KINA_BACSU
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 03-AUG-2022, entry version 171.
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; OrderedLocusNames=BSU13990;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; 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; NZ_JNCM01000035.1.
DR PDB; 2VLG; X-ray; 1.70 A; A/B/C/D=10-117.
DR PDBsum; 2VLG; -.
DR AlphaFoldDB; P16497; -.
DR SASBDB; P16497; -.
DR SMR; P16497; -.
DR DIP; DIP-58966N; -.
DR IntAct; P16497; 2.
DR STRING; 224308.BSU13990; -.
DR BindingDB; P16497; -.
DR ChEMBL; CHEMBL2111331; -.
DR PaxDb; P16497; -.
DR PRIDE; P16497; -.
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; YTEMVCI; -.
DR PhylomeDB; P16497; -.
DR BioCyc; BSUB:BSU13990-MON; -.
DR BRENDA; 2.7.13.3; 658.
DR EvolutionaryTrace; P16497; -.
DR PRO; PR:P16497; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; IMP:CACAO.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
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; 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 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; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55785; SSF55785; 3.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 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
