KIND_BACSU
ID KIND_BACSU Reviewed; 506 AA.
AC O31671;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Sporulation kinase D;
DE EC=2.7.13.3;
DE AltName: Full=Sensor histidine kinase D;
GN Name=kinD; Synonyms=ykvD; OrderedLocusNames=BSU13660;
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 DISRUPTION PHENOTYPE.
RC STRAIN=168 / JH642;
RX PubMed=10411754; DOI=10.1046/j.1365-2958.1999.01481.x;
RA Jiang M., Tzeng Y.-L., Feher V.A., Perego M., Hoch J.A.;
RT "Alanine mutants of the Spo0F response regulator modifying specificity for
RT sensor kinases in sporulation initiation.";
RL Mol. Microbiol. 33:389-395(1999).
RN [3]
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 [4]
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).
RN [5]
RP FUNCTION IN PHOSPHORYLATING SPO0A.
RC STRAIN=168 / JH642;
RX PubMed=18410285; DOI=10.1111/j.1365-2958.2008.06234.x;
RA Castilla-Llorente V., Salas M., Meijer W.J.J.;
RT "kinC/D-mediated heterogeneous expression of spo0A during logarithmical
RT growth in Bacillus subtilis is responsible for partial suppression of phi
RT 29 development.";
RL Mol. Microbiol. 68:1406-1417(2008).
RN [6]
RP SUBUNIT, AND INTERACTION WITH FLOT.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=26297017; DOI=10.1099/mic.0.000137;
RA Schneider J., Mielich-Suess B., Boehme R., Lopez D.;
RT "In vivo characterization of the scaffold activity of flotillin on the
RT membrane kinase KinC of Bacillus subtilis.";
RL Microbiology 161:1871-1887(2015).
CC -!- FUNCTION: Phosphorylates the sporulation-regulatory protein spo0F and,
CC to a minor extent, is responsible for heterogeneous expression of spo0A
CC during logarithmical growth. Also phosphorylates spo0A under biofilm
CC growth conditions. {ECO:0000269|PubMed:11069677,
CC ECO:0000269|PubMed:11886552, ECO:0000269|PubMed:18410285}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBUNIT: Oligomerizes, probably forms homodimers; oligomerization is
CC assisted by FloT. Interacts with FloT. {ECO:0000269|PubMed:26297017}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Expressed during growth and early stationary phase.
CC {ECO:0000269|PubMed:11069677}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene sporulate normally in
CC spo0F mutants. {ECO:0000269|PubMed:10411754}.
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DR EMBL; AL009126; CAB13239.1; -; Genomic_DNA.
DR PIR; F69867; F69867.
DR RefSeq; NP_389249.1; NC_000964.3.
DR RefSeq; WP_010886497.1; NZ_JNCM01000035.1.
DR PDB; 4JGO; X-ray; 2.28 A; A/B=37-250.
DR PDB; 4JGP; X-ray; 2.03 A; A/B=37-250.
DR PDB; 4JGQ; X-ray; 2.63 A; A/B=37-250.
DR PDB; 4JGR; X-ray; 2.40 A; A/B=37-250.
DR PDBsum; 4JGO; -.
DR PDBsum; 4JGP; -.
DR PDBsum; 4JGQ; -.
DR PDBsum; 4JGR; -.
DR AlphaFoldDB; O31671; -.
DR SMR; O31671; -.
DR STRING; 224308.BSU13660; -.
DR PaxDb; O31671; -.
DR PRIDE; O31671; -.
DR DNASU; 939300; -.
DR EnsemblBacteria; CAB13239; CAB13239; BSU_13660.
DR GeneID; 939300; -.
DR KEGG; bsu:BSU13660; -.
DR PATRIC; fig|224308.43.peg.1442; -.
DR eggNOG; COG3852; Bacteria.
DR InParanoid; O31671; -.
DR OMA; YNGHIFI; -.
DR PhylomeDB; O31671; -.
DR BioCyc; BSUB:BSU13660-MON; -.
DR BRENDA; 2.7.13.3; 658.
DR EvolutionaryTrace; O31671; -.
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:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR033479; dCache_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; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF103190; SSF103190; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Sporulation;
KW Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..506
FT /note="Sporulation kinase D"
FT /id="PRO_0000375263"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 298..505
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 301
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT HELIX 40..79
FT /evidence="ECO:0007829|PDB:4JGP"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:4JGP"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:4JGP"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:4JGP"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:4JGP"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:4JGP"
FT STRAND 156..166
FT /evidence="ECO:0007829|PDB:4JGP"
FT STRAND 172..181
FT /evidence="ECO:0007829|PDB:4JGP"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:4JGP"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:4JGP"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:4JGP"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:4JGP"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:4JGP"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:4JGP"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:4JGP"
SQ SEQUENCE 506 AA; 56704 MW; 4A93A6A4500C179A CRC64;
MLERCKLKIL KGACGRVKLY IILVVIPAIV ISFFVYEKEK DTIAAEHKQE ASVLLNLHRN
KINYLIGETM ARMTSLSIAI DRPVDIKKMQ SILEKTFDSE PRFSGLYFLN AKGDVTASTT
ELKTKVNLAD RSFFIKAKET KKTVISDSYS SRITGQPIFT ICVPVLDSKR NVTDYLVAAI
QIDYLKNLIN LLSPDVYIEV VNQDGKMIFA SGQASHAEDQ KPVSGYLDDI SWNMKVYPNP
VTIEELSKSL VLPLSCIIVL LNILFILVLY YLLKRQTQLE RSENEAQKLE LIGTLAASTA
HEIRNPLTGI SGFIQLLQKK YKGEEDQLYF SIIEQEIKRI NQIVSEFLVL GKPTAEKWEL
NSLQDIIGEI MPIIYSEGNL YNVEVELQYL TEQPLLVKCT KDHIKQVILN VAKNGLESMP
EGGKLTISLG ALDKKAIIKV VDNGEGISQE MLDHIFLPFV TSKEKGTGLG LVVCKRIVLM
YGGSIHIESE VRRGTEVTIT LPVSAS
