SRKA_SHIFL
ID SRKA_SHIFL Reviewed; 328 AA.
AC Q83IV7; Q7BZD6;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Stress response kinase A {ECO:0000255|HAMAP-Rule:MF_01497};
DE EC=2.7.11.1 {ECO:0000255|HAMAP-Rule:MF_01497};
DE AltName: Full=Serine/threonine-protein kinase SrkA {ECO:0000255|HAMAP-Rule:MF_01497};
GN Name=srkA {ECO:0000255|HAMAP-Rule:MF_01497};
GN Synonyms=yihE {ECO:0000303|PubMed:11594757};
GN OrderedLocusNames=SF3930, S3817;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
RN [3]
RP FUNCTION, AND INDUCTION.
RC STRAIN=M90T / Serotype 5a;
RX PubMed=11594757; DOI=10.1006/bbrc.2001.5734;
RA Li M.-S., Kroll J.S., Yu J.;
RT "Influence of the yihE gene of Shigella flexneri on global gene expression:
RT on analysis using DNA arrays.";
RL Biochem. Biophys. Res. Commun. 288:91-100(2001).
RN [4]
RP FUNCTION.
RC STRAIN=M90T / Serotype 5a;
RX PubMed=15073317; DOI=10.1099/mic.0.26840-0;
RA Edwards-Jones B., Langford P.R., Kroll J.S., Yu J.;
RT "The role of the Shigella flexneri yihE gene in LPS synthesis and
RT virulence.";
RL Microbiology 150:1079-1084(2004).
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 (By similarity). Probably involved in the
CC extracytoplasmic stress response (PubMed:11594757). Has also a role in
CC LPS synthesis, through regulation of the galETK expression
CC (PubMed:15073317). {ECO:0000255|HAMAP-Rule:MF_01497,
CC ECO:0000269|PubMed:11594757, ECO:0000269|PubMed:15073317}.
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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01497};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01497};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01497}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01497}.
CC -!- INDUCTION: Expression is regulated by the CpxRA two-component
CC regulatory system. {ECO:0000269|PubMed:11594757}.
CC -!- SIMILARITY: Belongs to the SrkA/RdoA protein kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_01497}.
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DR EMBL; AE005674; AAN45365.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18833.1; -; Genomic_DNA.
DR RefSeq; NP_709658.1; NC_004337.2.
DR RefSeq; WP_001065539.1; NZ_WPGW01000069.1.
DR AlphaFoldDB; Q83IV7; -.
DR SMR; Q83IV7; -.
DR STRING; 198214.SF3930; -.
DR EnsemblBacteria; AAN45365; AAN45365; SF3930.
DR EnsemblBacteria; AAP18833; AAP18833; S3817.
DR GeneID; 1024218; -.
DR KEGG; sfl:SF3930; -.
DR KEGG; sft:NCTC1_04251; -.
DR KEGG; sfx:S3817; -.
DR PATRIC; fig|198214.7.peg.4630; -.
DR HOGENOM; CLU_054715_0_0_6; -.
DR OMA; MHYSAWL; -.
DR OrthoDB; 1003984at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
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: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 2: Evidence at transcript level;
KW 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_0000209581"
FT ACT_SITE 201
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01497"
FT ACT_SITE 217
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01497"
FT BINDING 206
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01497"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01497"
FT SITE 36
FT /note="ATP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01497"
SQ SEQUENCE 328 AA; 38118 MW; 53818BBBDEAE7BEF CRC64;
MNNSAFTFQT LHPDTIMDAL FKQGIRVDSG LTPLNSYENR VYQFQDEERR RFVVKFYRPE
RWTADQILEE HQFALQLVND EVPVAAPVAF NGQTLLNHQG FYFAVFPSVG GRQFEADNID
QMEAVGRYLG RMHQTGRKQL FIHRPTIGLN EYLIEPRKLF EDATLIPSGL KAAFLKATDE
LIAAVTAHWR EDFTVLRLHG DCHAGNILWR DGPMFVDLDD ARNGPAIQDL WMLLNGDKAQ
QRMQLETIIE AYEEFSEFDT AEIGLIEPLR AMRLVYYLAW LMRHWADPAF PKNFPWLTGE
DYWLRQTATF IEQAKVLQEP PLQLTPMY
