KINC_BACSU
ID KINC_BACSU Reviewed; 428 AA.
AC P39764;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Sporulation kinase C;
DE EC=2.7.13.3;
GN Name=kinC {ECO:0000303|PubMed:8002615}; Synonyms=mskA, ssb;
GN OrderedLocusNames=BSU14490;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / JH642;
RX PubMed=8002615; DOI=10.1128/jb.177.1.176-182.1995;
RA Kobayashi K., Shoji K., Shimizu T., Nakano K., Sato T., Kobayashi Y.;
RT "Analysis of a suppressor mutation ssb (kinC) of sur0B20 (spo0A) mutation
RT in Bacillus subtilis reveals that kinC encodes a histidine protein
RT kinase.";
RL J. Bacteriol. 177:176-182(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=8002614; DOI=10.1128/jb.177.1.166-175.1995;
RA Ledeaux J.R., Grossman A.D.;
RT "Isolation and characterization of kinC, a gene that encodes a sensor
RT kinase homologous to the sporulation sensor kinases KinA and KinB in
RT Bacillus subtilis.";
RL J. Bacteriol. 177:166-175(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969500; DOI=10.1099/13500872-142-11-3033;
RA Winters P., Caldwell R.M., Enfield L., Ferrari E.;
RT "The ampS-nprE (124 degrees-127 degrees) region of the Bacillus subtilis
RT 168 chromosome: sequencing of a 27 kb segment and identification of several
RT genes in the area.";
RL Microbiology 142:3033-3037(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Caldwell R.M., Ferrari E.;
RT "Sequence analysis of the mobA-ampS region of the Bacillus subtilis
RT chromosome.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=20713508; DOI=10.1101/gad.1945010;
RA Lopez D., Kolter R.;
RT "Functional microdomains in bacterial membranes.";
RL Genes Dev. 24:1893-1902(2010).
RN [7]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=22882210; DOI=10.1111/j.1365-2958.2012.08205.x;
RA Yepes A., Schneider J., Mielich B., Koch G., Garcia-Betancur J.C.,
RA Ramamurthi K.S., Vlamakis H., Lopez D.;
RT "The biofilm formation defect of a Bacillus subtilis flotillin-defective
RT mutant involves the protease FtsH.";
RL Mol. Microbiol. 86:457-471(2012).
RN [8]
RP SUBUNIT, INTERACTION WITH FLOT, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
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).
RN [9]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=168 / PY79;
RX PubMed=27362352; DOI=10.1371/journal.pgen.1006116;
RA Dempwolff F., Schmidt F.K., Hervas A.B., Stroh A., Roesch T.C., Riese C.N.,
RA Dersch S., Heimerl T., Lucena D., Huelsbusch N., Stuermer C.A.,
RA Takeshita N., Fischer R., Eckhardt B., Graumann P.L.;
RT "Super Resolution Fluorescence Microscopy and Tracking of Bacterial
RT Flotillin (Reggie) Paralogs Provide Evidence for Defined-Sized Protein
RT Microdomains within the Bacterial Membrane but Absence of Clusters
RT Containing Detergent-Resistant Proteins.";
RL PLoS Genet. 12:e1006116-e1006116(2016).
CC -!- FUNCTION: Phosphorylates the sporulation-regulatory protein Spo0A a
CC transcription factor that also controls biofilm formation (Probable).
CC Requires FloT and FloA for localization to DRMs and for activity
CC (PubMed:20713508). {ECO:0000269|PubMed:20713508,
CC ECO:0000305|PubMed:8002614}.
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 (PubMed:26297017). Another study
CC shows only rare colocalization with FloT or FloA membrane assemblies.
CC KinC membrane assemblies are more mobile than FloT membrane assemblies
CC (PubMed:27362352). {ECO:0000269|PubMed:26297017,
CC ECO:0000269|PubMed:27362352}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20713508,
CC ECO:0000269|PubMed:26297017, ECO:0000269|PubMed:27362352}; Multi-pass
CC membrane protein. Membrane raft {ECO:0000269|PubMed:20713508,
CC ECO:0000269|PubMed:26297017, ECO:0000269|PubMed:27362352}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Present in detergent-resistant
CC membrane (DRM) fractions that may be equivalent to eukaryotic membrane
CC rafts; these rafts include proteins involved in signaling, molecule
CC trafficking and protein secretion. Lost from DRM in the absence of
CC farnesyl diphosphate phosphatase YisP or when cells are treated with
CC YisP inhibitor zaragozic acid. Colocalizes with FloT in DRMs
CC (PubMed:20713508, PubMed:26297017). Another study shows KinC foci are
CC membrane assemblies of 85-110 nm, but found no evidence of
CC colocalization of these foci with FloA or FloT (PubMed:27362352).
CC {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:26297017,
CC ECO:0000269|PubMed:27362352}.
CC -!- INDUCTION: Induced at the onset of sporulation, shuts off at T3. May be
CC under the control of Spo0A. {ECO:0000269|PubMed:8002615}.
CC -!- DISRUPTION PHENOTYPE: No observable effect on sporulation
CC (PubMed:8002615). Forms a weak or no biofilm, wild-type sporulation
CC (PubMed:22882210, PubMed:26297017). {ECO:0000269|PubMed:22882210,
CC ECO:0000269|PubMed:26297017, ECO:0000269|PubMed:8002615}.
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DR EMBL; D37798; BAA07045.1; -; Genomic_DNA.
DR EMBL; D37799; BAA07049.1; -; Genomic_DNA.
DR EMBL; L34803; AAA66183.1; -; Genomic_DNA.
DR EMBL; AF012285; AAC24924.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13322.1; -; Genomic_DNA.
DR PIR; I39871; I39871.
DR RefSeq; NP_389332.1; NC_000964.3.
DR RefSeq; WP_003232333.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P39764; -.
DR SMR; P39764; -.
DR IntAct; P39764; 1.
DR STRING; 224308.BSU14490; -.
DR PaxDb; P39764; -.
DR PRIDE; P39764; -.
DR EnsemblBacteria; CAB13322; CAB13322; BSU_14490.
DR GeneID; 938742; -.
DR KEGG; bsu:BSU14490; -.
DR PATRIC; fig|224308.179.peg.1579; -.
DR eggNOG; COG3852; Bacteria.
DR InParanoid; P39764; -.
DR OMA; GVAQDEG; -.
DR PhylomeDB; P39764; -.
DR BioCyc; BSUB:BSU14490-MON; -.
DR BRENDA; 2.7.13.3; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
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: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; 1.
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; IPR000700; PAS-assoc_C.
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 PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Sporulation; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..428
FT /note="Sporulation kinase C"
FT /id="PRO_0000074779"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 76..147
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 148..200
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 221..426
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 224
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 428 AA; 48846 MW; 18B78E68FD933297 CRC64;
MRKYQARIIS IILAMIFIMF WDYLFYFIGK NPINWPVDIV YTAVTLVSVW MLAYYIDEKQ
QLVKKMKDNE WKYKQLSEEK NRIMDNLQEI VFQTNAKGEI TYLNQAWASI TGFSISECMG
TMYNDYFIKE KHVADHINTQ IQNKASSGMF TAKYVTKNGT IFWGEVHYKL YYDRDDQFTG
SLGTMSDITE RKEAEDELIE INERLARESQ KLSITSELAA GIAHEVRNPL TSVSGFLQIM
KTQYPDRKDY FDIIFSEIKR IDLVLSELLL LAKPQAITFK THQLNEILKQ VTTLLDTNAI
LSNIVIEKNF KETDGCMING DENQLKQVFI NIIKNGIEAM PKGGVVTIST AKTASHAVIS
VKDEGNGMPQ EKLKQIGKPF YSTKEKGTGL GLPICLRILK EHDGELKIES EAGKGSVFQV
VLPLKSDS
