ID A0A272EZ45_9RHOO Unreviewed; 327 AA.
AC A0A272EZ45;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=CGU29_00715 {ECO:0000313|EMBL:PAS95392.1};
OS Candidatus Dactylopiibacterium carminicum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Dactylopiibacterium.
OX NCBI_TaxID=857335 {ECO:0000313|EMBL:PAS95392.1, ECO:0000313|Proteomes:UP000216107};
RN [1] {ECO:0000313|EMBL:PAS95392.1, ECO:0000313|Proteomes:UP000216107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NFDCM {ECO:0000313|EMBL:PAS95392.1,
RC ECO:0000313|Proteomes:UP000216107};
RA Vera A.;
RT "Candidatus Dactylopiibacterium carminicum, a nitrogen-fixing symbiont of
RT the cochineal insect Dactylopius coccus and Dactylopius opuntiae
RT (Hemiptera: Coccoidea: Dactylopiidae).";
RL Submitted (JUL-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}.
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:PAS95392.1}.
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; NMRN01000001; PAS95392.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A272EZ45; -.
DR OrthoDB; 5392197at2; -.
DR Proteomes; UP000216107; 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:PAS95392.1};
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 ECO:0000313|EMBL:PAS95392.1};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_01497}; Transferase {ECO:0000256|HAMAP-Rule:MF_01497}.
FT DOMAIN 35..267
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT ACT_SITE 204
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01497"
FT ACT_SITE 221
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01497"
FT BINDING 209
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01497"
FT BINDING 221
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 327 AA; 36732 MW; 6D0482B2B4D12D0E CRC64;
MSDAPHPFAT LTPDRVLDAI DATGLRTDGR LLALNSYENR VYQAGLEEGG FIVAKFYRPD
RWSDAAIREE HAFTRALAEA EIPAVPPLLR ADGDSLTHAE GFRVAVFPRR GGRSLELNDP
EVLEWLGRFI GRIHAVGATA AFRERLTLDV ATWGEAPSAF VLASPHLPSD LCEAYRGAVS
AALEGVHACF ERAGDITRLR LHGDCHPGNV MWTDAGPHFV DFDDACTGPA VQDLWMLLSG
ERGEMTRQLA DLVAGYEDFR EFNPREVDLI EALRTLRLIH HAAWLARRWD DPAFPTAFPW
FNTRGWWEEH IGNLRDQLPR MAEPWRF
//
