ID   KINE_BACSU              Reviewed;         738 AA.
AC   O31661;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Sporulation kinase E;
DE            EC=2.7.13.3;
DE   AltName: Full=Sensor histidine kinase E;
GN   Name=kinE; Synonyms=ykrQ; OrderedLocusNames=BSU13530;
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   FUNCTION IN PHOSPHORYLATING SPO0F, AND INDUCTION.
RC   STRAIN=168 / JH642;
RX   PubMed=11069677; DOI=10.1046/j.1365-2958.2000.02148.x;
RA   Jiang M., Shao W., Perego M., Hoch J.A.;
RT   "Multiple histidine kinases regulate entry into stationary phase and
RT   sporulation in Bacillus subtilis.";
RL   Mol. Microbiol. 38:535-542(2000).
RN   [3]
RP   FUNCTION IN PHOSPHORYLATING SPO0A.
RC   STRAIN=168 / JH642;
RX   PubMed=11886552; DOI=10.1046/j.1365-2958.2001.02709.x;
RA   Hamon M.A., Lazazzera B.A.;
RT   "The sporulation transcription factor Spo0A is required for biofilm
RT   development in Bacillus subtilis.";
RL   Mol. Microbiol. 42:1199-1209(2001).
CC   -!- FUNCTION: Phosphorylates the sporulation-regulatory protein spo0A under
CC       biofilm growth conditions. Also able to weakly phosphorylate spo0F.
CC       {ECO:0000269|PubMed:11069677, ECO:0000269|PubMed:11886552}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- INDUCTION: Expressed during growth and early stationary phase.
CC       {ECO:0000269|PubMed:11069677}.
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DR   EMBL; AL009126; CAB13226.1; -; Genomic_DNA.
DR   PIR; B69863; B69863.
DR   RefSeq; NP_389236.1; NC_000964.3.
DR   RefSeq; WP_003232504.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O31661; -.
DR   IntAct; O31661; 1.
DR   STRING; 224308.BSU13530; -.
DR   PaxDb; O31661; -.
DR   PRIDE; O31661; -.
DR   EnsemblBacteria; CAB13226; CAB13226; BSU_13530.
DR   GeneID; 939349; -.
DR   KEGG; bsu:BSU13530; -.
DR   PATRIC; fig|224308.179.peg.1469; -.
DR   eggNOG; COG5002; Bacteria.
DR   InParanoid; O31661; -.
DR   OMA; GMSENVL; -.
DR   PhylomeDB; O31661; -.
DR   BioCyc; BSUB:BSU13530-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 4.
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; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF13188; PAS_8; 2.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 4.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55785; SSF55785; 4.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 4.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 3.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Sporulation; Transferase;
KW   Two-component regulatory system.
FT   CHAIN           1..738
FT                   /note="Sporulation kinase E"
FT                   /id="PRO_0000375264"
FT   DOMAIN          29..99
FT                   /note="PAS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          150..220
FT                   /note="PAS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          271..342
FT                   /note="PAS 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          391..462
FT                   /note="PAS 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          523..729
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         526
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   738 AA;  85513 MW;  FE27DAB7F08AC64B CRC64;
     METLGVQTNS ELREELNRLK EENARLKKEL NQHQVIVNNT LDAIFICDNE MRIVQANEAT
     ERMLQVDSED LKKRSVLDFL FSIPKDELNL SVKKFFKKGF LWKEVPIRLD CGATKYIEFL
     AKRGIGEDFF FVVMRDISSK KILEREFSMN EQLFKDLFDR AVDGIVLFDK DGGFIDANLS
     FCKSFEINHN ELSHLSLYEF IDSGSRKDFD NIWKALNRKG KAKGELPVKL RSGVQKLFEF
     TITSNIISGF YMSIMRDITE KRSMELQLFK SEERFREIFE NAMDAIIIWS NDGRIVKANQ
     SACKIFELPM NLLLKRKLCD FLVDSQQKYS ITKRKYAKYG EIREELLFQM GNGQFKELEF
     TSKRTILENQ HLTILRNVSD RKRMEKELRE SELKFRKVFN GSMDGNVLFD NQYRIIDANP
     LASHILGLSH EEIKQHSLLD IISAYEIENL ASPARQINFD EMDNEIPFLL SSGDNRKLEF
     SFKRNIIQNM NLAIFKDVTE RKELEERLRK SDTLHVVGEL AAGIAHEIRN PMTALKGFIQ
     LLKGSVEGDY ALYFNVITSE LKRIESIITE FLILAKPQAI MYEEKHVTQI MRDTIDLLNA
     QANLSNVQMQ LDLIDDIPPI YCEPNQLKQV FINILKNAIE VMPDGGNIFV TIKALDQDHV
     LISLKDEGIG MTEDKLKRLG EPFYTTKERG TGLGLMVSYK IIEEHQGEIM VESEEGKGTV
     FHITLPVRQN AEERRNDE