RDOA_SALTY
ID RDOA_SALTY Reviewed; 328 AA.
AC Q8ZKU8;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Serine/threonine protein kinase RdoA {ECO:0000303|PubMed:17302814};
DE EC=2.7.11.1 {ECO:0000255|HAMAP-Rule:MF_01497, ECO:0000269|PubMed:17302814};
DE AltName: Full=Serine/threonine-protein kinase SrkA {ECO:0000255|HAMAP-Rule:MF_01497};
DE AltName: Full=Stress response kinase A {ECO:0000255|HAMAP-Rule:MF_01497};
GN Name=rdoA {ECO:0000303|PubMed:12511488}; Synonyms=srkA {ECO:0000305};
GN OrderedLocusNames=STM3996;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP FUNCTION, AND INDUCTION.
RC STRAIN=SL1344;
RX PubMed=12511488; DOI=10.1128/jb.185.2.432-443.2003;
RA Suntharalingam P., Spencer H., Gallant C.V., Martin N.L.;
RT "Salmonella enterica serovar typhimurium rdoA is growth phase regulated and
RT involved in relaying Cpx-induced signals.";
RL J. Bacteriol. 185:432-443(2003).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=SL1344;
RX PubMed=17302814; DOI=10.1111/j.1365-2958.2007.05611.x;
RA Zheng J., He C., Singh V.K., Martin N.L., Jia Z.;
RT "Crystal structure of a novel prokaryotic Ser/Thr kinase and its
RT implication in the Cpx stress response pathway.";
RL Mol. Microbiol. 63:1360-1371(2007).
CC -!- FUNCTION: A protein kinase that (auto)phosphorylates on Ser and Thr
CC residues, probably involved in the extracytoplasmic stress response
CC (PubMed:12511488). Probably acts to suppress the effects of stress
CC linked to accumulation of reactive oxygen species (By similarity).
CC {ECO:0000255|HAMAP-Rule:MF_01497, ECO:0000269|PubMed:12511488}.
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, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01497,
CC ECO:0000269|PubMed:17302814};
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:0000255|HAMAP-Rule:MF_01497,
CC ECO:0000269|PubMed:17302814};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01497};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01497}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01497,
CC ECO:0000305|PubMed:17302814}.
CC -!- INDUCTION: Expression is growth phase dependent and sensitive to the
CC media conditions reaching high levels in stationary phase (at protein
CC level) (PubMed:17302814). It is probably regulated by the CpxRA two-
CC component regulatory system (PubMed:12511488).
CC {ECO:0000269|PubMed:12511488, ECO:0000269|PubMed:17302814}.
CC -!- DISRUPTION PHENOTYPE: Decreases long-term survival (1000-fold decrease
CC after 20 days in liquid culture), derepresses curli production under
CC non-curli-inducing growth conditions. {ECO:0000269|PubMed:17302814}.
CC -!- SIMILARITY: Belongs to the SrkA/RdoA protein kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_01497}.
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DR EMBL; AE006468; AAL22835.1; -; Genomic_DNA.
DR RefSeq; NP_462876.1; NC_003197.2.
DR RefSeq; WP_000999249.1; NC_003197.2.
DR AlphaFoldDB; Q8ZKU8; -.
DR SMR; Q8ZKU8; -.
DR STRING; 99287.STM3996; -.
DR PaxDb; Q8ZKU8; -.
DR EnsemblBacteria; AAL22835; AAL22835; STM3996.
DR GeneID; 1255522; -.
DR KEGG; stm:STM3996; -.
DR PATRIC; fig|99287.12.peg.4210; -.
DR HOGENOM; CLU_054715_0_0_6; -.
DR OMA; MHYSAWL; -.
DR PhylomeDB; Q8ZKU8; -.
DR BioCyc; SENT99287:STM3996-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Stress response; Transferase.
FT CHAIN 1..328
FT /note="Serine/threonine protein kinase RdoA"
FT /id="PRO_0000209580"
FT ACT_SITE 201
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01497"
FT ACT_SITE 217
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01497"
FT BINDING 206
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01497"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01497"
FT SITE 36
FT /note="ATP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01497"
SQ SEQUENCE 328 AA; 38129 MW; 4164C01ED6041E1B CRC64;
MNDNAFTFQT LHPETIMDAL FEQGIMVDSG LTPLNSYENR VYQFQDEDRR RFVVKFYRPE
RWSVDQIREE HQFALELVKD EVPVAAPLAF NGQTLLAHQG YHYAIFPSVG GRQFEADNID
QMEAVGRYLG RLHQTGRKRP FTFRPDIGLA EYLFEPRQVF EDAALIPSGQ KAAFLKATDT
LLSAVTECWR TDFATLRLHG DCHAGNILWR DGPLFVDLDD ARNGPAIQDL WMLLNGDKAE
QRMQLETIIE AYEEVSEFDT AEIGLIEPLR AMRLVYYLAW LIRRWGDPAF PKNFPWLTGE
DYWQRQTTTF IEQTKILHEP PLQLTPMY
