ID B5RFH4_SALG2 Unreviewed; 328 AA.
AC B5RFH4;
DT 04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
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=yihE {ECO:0000313|EMBL:CAR39217.1};
GN Synonyms=srkA {ECO:0000256|HAMAP-Rule:MF_01497};
GN OrderedLocusNames=SG3426 {ECO:0000313|EMBL:CAR39217.1};
OS Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550538 {ECO:0000313|EMBL:CAR39217.1, ECO:0000313|Proteomes:UP000008321};
RN [1] {ECO:0000313|EMBL:CAR39217.1, ECO:0000313|Proteomes:UP000008321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=287/91 / NCTC 13346 {ECO:0000313|Proteomes:UP000008321};
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Sanders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphrey T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(2008).
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:0000256|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: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;
CC Evidence={ECO:0000256|HAMAP-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM933173; CAR39217.1; -; Genomic_DNA.
DR RefSeq; WP_000999264.1; NC_011274.1.
DR AlphaFoldDB; B5RFH4; -.
DR KEGG; seg:SG3426; -.
DR HOGENOM; CLU_054715_0_0_6; -.
DR Proteomes; UP000008321; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1270.170; -; 1.
DR Gene3D; 3.30.200.70; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; STRESS RESPONSE KINASE A; 1.
DR PANTHER; PTHR39573:SF1; STRESS RESPONSE KINASE A; 1.
DR Pfam; PF01636; APH; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01497};
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 Serine/threonine-protein kinase {ECO:0000256|HAMAP-Rule:MF_01497};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_01497}; Transferase {ECO:0000256|HAMAP-Rule:MF_01497}.
FT DOMAIN 31..259
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT ACT_SITE 201
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01497"
FT ACT_SITE 217
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01497"
FT BINDING 206
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01497"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01497"
FT SITE 36
FT /note="ATP"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01497"
SQ SEQUENCE 328 AA; 38154 MW; ACD79A9ABBBAD72C 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 AYEEVSEFDT AEIGLIEPLR AMRLVYYLAW LIRRWGDPAF PKNFPWLTGE
DYWQRQTTTF IEQTKILHEP PLQLTPMY
//
