ID   SRKA_SALCH              Reviewed;         328 AA.
AC   Q57HL7;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=SCH_3889;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
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; AE017220; AAX67795.1; -; Genomic_DNA.
DR   RefSeq; WP_000999261.1; NC_006905.1.
DR   AlphaFoldDB; Q57HL7; -.
DR   SMR; Q57HL7; -.
DR   EnsemblBacteria; AAX67795; AAX67795; SCH_3889.
DR   KEGG; sec:SCH_3889; -.
DR   HOGENOM; CLU_054715_0_0_6; -.
DR   OMA; MHYSAWL; -.
DR   Proteomes; UP000000538; 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_0000209577"
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;  38168 MW;  ACCF2139A301742C CRC64;
     MNDNAFTFQT LHPETIMDAL FEQGIRVDSG LTPLNSYENR VYQFQDEDRR RFVVKFYRPE
     RWSVDQIREE HQFALELVKD EVPVAAPLAF NGQTLLAHQG YHYAIFPSVG GRQFEADNID
     QMEAVGRYLG RLHQTGRKRP FTFRPDIGLA EYLFEPRQVF EDAALIPSGQ KAAFLKATDT
     LLSAVTECWR TDFATLRLHG DCHAGNILWR DGPLFVDLDD ARNGPAIQDL WMLLNGDKAE
     QRMQLETIIE AYEEISEFDT AEIGLIEPLR AMRLVYYLAW LIRRWGDPAF PKNFPWLTGE
     DYWQRQTTTF IEQTKILHEP PLQLTPMY