ID   D5SRS4_PLAL2            Unreviewed;       356 AA.
AC   D5SRS4;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Protein-arginine kinase {ECO:0000256|HAMAP-Rule:MF_00602};
DE            EC=2.7.14.1 {ECO:0000256|HAMAP-Rule:MF_00602};
GN   Name=mcsB {ECO:0000256|HAMAP-Rule:MF_00602};
GN   OrderedLocusNames=Plim_0763 {ECO:0000313|EMBL:ADG66608.1};
OS   Planctopirus limnophila (strain ATCC 43296 / DSM 3776 / IFAM 1008 / Mu 290)
OS   (Planctomyces limnophilus).
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Planctopirus.
OX   NCBI_TaxID=521674 {ECO:0000313|EMBL:ADG66608.1, ECO:0000313|Proteomes:UP000002220};
RN   [1] {ECO:0000313|EMBL:ADG66608.1, ECO:0000313|Proteomes:UP000002220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43296 / DSM 3776 / IFAM 1008 / 290
RC   {ECO:0000313|Proteomes:UP000002220};
RX   PubMed=21304691; DOI=10.4056/sigs.1052813;
RA   Labutti K., Sikorski J., Schneider S., Nolan M., Lucas S.,
RA   Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Tindall B.J., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Planctomyces limnophilus type strain (Mu
RT   290).";
RL   Stand. Genomic Sci. 3:47-56(2010).
CC   -!- FUNCTION: Catalyzes the specific phosphorylation of arginine residues
CC       in proteins. {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   -!- 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00602,
CC       ECO:0000256|PROSITE-ProRule:PRU00843}.
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DR   EMBL; CP001744; ADG66608.1; -; Genomic_DNA.
DR   RefSeq; WP_013109039.1; NC_014148.1.
DR   AlphaFoldDB; D5SRS4; -.
DR   STRING; 521674.Plim_0763; -.
DR   KEGG; plm:Plim_0763; -.
DR   eggNOG; COG3869; Bacteria.
DR   HOGENOM; CLU_066591_1_0_0; -.
DR   OrthoDB; 9791353at2; -.
DR   Proteomes; UP000002220; Chromosome.
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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd07930; bacterial_phosphagen_kinase; 1.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 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:SF38; ARGININE KINASE; 1.
DR   PANTHER; PTHR11547; ARGININE OR CREATINE KINASE; 1.
DR   Pfam; PF00217; ATP-gua_Ptrans; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR   PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR   PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00602};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00602};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00602}; Reference proteome {ECO:0000313|Proteomes:UP000002220};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00602}.
FT   DOMAIN          23..252
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51510"
FT   BINDING         26..30
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00602,
FT                   ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00602,
FT                   ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         174..178
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         205..210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00602,
FT                   ECO:0000256|PROSITE-ProRule:PRU00843"
SQ   SEQUENCE   356 AA;  40146 MW;  24733F9E7CA2452E CRC64;
     MNLDVLTQRS GEWLRGTGPE ADIVISSRIR LARNLAEFPF VNRASDTVRA QIEDFLRERI
     EKLQGRRPLT YLRTSDLEPL DRQFLVERQL ISREHAEDHG QCGVGVSSEE NVSLMVNEED
     HLRMQVLRSG MDLDAAWAEI NEIDDLMEQE VAYAFDSQFG YLTACPTNVG TGIRVSVMLH
     LPALVATKEI QKVFQALQKI GLAVRGLYGE GSQAMGDFYQ ISNQVTLGKS EIDIMKSIKD
     VVAQILGYER RVRTALVKEN RQALHDQVSR AFGILQNAQT ISSEETMHLL SSVRMGVNLG
     LIDDVEIPTV NELFIQTQPA HLQKLRHQKL ESAERNIARA AYIRQRLAEN NPHTSA
//