0000256|SAAS:SAAS00894303};
GN   Name=mcsB {ECO:0000256|HAMAP-Rule:MF_00602};
GN   OrderedLocusNames=GY4MC1_0081 {ECO:0000313|EMBL:ADP72937.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72937.1};
RN   [1] {ECO:0000313|EMBL:ADP72937.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72937.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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. Protein arginine phosphorylation has a physiologically
CC       important role and is involved in the regulation of many critical
CC       cellular processes, such as protein homeostasis, motility, competence,
CC       and stringent and stress responses, by regulating gene expression and
CC       protein activity. {ECO:0000256|HAMAP-Rule:MF_00602}.
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:0000256|HAMAP-Rule:MF_00602,
CC         ECO:0000256|SAAS:SAAS01117987};
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. {ECO:0000256|HAMAP-
CC       Rule:MF_00602}.
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00602, ECO:0000256|PROSITE-ProRule:PRU00843,
CC       ECO:0000256|RuleBase:RU000505, ECO:0000256|SAAS:SAAS00894300}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002293; ADP72937.1; -; Genomic_DNA.
DR   RefSeq; WP_003247502.1; NC_014650.1.
DR   EnsemblBacteria; ADP72937; ADP72937; GY4MC1_0081.
DR   GeneID; 29237283; -.
DR   KEGG; gmc:GY4MC1_0081; -.
DR   KO; K19405; -.
DR   OMA; ACPTNVG; -.
DR   OrthoDB; 904915at2; -.
DR   BioCyc; GSP581103:G1GOQ-108-MONOMER; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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   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   3: Inferred from homology;
DR   PRODOM; A0A0F6BHN6.
DR   SWISS-2DPAGE; A0A0F6BHN6.
KW   Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_00602};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00602, ECO:0000256|PROSITE-
KW   ProRule:PRU00843, ECO:0000256|SAAS:SAAS00894316};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00602, ECO:0000256|PROSITE-
KW   ProRule:PRU00843, ECO:0000256|RuleBase:RU000505,
KW   ECO:0000256|SAAS:SAAS00894304};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00602, ECO:0000256|PROSITE-
KW   ProRule:PRU00843, ECO:0000256|SAAS:SAAS00894308};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00602, ECO:0000256|PROSITE-
KW   ProRule:PRU00843, ECO:0000256|RuleBase:RU000505,
KW   ECO:0000256|SAAS:SAAS00894312}.
FT   DOMAIN          24..255
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51510"
FT   NP_BIND         27..31
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00602,
FT                   ECO:0000256|PROSITE-ProRule:PRU00843"
FT   NP_BIND         177..181
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00602,
FT                   ECO:0000256|PROSITE-ProRule:PRU00843"
FT   NP_BIND         208..213
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00602,
FT                   ECO:0000256|PROSITE-ProRule:PRU00843"
FT   MOTIF           338..343
FT                   /note="RDXXRA motif of the pArg binding pocket involved in
FT                   allosteric regulation"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00602"
FT   BINDING         92
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00602,
FT                   ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         126
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00602,
FT                   ECO:0000256|PROSITE-ProRule:PRU00843"
SQ   SEQUENCE   360 AA;  40977 MW;  1470F83372B017FA CRC64;
     MSFEKFFNTA VSSWMSQEGP DSDIVLSSRI RLARNIVDFR FPTLFSNEEA QQIVSLFEQT
     FAHRFYRSVG RFELLKMSEL QPIEKRVLVE KHLISPHLAE DSPFGACLLS ENEEISIMIN
     EEDHIRIQCL FPGFQLTEAL KAANELDDWI EEHVIYAFDE KLGYLTSCPT NVGTGMRASV
     MMHLPALVLT QQMNRIIPAV NQLGLVVRGT YGEGSEALGN IFQISNQMTL GKSEEDIVED
     LKSVVQQLIT QERMARETLV KTLNIQLEDR VFRSYGILAN SRVIDSKEAA QCLSDVRLGI
     DLGYIKNISR NILNELMILT QPGFLQQYAG GVLRPEERDV RRAALIRERL KMEERKMNGG
//

If you have problems or comments...

PBIL Back to PBIL home page