(data stored in ACNUC7421 zone)

SWISSPROT: Q146U9_PARXL

ID   Q146U9_PARXL            Unreviewed;       359 AA.
AC   Q146U9;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 70.
DE   RecName: Full=Stress response kinase A {ECO:0000256|HAMAP-Rule:MF_01497};
DE            EC=2.7.11.1 {ECO:0000256|HAMAP-Rule:MF_01497};
DE   AltName: Full=Serine/threonine-protein kinase SrkA {ECO:0000256|HAMAP-Rule:MF_01497};
GN   Name=srkA {ECO:0000256|HAMAP-Rule:MF_01497};
GN   ORFNames=Bxe_A4360 {ECO:0000313|EMBL:ABE28640.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE28640.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE28640.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE28640.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: A protein kinase that phosphorylates Ser and Thr
CC       residues. Probably acts to suppress the effects of stress linked
CC       to accumulation of reactive oxygen species. Probably involved in
CC       the extracytoplasmic stress response. {ECO:0000256|HAMAP-
CC       Rule:MF_01497}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|HAMAP-Rule:MF_01497};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|HAMAP-Rule:MF_01497};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01497};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01497}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01497}.
CC   -!- SIMILARITY: Belongs to the SrkA/RdoA protein kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01497}.
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DR   EMBL; CP000270; ABE28640.1; -; Genomic_DNA.
DR   STRING; 266265.Bxe_A4360; -.
DR   EnsemblBacteria; ABE28640; ABE28640; Bxe_A4360.
DR   KEGG; bxe:Bxe_A4360; -.
DR   eggNOG; ENOG4105E27; Bacteria.
DR   eggNOG; COG2334; LUCA.
DR   HOGENOM; HOG000265894; -.
DR   OMA; PEPGNLD; -.
DR   Proteomes; UP000001817; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01497; SrkA_kinase; 1.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR032882; SrkA/RdoA.
DR   PANTHER; PTHR39573; PTHR39573; 1.
DR   Pfam; PF01636; APH; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q146U9.
DR   SWISS-2DPAGE; Q146U9.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01497};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01497};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01497};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01497};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01497};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01497};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_01497};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Serine/threonine-protein kinase {ECO:0000256|HAMAP-Rule:MF_01497};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_01497};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01497}.
FT   DOMAIN       66    296       APH. {ECO:0000259|Pfam:PF01636}.
FT   ACT_SITE    234    234       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01497}.
FT   ACT_SITE    251    251       {ECO:0000256|HAMAP-Rule:MF_01497}.
FT   METAL       239    239       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01497}.
FT   METAL       251    251       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01497}.
FT   SITE         67     67       ATP. {ECO:0000256|HAMAP-Rule:MF_01497}.
SQ   SEQUENCE   359 AA;  40873 MW;  B6BD88EFBCE9ED2C CRC64;
     MCVVTLVFDG GAAHNAGMND DILDPQDGAN SAVPFARLKP EIVLDALDGV LSTVGVRTDG
     RMLPLNSYEN RVYQVGVEDG PPVVAKFYRP ERWSDAAILE EHAFVADLAS REIPAVPARV
     FEGRTLHSFD GFRFSIFERR GGRAPDLDRP DTLEWLGRFI GRIHAVGQTQ NYVERPTLDI
     HTFGYEPRDF LLAHRFVPDN LRTAWETVVN LALEGVERAF ERAGDIRMLR MHGDCHPSNV
     LWTDAGPHFV DFDDSRMGPA VQDLWLLLPG ERAEASRALA DLLAGYEDFC DFEPRELYLV
     EALRTLRLIH YQAWLARRWD DPAFPAAFPW FNTQRYWEDR ILELREQIGA MQEGPLWPV
//

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