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Database: UniProt
Entry: A0A0A0DMR6_9BURK
LinkDB: A0A0A0DMR6_9BURK
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ID   A0A0A0DMR6_9BURK        Unreviewed;       342 AA.
AC   A0A0A0DMR6;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=JY96_04490 {ECO:0000313|EMBL:KGM39529.1};
OS   Aquabacterium sp. NJ1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Aquabacterium.
OX   NCBI_TaxID=1538295 {ECO:0000313|EMBL:KGM39529.1, ECO:0000313|Proteomes:UP000029993};
RN   [1] {ECO:0000313|EMBL:KGM39529.1, ECO:0000313|Proteomes:UP000029993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJ1 {ECO:0000313|EMBL:KGM39529.1,
RC   ECO:0000313|Proteomes:UP000029993};
RA   Masuda H.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KGM39529.1, ECO:0000313|Proteomes:UP000029993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJ1 {ECO:0000313|EMBL:KGM39529.1,
RC   ECO:0000313|Proteomes:UP000029993};
RA   Shiwa Y., Yoshikawa H., Zylstra G.J.;
RT   "The draft genome sequence of a soil bacterium, Aquabacterium sp. strain
RT   NJ1, capable of utilizing both liquid and solid n-alkanes.";
RL   Submitted (OCT-2014) 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}.
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:KGM39529.1}.
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DR   EMBL; JRKM01000001; KGM39529.1; -; Genomic_DNA.
DR   RefSeq; WP_035035308.1; NZ_JRKM01000001.1.
DR   AlphaFoldDB; A0A0A0DMR6; -.
DR   STRING; 1538295.JY96_04490; -.
DR   eggNOG; COG2334; Bacteria.
DR   OrthoDB; 5392197at2; -.
DR   Proteomes; UP000029993; 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:KGM39529.1};
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:UP000029993};
KW   Serine/threonine-protein kinase {ECO:0000256|HAMAP-Rule:MF_01497,
KW   ECO:0000313|EMBL:KGM39529.1};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_01497}; Transferase {ECO:0000256|HAMAP-Rule:MF_01497}.
FT   DOMAIN          33..278
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
FT   ACT_SITE        213
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01497"
FT   ACT_SITE        230
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01497"
FT   BINDING         218
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01497"
FT   BINDING         230
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01497"
FT   SITE            35
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01497"
SQ   SEQUENCE   342 AA;  38782 MW;  50879C19151AFF9C CRC64;
     MHADTPYADL TPDLVLDALE ALGQRVDGRL LQLNSYENRV FQIGLDSGHF VVAKFYRPGR
     WSDAQILEEH AFAHELVAAE VPAVPPMPLQ AALEGASVQG DPPTLGFFKG HRVAVSHRRG
     GRSPELEDLG VLTWLGRFLA RLHLVGAQHP FVHRPTMGVA QTGRQARQWL ADSDSLPIEQ
     RTLWLAVADQ ALDLCQQAFD RIDGLRLRRL HGDCHPGNIL WTPDGPHFVD LDDACMGPAV
     QDFWMLLSGD PRDRQVQLNA LLEGYESIAE FDWRELKLVE PLRTLRIIHH SAWLARRWHD
     PAFPAAFPWF GSAMYWQQQI DLLRQQIDVM QTPDDQPAWM MD
//
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