ID A0A1Y6L3V9_9GAMM Unreviewed; 328 AA.
AC A0A1Y6L3V9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=PAQU9191_03617 {ECO:0000313|EMBL:SMY18276.1};
OS Photobacterium aquimaris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=512643 {ECO:0000313|EMBL:SMY18276.1, ECO:0000313|Proteomes:UP000196485};
RN [1] {ECO:0000313|Proteomes:UP000196485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=type strain: CECT 9192 {ECO:0000313|Proteomes:UP000196485};
RA Rodrigo-Torres L., Arahal R. D., Lucena T.;
RL Submitted (JUN-2017) 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; FYAH01000014; SMY18276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6L3V9; -.
DR Proteomes; UP000196485; 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, ECO:0000313|EMBL:SMY18276.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000196485};
KW Serine/threonine-protein kinase {ECO:0000256|HAMAP-Rule:MF_01497,
KW ECO:0000313|EMBL:SMY18276.1};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_01497}; Transferase {ECO:0000256|HAMAP-Rule:MF_01497}.
FT DOMAIN 35..264
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; 38508 MW; FAA512B71805B015 CRC64;
MEKQSFSFAD LSPDVLLDAL DSIEVHAESG LLALNSYENR VYQFKAEDGQ RYVTKFYRPA
RWSDQQIDEE HQFTLELEQH DIPVAAPIAI NGSTLHHYNG YRFALFPSVG GRQFEVDNFD
QLEWVGRFLG RIHQVGQRQP FIHRPTLGLE EYVYQPRQIL ANSDFIPDYL KHSFFADLDR
LIAEIESHWS TDWPALRLHG DCHPGNILWR DGPMFVDLDD ARNGPAVQDL WMMLNGERHD
QLAQLDTLLE AYNEFADFDP RQLKLIEPLR ALRMVHYMAW LAKRWQDPAF PRAFPWFGDA
KYWEGQVLAF KEQIFSLNEQ PLQLMPQW
//
