SRKA_ECOLI
ID SRKA_ECOLI Reviewed; 328 AA.
AC P0C0K3; P32127; Q2M8F7;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Stress response kinase A {ECO:0000255|HAMAP-Rule:MF_01497, ECO:0000303|PubMed:23416055};
DE EC=2.7.11.1 {ECO:0000255|HAMAP-Rule:MF_01497, ECO:0000269|PubMed:17302814};
DE AltName: Full=Serine/threonine protein kinase YihE {ECO:0000303|PubMed:17302814};
DE AltName: Full=Serine/threonine-protein kinase SrkA {ECO:0000255|HAMAP-Rule:MF_01497, ECO:0000305};
GN Name=srkA {ECO:0000255|HAMAP-Rule:MF_01497, ECO:0000303|PubMed:23416055};
GN Synonyms=rdoA, yihE; OrderedLocusNames=b3859, JW3831;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=7881552; DOI=10.1099/13500872-140-12-3337;
RA Belin P., Boquet P.L.;
RT "The Escherichia coli dsbA gene is partly transcribed from the promoter of
RT a weakly expressed upstream gene.";
RL Microbiology 140:3337-3348(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, AND INDUCTION BY CPX.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=9159398; DOI=10.1101/gad.11.9.1169;
RA Pogliano J., Lynch A.S., Belin D., Lin E.C., Beckwith J.;
RT "Regulation of Escherichia coli cell envelope proteins involved in protein
RT folding and degradation by the Cpx two-component system.";
RL Genes Dev. 11:1169-1182(1997).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-36 AND ASP-217.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=23416055; DOI=10.1016/j.celrep.2013.01.026;
RA Dorsey-Oresto A., Lu T., Mosel M., Wang X., Salz T., Drlica K., Zhao X.;
RT "YihE kinase is a central regulator of programmed cell death in bacteria.";
RL Cell Rep. 3:528-537(2013).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP POSSIBLE COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ASP-217.
RX PubMed=17302814; DOI=10.1111/j.1365-2958.2007.05611.x;
RA Zheng J., He C., Singh V.K., Martin N.L., Jia Z.;
RT "Crystal structure of a novel prokaryotic Ser/Thr kinase and its
RT implication in the Cpx stress response pathway.";
RL Mol. Microbiol. 63:1360-1371(2007).
CC -!- FUNCTION: A protein kinase that (auto)phosphorylates on Ser and Thr
CC residues (PubMed:17302814). Probably acts to suppress the effects of
CC stress linked to accumulation of reactive oxygen species. Protects
CC cells from stress by antagonizing the MazE-MazF TA module, probably
CC indirectly as it has not been seen to phosphorylate MazE, MazF or MazG
CC (PubMed:23416055). Probably involved in the extracytoplasmic stress
CC response (PubMed:9159398). {ECO:0000255|HAMAP-Rule:MF_01497,
CC ECO:0000269|PubMed:17302814, ECO:0000269|PubMed:23416055,
CC ECO:0000269|PubMed:9159398}.
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:0000255|HAMAP-Rule:MF_01497,
CC ECO:0000269|PubMed:17302814};
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:0000255|HAMAP-Rule:MF_01497,
CC ECO:0000269|PubMed:17302814};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:17302814};
CC Note=May bind 2 Mg(2+) ions. {ECO:0000305|PubMed:17302814};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01497,
CC ECO:0000269|PubMed:17302814}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01497,
CC ECO:0000305|PubMed:17302814}.
CC -!- INDUCTION: Induced by the two-component Cpx system that responds to
CC extracellular stress. {ECO:0000269|PubMed:9159398}.
CC -!- DISRUPTION PHENOTYPE: A hyperlethal phenotype (reduced survival in the
CC presence of antibiotic but no change in minimal inhibitory
CC concentration) for a number of antimicrobials including nalidixic acid,
CC tetracycline, ampicillin and mitomycin C as well as exposure to UV
CC light and H(2)O(2). Lethality is mitigated by pretreatment with 2,2'-
CC bipyridyl and thiourea, which inhibit hydroxyl radical accumulation. No
CC change in cell survival upon heat shock (up to 55 degrees Celsius),
CC rifampicin or fluoroquinolone PD161144 treatment. A triple srkA-mazE-
CC mazF disruption mutant shows no hyperlethality in the presence of
CC nalidixic acid or UV light, suggesting SrkA has a negative effect on
CC MazF. Double katG-srkA and double cpxR-srkA disruption mutants are as
CC sensitive to killing as single srkA mutants; i.e. all 3 genes are
CC epistatic and function in the same genetic pathway.
CC {ECO:0000269|PubMed:23416055}.
CC -!- SIMILARITY: Belongs to the SrkA/RdoA protein kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_01497}.
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DR EMBL; X80762; CAA56735.1; -; Genomic_DNA.
DR EMBL; L19201; AAB02994.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76857.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77449.1; -; Genomic_DNA.
DR PIR; S40805; S40805.
DR RefSeq; NP_418296.1; NC_000913.3.
DR RefSeq; WP_001065497.1; NZ_SSZK01000026.1.
DR PDB; 1ZYL; X-ray; 2.80 A; A=1-328.
DR PDBsum; 1ZYL; -.
DR AlphaFoldDB; P0C0K3; -.
DR SMR; P0C0K3; -.
DR BioGRID; 4261338; 3.
DR IntAct; P0C0K3; 5.
DR STRING; 511145.b3859; -.
DR jPOST; P0C0K3; -.
DR PaxDb; P0C0K3; -.
DR PRIDE; P0C0K3; -.
DR EnsemblBacteria; AAC76857; AAC76857; b3859.
DR EnsemblBacteria; BAE77449; BAE77449; BAE77449.
DR GeneID; 948346; -.
DR KEGG; ecj:JW3831; -.
DR KEGG; eco:b3859; -.
DR PATRIC; fig|511145.12.peg.3968; -.
DR EchoBASE; EB1778; -.
DR eggNOG; COG2334; Bacteria.
DR HOGENOM; CLU_054715_0_0_6; -.
DR InParanoid; P0C0K3; -.
DR OMA; MHYSAWL; -.
DR PhylomeDB; P0C0K3; -.
DR BioCyc; EcoCyc:EG11831-MON; -.
DR BioCyc; MetaCyc:EG11831-MON; -.
DR EvolutionaryTrace; P0C0K3; -.
DR PRO; PR:P0C0K3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; EXP:EcoCyc.
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; IDA:EcoCyc.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; PTHR39573; 1.
DR Pfam; PF01636; APH; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Stress response; Transferase.
FT CHAIN 1..328
FT /note="Stress response kinase A"
FT /id="PRO_0000209574"
FT ACT_SITE 201
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01497,
FT ECO:0000305|PubMed:17302814"
FT ACT_SITE 217
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01497,
FT ECO:0000305|PubMed:17302814"
FT BINDING 206
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01497,
FT ECO:0000305|PubMed:17302814"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01497,
FT ECO:0000305|PubMed:17302814"
FT SITE 36
FT /note="ATP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01497,
FT ECO:0000305|PubMed:17302814"
FT MUTAGEN 36
FT /note="S->A: Partial loss of kinase activity, only
FT partially protects bacteria against hyperlethal stress."
FT /evidence="ECO:0000269|PubMed:23416055"
FT MUTAGEN 217
FT /note="D->A: Loss of kinase activity; does not protect
FT bacteria against hyperlethal stress."
FT /evidence="ECO:0000269|PubMed:17302814,
FT ECO:0000269|PubMed:23416055"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:1ZYL"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1ZYL"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:1ZYL"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:1ZYL"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1ZYL"
FT HELIX 64..79
FT /evidence="ECO:0007829|PDB:1ZYL"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1ZYL"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:1ZYL"
FT HELIX 119..136
FT /evidence="ECO:0007829|PDB:1ZYL"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1ZYL"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:1ZYL"
FT HELIX 154..161
FT /evidence="ECO:0007829|PDB:1ZYL"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1ZYL"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:1ZYL"
FT HELIX 171..188
FT /evidence="ECO:0007829|PDB:1ZYL"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:1ZYL"
FT STRAND 207..215
FT /evidence="ECO:0007829|PDB:1ZYL"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:1ZYL"
FT HELIX 238..252
FT /evidence="ECO:0007829|PDB:1ZYL"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:1ZYL"
FT HELIX 260..265
FT /evidence="ECO:0007829|PDB:1ZYL"
FT HELIX 266..283
FT /evidence="ECO:0007829|PDB:1ZYL"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:1ZYL"
FT HELIX 289..293
FT /evidence="ECO:0007829|PDB:1ZYL"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:1ZYL"
FT HELIX 300..316
FT /evidence="ECO:0007829|PDB:1ZYL"
SQ SEQUENCE 328 AA; 38120 MW; 100AEEF0FBF04436 CRC64;
MNNSAFTFQT LHPDTIMDAL FEHGIRVDSG LTPLNSYENR VYQFQDEDRR RFVVKFYRPE
RWTADQILEE HQFALQLVND EVPVAAPVAF NGQTLLNHQG FYFAVFPSVG GRQFEADNID
QMEAVGRYLG RMHQTGRKQL FIHRPTIGLN EYLIEPRKLF EDATLIPSGL KAAFLKATDE
LIAAVTAHWR EDFTVLRLHG DCHAGNILWR DGPMFVDLDD ARNGPAVQDL WMLLNGDKAE
QRMQLETIIE AYEEFSEFDT AEIGLIEPLR AMRLVYYLAW LMRRWADPAF PKNFPWLTGE
DYWLRQTATF IEQAKVLQEP PLQLTPMY
