ID E7C8I0_9GAMM Unreviewed; 328 AA.
AC E7C8I0;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 27.
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};
OS uncultured Oceanospirillales bacterium HF4000_43P14.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC environmental samples.
OX NCBI_TaxID=723620 {ECO:0000313|EMBL:ADI23754.1};
RN [1] {ECO:0000313|EMBL:ADI23754.1}
RP NUCLEOTIDE SEQUENCE.
RA Pham V.D., Delong E.F.;
RT "Genome fragments of uncultured bacteria from the North Pacific subtropical
RT Gyre.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; GU568023; ADI23754.1; -; Genomic_DNA.
DR AlphaFoldDB; E7C8I0; -.
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, ECO:0000313|EMBL:ADI23754.1};
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 40..269
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT ACT_SITE 205
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01497"
FT ACT_SITE 222
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01497"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01497"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01497"
FT SITE 39
FT /note="ATP"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01497"
SQ SEQUENCE 328 AA; 37721 MW; ACD1A3CE7AE1DC20 CRC64;
MTDQEGSTHP FDALTPDVIL DAVDSAGFVT DGRLMGLNSF ENRVYQVGLE DTTPVVVKFY
RPQRWSDAQI LEEHAFSRFL REQELPVVAP LANDRGETLF YHADFRFTVF PRQGGHAPEL
DNADHLLVLG RTLARWHAAG NDRPFQTRPA IDIIADCRAA VDYVNQGVVD PNFSGRYRDL
GGALIEAMER RLDGITWRAI NVHGDCHTGN ILWRDDLPHF VDLDDSVRGP AMQDLWMLLS
GDAEENSQQL RTLSEGYETF LPFPWAQRRL IEPLRARRML RHSAWLAQRW DDPAFPLAFP
WFDSPRYWQD HINDLEQELA TMQRLLEP
//
