(data stored in ACNUC7421 zone)

SWISSPROT: D6XV73_BACIE

ID   D6XV73_BACIE            Unreviewed;       365 AA.
AC   D6XV73;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 72.
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=Bsel_0082 {ECO:0000313|EMBL:ADH97631.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97631.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97631.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the specific phosphorylation of arginine
CC       residues in proteins. {ECO:0000256|HAMAP-Rule:MF_00602}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-
CC         phospho-L-arginyl-[protein]; Xref=Rhea:RHEA:43384, Rhea:RHEA-
CC         COMP:10532, Rhea:RHEA-COMP:10533, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29965, ChEBI:CHEBI:30616, ChEBI:CHEBI:83226,
CC         ChEBI:CHEBI:456216; EC=2.7.14.1; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00602, ECO:0000256|SAAS:SAAS01117987};
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00602, ECO:0000256|PROSITE-
CC       ProRule:PRU00843, ECO:0000256|RuleBase:RU000505,
CC       ECO:0000256|SAAS:SAAS00894300}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00602}.
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DR   EMBL; CP001791; ADH97631.1; -; Genomic_DNA.
DR   RefSeq; WP_013171061.1; NC_014219.1.
DR   STRING; 439292.Bsel_0082; -.
DR   EnsemblBacteria; ADH97631; ADH97631; Bsel_0082.
DR   KEGG; bse:Bsel_0082; -.
DR   eggNOG; ENOG41066A3; Bacteria.
DR   eggNOG; COG3869; LUCA.
DR   HOGENOM; HOG000082112; -.
DR   KO; K19405; -.
DR   OMA; ACPTNVG; -.
DR   OrthoDB; 904915at2; -.
DR   BioCyc; BSEL439292:G1GLR-106-MONOMER; -.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016775; F:phosphotransferase activity, nitrogenous group as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:UniProtKB-UniRule.
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; D6XV73.
DR   SWISS-2DPAGE; D6XV73.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00602, ECO:0000256|PROSITE-
KW   ProRule:PRU00843, ECO:0000256|SAAS:SAAS00894316};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
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,
KW   ECO:0000256|PROSITE-ProRule:PRU00843, ECO:0000256|SAAS:SAAS00894308};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
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       Phosphagen kinase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51510}.
FT   NP_BIND      27     31       ATP. {ECO:0000256|HAMAP-Rule:MF_00602,
FT                                ECO:0000256|PROSITE-ProRule:PRU00843}.
FT   NP_BIND     177    181       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00843}.
FT   NP_BIND     208    213       ATP. {ECO:0000256|HAMAP-Rule:MF_00602,
FT                                ECO:0000256|PROSITE-ProRule:PRU00843}.
FT   BINDING      92     92       ATP. {ECO:0000256|HAMAP-Rule:MF_00602,
FT                                ECO:0000256|PROSITE-ProRule:PRU00843}.
FT   BINDING     126    126       ATP. {ECO:0000256|HAMAP-Rule:MF_00602,
FT                                ECO:0000256|PROSITE-ProRule:PRU00843}.
SQ   SEQUENCE   365 AA;  41316 MW;  6B266B6AF3357761 CRC64;
     MSLQSFISEA ISPWMKNEGP ESDIVISTRV RLARNEAHTA FPIAAMNDRL EEVLNRVKQN
     FAGRSHRRFG ELELLAMTDL SPNERRMLVE KHLISPNLAA GEHGSGVLLS EDESLSVMIN
     EEDHYRIQCL MSGFQLDACL KYANAMDDWM EEKVDFAFHE NRGYLTSCPT NVGTGLRSSV
     MMHLPALVLT NQFNRIVPAI SQLGLVVRGI YGEGSEALGN LFQISNQTTL GKTEADIVDN
     LKGVVKQLIQ HERAARQTLY EQSQLFLEDR VYRSLGTLAY SRRMETQEAM QRLSDVRLGI
     DLGIINHMQG KILNELMVLT QPGFLQHYAE QELSAEERDE RRATFIRERL QLEKKNDHTN
     GGGQP
//

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