ID   ARNS_SULAC              Reviewed;         623 AA.
AC   Q4J9K4;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Serine/threonine-protein kinase ArnS {ECO:0000303|PubMed:27731916};
DE            Short=Ser/Thr protein kinase ArnS {ECO:0000303|PubMed:27731916};
DE            EC=2.7.11.1 {ECO:0000269|PubMed:27731916};
DE   AltName: Full=Archaellum regulatory network protein ArnS {ECO:0000305};
GN   Name=arnS {ECO:0000303|PubMed:27731916};
GN   OrderedLocusNames=Saci_1181 {ECO:0000312|EMBL:AAY80528.1};
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INDUCTION,
RP   AUTOPHOSPHORYLATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-344.
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=27731916; DOI=10.1111/mmi.13550;
RA   Haurat M.F., Figueiredo A.S., Hoffmann L., Li L., Herr K., Wilson A.J.,
RA   Beeby M., Schaber J., Albers S.-V.;
RT   "ArnS, a kinase involved in starvation-induced archaellum expression.";
RL   Mol. Microbiol. 103:181-194(2017).
CC   -!- FUNCTION: Plays an essential role in the controlled expression of
CC       archaellum components during starvation-induced motility. May inhibit
CC       arnR transcription and promote ArnR translation.
CC       {ECO:0000269|PubMed:27731916}.
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:27731916};
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:27731916};
CC   -!- ACTIVITY REGULATION: Autophosphorylation is stimulated by Mn(2+).
CC       {ECO:0000269|PubMed:27731916}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Induced during starvation conditions.
CC       {ECO:0000269|PubMed:27731916}.
CC   -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:27731916}.
CC   -!- DISRUPTION PHENOTYPE: Deletion results in dysregulation of the
CC       archaellum regulatory network that leads to reduced motility, though
CC       the archaellum is properly assembled. Deletion mutant is still able to
CC       sense starvation and to induce archaellum formation, but with a delay
CC       at the signal transduction cascade level.
CC       {ECO:0000269|PubMed:27731916}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; CP000077; AAY80528.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4J9K4; -.
DR   SMR; Q4J9K4; -.
DR   STRING; 330779.Saci_1181; -.
DR   EnsemblBacteria; AAY80528; AAY80528; Saci_1181.
DR   KEGG; sai:Saci_1181; -.
DR   PATRIC; fig|330779.12.peg.1145; -.
DR   eggNOG; arCOG03682; Archaea.
DR   HOGENOM; CLU_446654_0_0_2; -.
DR   Proteomes; UP000001018; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP 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; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Stress response; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..623
FT                   /note="Serine/threonine-protein kinase ArnS"
FT                   /id="PRO_0000439510"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          317..623
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        460
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         323..331
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         344
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MUTAGEN         344
FT                   /note="K->A: Abolishes autophosphorylation."
FT                   /evidence="ECO:0000269|PubMed:27731916"
SQ   SEQUENCE   623 AA;  70061 MW;  81A9B51DD18E11D7 CRC64;
     MLMSFILLIS TSMILISVFS YVLIALIVLG IVLSLISLLS PRVSYVSSVY LIGLTVYLNP
     GFSLTQSLIN TVPILGEINM LSGLLKTPVT SIISSLFSLA LLNLGIKGYE IYLSKHADIV
     KLDSIIFSQH GLPKQANWNI VVNSEVKLLK SNEKLILSNT PEAKYELCPT LVDHKYYVPN
     KVTGLAFEGE VIRINYSPVD GVPYEKFRNC FTVFEVEGLP PDTSFVIEIN GASLKLKDRK
     FAKLSLEPLY WKVNEIRISR EDEEEIYEPD IKEGLTFRGG TVKINFRRKV IRYKTAKIPS
     IENWDPGIWV GQEVYGYRVI EVIGLGGNGY VMKVEKNGLL YAMKVLSVNK FTNSLEHFDN
     LLKESENLEK LSKDPRLVSI YGSFVDKNNI QSALAGDYTS YYKYPPAIIM EFMEGGTLFD
     LISRVDLVQS KYWQYIVKLV IKEIAKALTF LHKRGYVHLD VKPQNIFLKE KINGEPEVVY
     KILSSTPGII KLGDLGSAVR VGEKITQATP AYSPPEQIEA VITGKGAQPS MDNYALGVTL
     YKLLTMKNLD YVNYLDKAFD EYIKGDPSIA MKYINMAKMS MVNFKPKLPH NTLPELANVV
     QGTLVVDPKR RLTSYDIVKI LEG