HIPA_SHEON
ID HIPA_SHEON Reviewed; 433 AA.
AC Q8EIX3;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Serine/threonine-protein kinase toxin HipA {ECO:0000305};
DE Short=Ser/Thr-protein kinase HipA;
DE EC=2.7.11.1 {ECO:0000269|PubMed:25056321};
DE AltName: Full=Toxin HipA {ECO:0000303|PubMed:25056321};
GN Name=hipA {ECO:0000303|PubMed:25056321}; OrderedLocusNames=SO_0706;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=MR-1;
RX PubMed=20034561; DOI=10.1016/j.resmic.2009.12.002;
RA Theunissen S., De Smet L., Dansercoer A., Motte B., Coenye T.,
RA Van Beeumen J.J., Devreese B., Savvides S.N., Vergauwen B.;
RT "The 285 kDa Bap/RTX hybrid cell surface protein (SO4317) of Shewanella
RT oneidensis MR-1 is a key mediator of biofilm formation.";
RL Res. Microbiol. 161:144-152(2010).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF APOPROTEIN; IN COMPLEX WITH HIPB
RP AND DNA AND IN COMPLEX WITH ATP ANALOG, FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, INDUCTION, PHOSPHORYLATION AT SER-147, MUTAGENESIS OF ASP-306, AND
RP DNA-BINDING.
RC STRAIN=MR-1;
RX PubMed=25056321; DOI=10.1093/nar/gku665;
RA Wen Y., Behiels E., Felix J., Elegheert J., Vergauwen B., Devreese B.,
RA Savvides S.N.;
RT "The bacterial antitoxin HipB establishes a ternary complex with operator
RT DNA and phosphorylated toxin HipA to regulate bacterial persistence.";
RL Nucleic Acids Res. 42:10134-10147(2014).
CC -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system;
CC overexpression in wild-type temporarily inhibits cell growth,
CC overexpression in a hipAB deletion leads to acute growth inhibition.
CC The toxic effect of HipA is neutralized by its cognate antitoxin HipB.
CC In the ternary phosphoserine-HipA-HipB-DNA complex the DNA is bent
CC about 125 degrees; all HipA in the crystallized ternary complex is
CC phosphorylated. In E.coli phosphorylation of HipA is thought to release
CC HipB from the HipA-HipB-DNA complex, suggesting the complex functions
CC differently in the 2 bacteria (PubMed:25056321). Phosphorylates Glu-
CC tRNA-ligase (GltX, on 'Ser-239') in vivo, with HipB probably acts as a
CC corepressor for transcription of the hipBA promoter (By similarity).
CC {ECO:0000250|UniProtKB:P23874, ECO:0000269|PubMed:25056321}.
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:0000269|PubMed:25056321};
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:0000269|PubMed:25056321};
CC -!- SUBUNIT: Monomer. Forms a HipA(2)HipB(2)-DNA complex with cognate
CC antitoxin HipB; has higher affinity for the latter when HipB is
CC prebound to DNA and HipA is phosphorylated. Binds DNA in the ternary
CC complex. {ECO:0000269|PubMed:25056321}.
CC -!- INDUCTION: Expressed in late-exponential phase; part of the hipBA
CC operon. {ECO:0000269|PubMed:25056321}.
CC -!- DISRUPTION PHENOTYPE: 50% decrease in biofilm.
CC {ECO:0000269|PubMed:20034561}.
CC -!- SIMILARITY: Belongs to the HipA Ser/Thr kinase family. {ECO:0000305}.
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DR EMBL; AE014299; AAN53784.1; -; Genomic_DNA.
DR RefSeq; NP_716339.1; NC_004347.2.
DR RefSeq; WP_011071024.1; NZ_CP053946.1.
DR PDB; 4PU3; X-ray; 3.39 A; A/B=1-433.
DR PDB; 4PU4; X-ray; 3.79 A; A/B=1-433.
DR PDB; 4PU5; X-ray; 1.83 A; A=1-433.
DR PDBsum; 4PU3; -.
DR PDBsum; 4PU4; -.
DR PDBsum; 4PU5; -.
DR AlphaFoldDB; Q8EIX3; -.
DR SMR; Q8EIX3; -.
DR STRING; 211586.SO_0706; -.
DR iPTMnet; Q8EIX3; -.
DR PaxDb; Q8EIX3; -.
DR DNASU; 1168566; -.
DR KEGG; son:SO_0706; -.
DR PATRIC; fig|211586.12.peg.681; -.
DR eggNOG; COG3550; Bacteria.
DR HOGENOM; CLU_030167_1_0_6; -.
DR OMA; QWYFDNL; -.
DR OrthoDB; 1293681at2; -.
DR PhylomeDB; Q8EIX3; -.
DR BioCyc; SONE211586:G1GMP-666-MON; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR012893; HipA-like_C.
DR InterPro; IPR017508; HipA_N1.
DR Pfam; PF13657; Couple_hipA; 1.
DR Pfam; PF07804; HipA_C; 1.
DR TIGRFAMs; TIGR03071; couple_hipA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repressor;
KW Serine/threonine-protein kinase; Toxin-antitoxin system; Transferase.
FT CHAIN 1..433
FT /note="Serine/threonine-protein kinase toxin HipA"
FT /id="PRO_0000431937"
FT DNA_BIND 380..384
FT /evidence="ECO:0000269|PubMed:25056321"
FT DNA_BIND 429
FT /evidence="ECO:0000269|PubMed:25056321"
FT ACT_SITE 306
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P23874"
FT BINDING 151..154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25056321"
FT BINDING 178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25056321"
FT BINDING 220..222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25056321"
FT BINDING 308..311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25056321"
FT BINDING 327..328
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25056321"
FT MOD_RES 147
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:25056321"
FT MUTAGEN 306
FT /note="D->Q: No autophosphorylation."
FT /evidence="ECO:0000269|PubMed:25056321"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:4PU5"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:4PU5"
FT STRAND 16..24
FT /evidence="ECO:0007829|PDB:4PU5"
FT TURN 25..28
FT /evidence="ECO:0007829|PDB:4PU5"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:4PU5"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:4PU5"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:4PU5"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:4PU5"
FT HELIX 88..95
FT /evidence="ECO:0007829|PDB:4PU5"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:4PU5"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:4PU5"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:4PU5"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:4PU5"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:4PU5"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:4PU5"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:4PU5"
FT HELIX 185..198
FT /evidence="ECO:0007829|PDB:4PU5"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:4PU5"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:4PU5"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:4PU5"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:4PU5"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:4PU5"
FT HELIX 241..245
FT /evidence="ECO:0007829|PDB:4PU5"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:4PU5"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:4PU5"
FT TURN 261..265
FT /evidence="ECO:0007829|PDB:4PU3"
FT HELIX 272..277
FT /evidence="ECO:0007829|PDB:4PU5"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:4PU5"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:4PU5"
FT HELIX 285..302
FT /evidence="ECO:0007829|PDB:4PU5"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:4PU3"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:4PU5"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:4PU5"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:4PU5"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:4PU3"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:4PU5"
FT HELIX 357..367
FT /evidence="ECO:0007829|PDB:4PU5"
FT HELIX 371..393
FT /evidence="ECO:0007829|PDB:4PU5"
FT HELIX 401..422
FT /evidence="ECO:0007829|PDB:4PU5"
FT HELIX 425..430
FT /evidence="ECO:0007829|PDB:4PU5"
SQ SEQUENCE 433 AA; 48732 MW; 8B168C5DE511A92B CRC64;
MSTAKTLTLE MHLGDLMIGE LSFDATADTF AVHYTKDWQQ SGFPLSPTIP LDGTGTSNQI
SMFLVNLLPE NKGLDYLIES LGVSKGNTFA LIRAIGLDTA GAIAFVPKGA LLPETQLRPI
KAEEVIQRIE DPTMWPMEIW DGKPRLSVAG VQPKLNLFYN GKEFAFAEGT LSSTHIVKFE
KYHHLVINEF ITMRLAKVLG MNVANVDIVH FGRYKALCVE RFDRRNIPGE QRVLRRHIVD
SCQALGFSVS KKYERNFGTG RDVKDIREGV SFNRLFSLAA KCRNPVAAKQ DMLQWALFNL
LTGNADAHGK NYSFFMTPSG MEPTPWYDLV SVDMYEDFEQ QLAMAIDDEF DPNSIYAYQL
AAFMDGLGLP RNLLISNLTR IARRIPQAIA EVILMLPPLD EDEASFVAHY KTQLLARCER
YLGFVDEVRD VEV
