(data stored in SCRATCH zone)

SWISSPROT: E6SFI1_INTC7

ID   E6SFI1_INTC7            Unreviewed;       277 AA.
AC   E6SFI1;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   16-JAN-2019, entry version 49.
DE   RecName: Full=Putative phosphoenolpyruvate synthase regulatory protein {ECO:0000256|HAMAP-Rule:MF_01062};
DE            Short=PEP synthase regulatory protein {ECO:0000256|HAMAP-Rule:MF_01062};
DE            Short=PSRP {ECO:0000256|HAMAP-Rule:MF_01062};
DE            EC=2.7.11.33 {ECO:0000256|HAMAP-Rule:MF_01062};
DE            EC=2.7.4.28 {ECO:0000256|HAMAP-Rule:MF_01062};
DE   AltName: Full=Pyruvate, water dikinase regulatory protein {ECO:0000256|HAMAP-Rule:MF_01062};
GN   OrderedLocusNames=Intca_0158 {ECO:0000313|EMBL:ADU46719.1};
OS   Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 /
OS   NBRC 12989 / 7 KIP).
OC   Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae;
OC   Intrasporangium.
OX   NCBI_TaxID=710696 {ECO:0000313|EMBL:ADU46719.1, ECO:0000313|Proteomes:UP000008914};
RN   [1] {ECO:0000313|EMBL:ADU46719.1, ECO:0000313|Proteomes:UP000008914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP
RC   {ECO:0000313|Proteomes:UP000008914};
RX   PubMed=21304734; DOI=10.4056/sigs.1263355;
RA   Del Rio T.G., Chertkov O., Yasawong M., Lucas S., Deshpande S.,
RA   Cheng J.F., Detter C., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Rohde M., Pukall R., Sikorski J., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Intrasporangium calvum type strain (7
RT   KIP).";
RL   Stand. Genomic Sci. 3:294-303(2010).
CC   -!- FUNCTION: Bifunctional serine/threonine kinase and phosphorylase
CC       involved in the regulation of the phosphoenolpyruvate synthase
CC       (PEPS) by catalyzing its phosphorylation/dephosphorylation.
CC       {ECO:0000256|HAMAP-Rule:MF_01062, ECO:0000256|SAAS:SAAS00892141}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[pyruvate, water dikinase] + ADP = [pyruvate, water
CC         dikinase]-phosphate + AMP + H(+); Xref=Rhea:RHEA:46020,
CC         Rhea:RHEA-COMP:11425, Rhea:RHEA-COMP:11426, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456215,
CC         ChEBI:CHEBI:456216; EC=2.7.11.33; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01062, ECO:0000256|SAAS:SAAS01117524};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[pyruvate, water dikinase]-phosphate + H(+) + phosphate =
CC         [pyruvate, water dikinase] + diphosphate; Xref=Rhea:RHEA:48580,
CC         Rhea:RHEA-COMP:11425, Rhea:RHEA-COMP:11426, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:43176, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:68546; EC=2.7.4.28; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01062, ECO:0000256|SAAS:SAAS01117527};
CC   -!- SIMILARITY: Belongs to the pyruvate, phosphate/water dikinase
CC       regulatory protein family. PSRP subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_01062, ECO:0000256|SAAS:SAAS00892150}.
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DR   EMBL; CP002343; ADU46719.1; -; Genomic_DNA.
DR   RefSeq; WP_013491041.1; NC_014830.1.
DR   STRING; 710696.Intca_0158; -.
DR   EnsemblBacteria; ADU46719; ADU46719; Intca_0158.
DR   KEGG; ica:Intca_0158; -.
DR   eggNOG; ENOG4105CF9; Bacteria.
DR   eggNOG; COG1806; LUCA.
DR   HOGENOM; HOG000218053; -.
DR   KO; K09773; -.
DR   OrthoDB; 980472at2; -.
DR   BioCyc; ICAL710696:GH9U-162-MONOMER; -.
DR   Proteomes; UP000008914; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043531; F:ADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016776; F:phosphotransferase activity, phosphate group as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01062; PSRP; 1.
DR   InterPro; IPR005177; Kinase-pyrophosphorylase.
DR   InterPro; IPR026530; PSRP.
DR   PANTHER; PTHR31756; PTHR31756; 1.
DR   Pfam; PF03618; Kinase-PPPase; 1.
PE   3: Inferred from homology;
DR   PRODOM; E6SFI1.
DR   SWISS-2DPAGE; E6SFI1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008914};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01062,
KW   ECO:0000256|SAAS:SAAS00918839}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01062,
KW   ECO:0000256|SAAS:SAAS00918828};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008914};
KW   Serine/threonine-protein kinase {ECO:0000256|HAMAP-Rule:MF_01062,
KW   ECO:0000256|SAAS:SAAS00918833};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01062,
KW   ECO:0000256|SAAS:SAAS00918832};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     12     31       Helical. {ECO:0000256|SAM:Phobius}.
FT   NP_BIND     158    165       ADP. {ECO:0000256|HAMAP-Rule:MF_01062}.
SQ   SEQUENCE   277 AA;  30868 MW;  F7CE57AF537D031F CRC64;
     MSAPDSVTET PVFFLAGGTG ISAETLGNLM LNQFPSVRFR RRKIPFITTP EIARQVVAEM
     DEAMTDAVTP LVFSTVADEE VRTELVKTKC AFIDLFGSHL DAIERVLHVN ASHNRAGLHG
     LGDPRRYEQR MKAIEYAMEH DDGQSLRNLA QAELILVAPS RCGKTPTSMY LALQHGIRVA
     NYPLVEEDLH STHLPRPIRD YADRCFGLVS TPARLSQVRS ERRPGSTYAS LAQCSYELRR
     AEALYRAHRI PSINSASMSV EEMAAVIMQT RHMSNLA
//

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