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 03-AUG-2022, entry version 146.
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 P40758; 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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 AlphaFoldDB; P40758; -.
DR SMR; P40758; -.
DR IntAct; P40758; 2.
DR MINT; P40758; -.
DR STRING; 224308.BSU02440; -.
DR PaxDb; P40758; -.
DR PRIDE; P40758; -.
DR EnsemblBacteria; CAB12038; CAB12038; BSU_02440.
DR GeneID; 938417; -.
DR KEGG; bsu:BSU02440; -.
DR PATRIC; fig|224308.43.peg.248; -.
DR eggNOG; COG4191; Bacteria.
DR InParanoid; P40758; -.
DR OMA; EHMLMIV; -.
DR BioCyc; BSUB:BSU02440-MON; -.
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;
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
