ID   SRKA_ECOL6              Reviewed;         328 AA.
AC   P0C0K4; P32127;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 81.
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}; OrderedLocusNames=c4803;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN83234.1; -; Genomic_DNA.
DR   RefSeq; WP_001065497.1; NZ_CP051263.1.
DR   AlphaFoldDB; P0C0K4; -.
DR   SMR; P0C0K4; -.
DR   STRING; 199310.c4803; -.
DR   EnsemblBacteria; AAN83234; AAN83234; c4803.
DR   KEGG; ecc:c4803; -.
DR   eggNOG; COG2334; Bacteria.
DR   HOGENOM; CLU_054715_0_0_6; -.
DR   OMA; MHYSAWL; -.
DR   BioCyc; ECOL199310:C4803-MON; -.
DR   Proteomes; UP000001410; 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_0000209576"
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;  38120 MW;  100AEEF0FBF04436 CRC64;
     MNNSAFTFQT LHPDTIMDAL FEHGIRVDSG LTPLNSYENR VYQFQDEDRR RFVVKFYRPE
     RWTADQILEE HQFALQLVND EVPVAAPVAF NGQTLLNHQG FYFAVFPSVG GRQFEADNID
     QMEAVGRYLG RMHQTGRKQL FIHRPTIGLN EYLIEPRKLF EDATLIPSGL KAAFLKATDE
     LIAAVTAHWR EDFTVLRLHG DCHAGNILWR DGPMFVDLDD ARNGPAVQDL WMLLNGDKAE
     QRMQLETIIE AYEEFSEFDT AEIGLIEPLR AMRLVYYLAW LMRRWADPAF PKNFPWLTGE
     DYWLRQTATF IEQAKVLQEP PLQLTPMY