ID G5S3J0_SALET Unreviewed; 328 AA.
AC G5S3J0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=srkA {ECO:0000256|HAMAP-Rule:MF_01497};
GN ORFNames=LTSEURB_5937 {ECO:0000313|EMBL:EHC97766.1};
OS Salmonella enterica subsp. enterica serovar Urbana str. R8-2977.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913084 {ECO:0000313|EMBL:EHC97766.1, ECO:0000313|Proteomes:UP000004776};
RN [1] {ECO:0000313|EMBL:EHC97766.1, ECO:0000313|Proteomes:UP000004776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R8-2977 {ECO:0000313|EMBL:EHC97766.1,
RC ECO:0000313|Proteomes:UP000004776};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(2011).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHC97766.1}.
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DR EMBL; AFCW01002168; EHC97766.1; -; Genomic_DNA.
DR AlphaFoldDB; G5S3J0; -.
DR PATRIC; fig|913084.3.peg.4411; -.
DR Proteomes; UP000004776; Unassembled WGS sequence.
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
//
