SRKA_SALTI
ID SRKA_SALTI Reviewed; 328 AA.
AC Q8Z2S0; Q7C6K0;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Stress response kinase A {ECO:0000255|HAMAP-Rule:MF_01497};
DE EC=2.7.11.1 {ECO:0000255|HAMAP-Rule:MF_01497};
DE AltName: Full=Serine/threonine-protein kinase SrkA {ECO:0000255|HAMAP-Rule:MF_01497};
GN Name=srkA {ECO:0000255|HAMAP-Rule:MF_01497};
GN OrderedLocusNames=STY3884, t3624;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
CC -!- FUNCTION: A protein kinase that phosphorylates Ser and Thr residues.
CC Probably acts to suppress the effects of stress linked to accumulation
CC of reactive oxygen species. Probably involved in the extracytoplasmic
CC stress response. {ECO:0000255|HAMAP-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, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_01497};
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 -!- SIMILARITY: Belongs to the SrkA/RdoA protein kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_01497}.
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DR EMBL; AL513382; CAD03103.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO71125.1; -; Genomic_DNA.
DR RefSeq; NP_458052.1; NC_003198.1.
DR RefSeq; WP_000999265.1; NZ_WSUR01000010.1.
DR AlphaFoldDB; Q8Z2S0; -.
DR SMR; Q8Z2S0; -.
DR STRING; 220341.16504740; -.
DR EnsemblBacteria; AAO71125; AAO71125; t3624.
DR KEGG; stt:t3624; -.
DR KEGG; sty:STY3884; -.
DR PATRIC; fig|220341.7.peg.3965; -.
DR eggNOG; COG2334; Bacteria.
DR HOGENOM; CLU_054715_0_0_6; -.
DR OMA; MHYSAWL; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase;
KW Stress response; Transferase.
FT CHAIN 1..328
FT /note="Stress response kinase A"
FT /id="PRO_0000209579"
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; 38153 MW; A2D77A9011B07786 CRC64;
MNDNAFTFQT LHPETIMDAL FEQGIRVDSG LTPLNSYENR VYQFQDEDRR RFVVKFYRPE
RWSVDQIREE HQFALELVKD EVPVAAPLAF NGQTLLAHQG YHYAIFPSVG GRQFEADNID
QMEAVGRYLG RLHQTGRKRP FTFRPDIGLA EYLFEPRQVF EDAALIPSGQ KAAFLKATDT
LLSAVTECWR TDFATLRLHG DCHAGNILWR DGPLFVDLDD ARNGPAIQDL WMLLNGNKAE
QRMQLETIIE AYEEVSEFDT AEIGLIEPLR AMRLVYYLAW LIRRWGDPAF PKNFPWLTGE
DYWQRQTTTF IEQTKILHEP PLQLTPMY
