(data stored in ACNUC7421 zone)

SWISSPROT: GLNK_BACSU

ID   GLNK_BACSU              Reviewed;         410 AA.
AC   P40758; O87101;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 3.
DT   11-DEC-2019, entry version 138.
DE   RecName: Full=Sensor histidine kinase GlnK {ECO:0000303|PubMed:15995196};
DE            EC=2.7.13.3 {ECO:0000305|PubMed:15995196};
GN   Name=glnK {ECO:0000303|PubMed:15995196}; Synonyms=nrgB, ycbA, yzgA;
GN   OrderedLocusNames=BSU02440;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [2]
RP   SEQUENCE REVISION TO N-TERMINUS.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-394.
RC   STRAIN=168;
RA   Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.;
RT   "Sequence analysis of the 70kb region between 17 and 23 degree of the
RT   Bacillus subtilis chromosome.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 333-410.
RC   STRAIN=BD99;
RX   PubMed=8011666; DOI=10.1016/0005-2728(94)90131-7;
RA   Quirk P.G., Guffanti A.A., Clejan S., Cheng J., Krulwich T.A.;
RT   "Isolation of Tn917 insertional mutants of Bacillus subtilis that are
RT   resistant to the protonophore carbonyl cyanide m-chlorophenylhydrazone.";
RL   Biochim. Biophys. Acta 1186:27-34(1994).
RN   [5]
RP   FUNCTION.
RX   PubMed=11717295; DOI=10.1128/jb.183.24.7365-7370.2001;
RA   Kobayashi K., Ogura M., Yamaguchi H., Yoshida K., Ogasawara N., Tanaka T.,
RA   Fujita Y.;
RT   "Comprehensive DNA microarray analysis of Bacillus subtilis two-component
RT   regulatory systems.";
RL   J. Bacteriol. 183:7365-7370(2001).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=168;
RX   PubMed=15995196; DOI=10.1128/jb.187.14.4813-4821.2005;
RA   Satomura T., Shimura D., Asai K., Sadaie Y., Hirooka K., Fujita Y.;
RT   "Enhancement of glutamine utilization in Bacillus subtilis through the
RT   GlnK-GlnL two-component regulatory system.";
RL   J. Bacteriol. 187:4813-4821(2005).
RN   [7]
RP   FUNCTION, INTERACTION WITH TNRA, DISRUPTION PHENOTYPE, SUBCELLULAR
RP   LOCATION, AND SUBUNIT.
RX   PubMed=17001076; DOI=10.1074/jbc.m607582200;
RA   Heinrich A., Woyda K., Brauburger K., Meiss G., Detsch C., Stuelke J.,
RA   Forchhammer K.;
RT   "Interaction of the membrane-bound GlnK-AmtB complex with the master
RT   regulator of nitrogen metabolism TnrA in Bacillus subtilis.";
RL   J. Biol. Chem. 281:34909-34917(2006).
RN   [8]
RP   FUNCTION, INTERACTION WITH TNRA, DISRUPTION PHENOTYPE, AND SUBUNIT.
RX   PubMed=21435182; DOI=10.1111/j.1742-4658.2011.08102.x;
RA   Kayumov A., Heinrich A., Fedorova K., Ilinskaya O., Forchhammer K.;
RT   "Interaction of the general transcription factor TnrA with the PII-like
RT   protein GlnK and glutamine synthetase in Bacillus subtilis.";
RL   FEBS J. 278:1779-1789(2011).
RN   [9]
RP   INTERACTION WITH TNRA AND AMTB, AND SUBUNIT.
RX   PubMed=25691471; DOI=10.1101/gad.254714.114;
RA   Schumacher M.A., Chinnam N.B., Cuthbert B., Tonthat N.K., Whitfill T.;
RT   "Structures of regulatory machinery reveal novel molecular mechanisms
RT   controlling B. subtilis nitrogen homeostasis.";
RL   Genes Dev. 29:451-464(2015).
CC   -!- FUNCTION: Member of the two-component regulatory system GlnK/GlnL that
CC       positively regulates the expression of the glsA-glnT operon in response
CC       to glutamine (PubMed:11717295, PubMed:15995196). It seems that
CC       autophosphorylated GlnK transfers a phosphoryl group to GlnL, which
CC       positively regulates the expression of the glsA-glnT operon
CC       (PubMed:11717295, PubMed:15995196). Interaction between GlnK-AmtB
CC       complex and TnrA protects TnrA from proteolytic degradation
CC       (PubMed:17001076, PubMed:21435182). {ECO:0000269|PubMed:11717295,
CC       ECO:0000269|PubMed:15995196, ECO:0000269|PubMed:17001076,
CC       ECO:0000269|PubMed:21435182}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000305|PubMed:15995196};
CC   -!- SUBUNIT: Homotrimer (PubMed:17001076, PubMed:25691471). Under poor
CC       nitrogen source such as nitrate, the complex between GlnK and AmtB,
CC       which are the transmembrane ammonium transporter and its cognate
CC       regulator, respectively, interacts with TnrA (PubMed:17001076,
CC       PubMed:21435182, PubMed:25691471). GlnK-ATP complex are not able to
CC       bind TnrA (PubMed:21435182). {ECO:0000269|PubMed:17001076,
CC       ECO:0000269|PubMed:21435182, ECO:0000269|PubMed:25691471}.
CC   -!- INTERACTION:
CC       Q45666:tnrA; NbExp=6; IntAct=EBI-8507093, EBI-8507041;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17001076};
CC       Multi-pass membrane protein {ECO:0000305|PubMed:15995196}. Note=ATP
CC       concentrations are sensed by GlnK and affect its cellular localization.
CC       {ECO:0000269|PubMed:17001076}.
CC   -!- DISRUPTION PHENOTYPE: In the absence of nitrogen source, cells lacking
CC       this gene do not show degradation of TnrA, which is entirely soluble.
CC       {ECO:0000269|PubMed:17001076, ECO:0000269|PubMed:21435182}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA33142.1; Type=Frameshift; Evidence={ECO:0000305};
DR   EMBL; AL009126; CAB12038.2; -; Genomic_DNA.
DR   EMBL; AB006424; BAA33142.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; L22503; AAA64346.1; -; Genomic_DNA.
DR   PIR; D69752; D69752.
DR   RefSeq; NP_388126.2; NC_000964.3.
DR   RefSeq; WP_010886394.1; NZ_JNCM01000030.1.
DR   SMR; P40758; -.
DR   IntAct; P40758; 2.
DR   MINT; P40758; -.
DR   STRING; 224308.BSU02440; -.
DR   PaxDb; P40758; -.
DR   PRIDE; P40758; -.
DR   EnsemblBacteria; CAB12038; CAB12038; BSU02440.
DR   GeneID; 938417; -.
DR   KEGG; bsu:BSU02440; -.
DR   PATRIC; fig|224308.43.peg.248; -.
DR   eggNOG; COG0642; LUCA.
DR   HOGENOM; HOG000087751; -.
DR   InParanoid; P40758; -.
DR   KO; K07717; -.
DR   OMA; EHMLMIV; -.
DR   BioCyc; BSUB:BSU02440-MONOMER; -.
DR   Proteomes; UP000001570; 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:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF02518; HATPase_c; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P40758.
DR   SWISS-2DPAGE; P40758.
KW   ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..410
FT                   /note="Sensor histidine kinase GlnK"
FT                   /id="PRO_0000074768"
FT   TOPO_DOM        1..15
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        37..38
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        60..71
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        93..102
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        124..139
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        161..410
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          189..405
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         190
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   410 AA;  46801 MW;  88D0E033366113E2 CRC64;
     MLITVPLAGE LKFYPLNEEF RVSFGAPVFF FFLSLLRHVP AVLPGFLTGA AVFIFRVFLE
     LWGGGHNGLT PILYDQASGF FFYMTYACLF SILKANRFRE RPIMLGFIGF MIEVVSDCVE
     LTVQFLIFHT VVTPEKITDI AVIAISHTFI VMSFYSVLKL YETQSREKQT RQQHEHMLMI
     VSNLYEETVH LKKTLKTTEK VTNDSYQLYR EMKGKDVQLS GRILRLAGEI HEVKKDNQRI
     FAGLSKLISN ESLRDYMRAS DLLQLVIRMN EKYAEALGKQ IDFYCSIEGE HDEYHVFIVL
     SIINNLTANA VEAMDEEGMV SLRLRKPNES MVEFQVEDNG PGISEKIGDI VFDPGFTSKY
     DEFGTPSTGI GLSYVKEIVT ELEGDITFDN QQRGVVFAIR LPVRHLIQKG
//

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