ID   KINA_BACSU              Reviewed;         606 AA.
AC   P16497; P22863;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   04-NOV-2026, entry version 185.
DE   RecName: Full=Sporulation kinase A;
DE            EC=2.7.13.3;
DE   AltName: Full=Stage II sporulation protein F;
DE   AltName: Full=Stage II sporulation protein J;
GN   Name=kinA; Synonyms=gsiC, scoD, spoIIF, spoIIJ;
GN   OrderedLocusNames=BSU13990;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2104615; DOI=10.1128/jb.172.1.86-93.1990;
RA   Antoniewski C., Savelli B., Stragier P.;
RT   "The spoIIJ gene, which regulates early developmental steps in Bacillus
RT   subtilis, belongs to a class of environmentally responsive genes.";
RL   J. Bacteriol. 172:86-93(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=2509430; DOI=10.1128/jb.171.11.6187-6196.1989;
RA   Perego M., Cole S.P., Burbulys D., Trach K., Hoch J.A.;
RT   "Characterization of the gene for a protein kinase which phosphorylates the
RT   sporulation-regulatory proteins Spo0A and Spo0F of Bacillus subtilis.";
RL   J. Bacteriol. 171:6187-6196(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Scanlan E., Devine K.M.;
RT   "Sequence of the Bacillus subtilis chromosome from ykuA to cse-15.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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).
CC   -!- FUNCTION: Phosphorylates the sporulation-regulatory proteins spo0A and
CC       spo0F. It also autophosphorylates in the presence of ATP.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- INTERACTION:
CC       P16497; P16497: kinA; NbExp=8; IntAct=EBI-6405707, EBI-6405707;
CC       P16497; Q7WY62: sda; NbExp=6; IntAct=EBI-6405707, EBI-6405714;
CC       P16497; P06628: spo0F; NbExp=3; IntAct=EBI-6405707, EBI-6418009;
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DR   EMBL; M29450; AAA22800.1; -; Genomic_DNA.
DR   EMBL; M31067; AAA22664.1; -; Genomic_DNA.
DR   EMBL; AJ222587; CAA10862.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13272.1; -; Genomic_DNA.
DR   PIR; A33496; A33496.
DR   RefSeq; NP_389282.1; NC_000964.3.
DR   RefSeq; WP_003245779.1; NC_000964.3.
DR   PDB; 2VLG; X-ray; 1.70 A; A/B/C/D=10-117.
DR   AlphaFoldDB; P16497; -.
DR   SASBDB; P16497; -.
DR   SMR; P16497; -.
DR   DIP; DIP-58966N; -.
DR   FunCoup; P16497; 313.
DR   IntAct; P16497; 2.
DR   STRING; 224308.BSU13990; -.
DR   BindingDB; P16497; -.
DR   ChEMBL; CHEMBL2111331; -.
DR   PaxDb; 224308-BSU13990; -.
DR   DNASU; 939230; -.
DR   EnsemblBacteria; CAB13272; CAB13272; BSU_13990.
DR   GeneID; 939230; -.
DR   KEGG; bsu:BSU13990; -.
DR   PATRIC; fig|224308.179.peg.1525; -.
DR   eggNOG; COG4191; Bacteria.
DR   InParanoid; P16497; -.
DR   OMA; AFHITFP; -.
DR   OrthoDB; 9815750at2; -.
DR   PhylomeDB; P16497; -.
DR   BioCyc; BSUB:BSU13990-MONOMER; -.
DR   BRENDA; 2.7.13.3; 658.
DR   EvolutionaryTrace; P16497; -.
DR   PRO; PR:P16497; -.
DR   Proteomes; UP000001570; Chromosome.
DR   AbasyAtlas; P16497; -.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:CACAO.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 3.
DR   FunFam; 1.10.287.130:FF:000040; PAS domain-containing sensor histidine kinase; 1.
DR   FunFam; 3.30.450.20:FF:000231; PAS domain-containing sensor histidine kinase; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 3.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR003594; HATPase_dom.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P_dom.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 3.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065:SF34; SPORULATION KINASE A; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 2.
DR   Pfam; PF08447; PAS_3; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 3.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 3.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Sporulation; Transferase;
KW   Two-component regulatory system.
FT   CHAIN           1..606
FT                   /note="Sporulation kinase A"
FT                   /id="PRO_0000074776"
FT   DOMAIN          3..73
FT                   /note="PAS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          77..116
FT                   /note="PAC 1"
FT   DOMAIN          140..214
FT                   /note="PAS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          218..255
FT                   /note="PAC 2"
FT   DOMAIN          265..335
FT                   /note="PAS 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          402..606
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         405
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   CONFLICT        276
FT                   /note="S -> F (in Ref. 1; AAA22800)"
FT                   /evidence="ECO:0000305"
FT   STRAND          17..21
FT                   /evidence="ECO:0007829|PDB:2VLG"
FT   STRAND          25..30
FT                   /evidence="ECO:0007829|PDB:2VLG"
FT   HELIX           34..38
FT                   /evidence="ECO:0007829|PDB:2VLG"
FT   HELIX           42..45
FT                   /evidence="ECO:0007829|PDB:2VLG"
FT   HELIX           50..53
FT                   /evidence="ECO:0007829|PDB:2VLG"
FT   HELIX           56..58
FT                   /evidence="ECO:0007829|PDB:2VLG"
FT   HELIX           59..67
FT                   /evidence="ECO:0007829|PDB:2VLG"
FT   STRAND          75..80
FT                   /evidence="ECO:0007829|PDB:2VLG"
FT   STRAND          86..95
FT                   /evidence="ECO:0007829|PDB:2VLG"
FT   STRAND          98..103
FT                   /evidence="ECO:0007829|PDB:2VLG"
FT   STRAND          107..113
FT                   /evidence="ECO:0007829|PDB:2VLG"
SQ   SEQUENCE   606 AA;  69171 MW;  A8BB97FE844B32EE CRC64;
     MEQDTQHVKP LQTKTDIHAV LASNGRIIYI SANSKLHLGY LQGEMIGSFL KTFLHEEDQF
     LVESYFYNEH HLMPCTFRFI KKDHTIVWVE AAVEIVTTRA ERTEREIILK MKVLEEETGH
     QSLNCEKHEI EPASPESTTY ITDDYERLVE NLPSPLCISV KGKIVYVNSA MLSMLGAKSK
     DAIIGKSSYE FIEEEYHDIV KNRIIRMQKG MEVGMIEQTW KRLDGTPVHL EVKASPTVYK
     NQQAELLLLI DISSRKKFQT ILQKSRERYQ LLIQNSIDTI AVIHNGKWVF MNESGISLFE
     AATYEDLIGK NIYDQLHPCD HEDVKERIQN IAEQKTESEI VKQSWFTFQN RVIYTEMVCI
     PTTFFGEAAV QVILRDISER KQTEELMLKS EKLSIAGQLA AGIAHEIRNP LTAIKGFLQL
     MKPTMEGNEH YFDIVFSELS RIELILSELL MLAKPQQNAV KEYLNLKKLI GEVSALLETQ
     ANLNGIFIRT SYEKDSIYIN GDQNQLKQVF INLIKNAVES MPDGGTVDII ITEDEHSVHV
     TVKDEGEGIP EKVLNRIGEP FLTTKEKGTG LGLMVTFNII ENHQGVIHVD SHPEKGTAFK
     ISFPKK
//