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Database: UniProt
Entry: Q65EA4_BACLD
LinkDB: Q65EA4_BACLD
Original site: Q65EA4_BACLD 
ID   Q65EA4_BACLD            Unreviewed;       385 AA.
AC   Q65EA4; Q62PS4;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 2.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=Signal transduction histidine-protein kinase/phosphatase DegS {ECO:0000256|PIRNR:PIRNR003169};
DE            EC=2.7.13.3 {ECO:0000256|PIRNR:PIRNR003169};
DE            EC=3.1.3.- {ECO:0000256|PIRNR:PIRNR003169};
GN   Name=degS {ECO:0000313|EMBL:AAU25237.1};
GN   OrderedLocusNames=BL03360 {ECO:0000313|EMBL:AAU25237.1};
OS   Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS   NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010 {ECO:0000313|EMBL:AAU25237.1, ECO:0000313|Proteomes:UP000000606};
RN   [1] {ECO:0000313|EMBL:AAU25237.1, ECO:0000313|Proteomes:UP000000606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB
RC   9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46
RC   {ECO:0000313|Proteomes:UP000000606};
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA   Rasmussen M.D., Andersen J.T., Jorgensen P.L., Larsen T.S., Sorokin A.,
RA   Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:R77.1-R77.12(2004).
CC   -!- FUNCTION: Member of the two-component regulatory system DegS/DegU,
CC       which plays an important role in the transition growth phase.
CC       {ECO:0000256|PIRNR:PIRNR003169}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|PIRNR:PIRNR003169};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR003169}.
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DR   EMBL; CP000002; AAU25237.1; -; Genomic_DNA.
DR   RefSeq; WP_003185733.1; NC_006322.1.
DR   AlphaFoldDB; Q65EA4; -.
DR   STRING; 279010.BL03360; -.
DR   GeneID; 76975671; -.
DR   KEGG; bli:BL03360; -.
DR   PATRIC; fig|279010.13.peg.3860; -.
DR   eggNOG; COG4585; Bacteria.
DR   HOGENOM; CLU_000445_20_0_9; -.
DR   Proteomes; UP000000606; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR   Gene3D; 1.20.5.1930; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR008595; DegS.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   InterPro; IPR016381; Sig_transdc_His_kinase_DegS.
DR   PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR   PANTHER; PTHR24421:SF55; SIGNAL TRANSDUCTION HISTIDINE-PROTEIN KINASE_PHOSPHATASE DEGS; 1.
DR   Pfam; PF05384; DegS; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   PIRSF; PIRSF003169; STHK_DegS; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR003169};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR003169};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR003169};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR003169};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR003169};
KW   Protein phosphatase {ECO:0000256|PIRNR:PIRNR003169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000606};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR003169};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012,
KW   ECO:0000256|PIRNR:PIRNR003169}.
FT   DOMAIN          183..385
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          33..138
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   385 AA;  44636 MW;  290B26C78F29B4A8 CRC64;
     MSVSKMDSKV LDSIIMKMLK TVDGSKDEVF QIGEQSRQQY EGLVEELKQI KQQVNEVIDL
     GDRLEVHARH ARNRLSEVSR NFHKFSEEEI REAYEKAHKL QVELTMIQQR EKQLREKRDD
     LERRLLGLQE IIERSEGLVS QITVVLNYLN QDLRQVGVLL EDAQAKQDFG LRIIEAQEEE
     RKRVSREIHD GPAQMLANVM MRSELIERIF RDKGTEEGFQ EIKNLRQNVR NALYEVRRII
     YDLRPMALDD LGLIPTLRKY LNTIEDYHGK AKIHFQCIGE SEERRIAPRF EVALFRLAQE
     AVTNALKHSE STEIHVKVEV TKDFVTLIIK DNGNGFDLKE VKGKKNKSFG LLGMKERVDL
     LEGSMTIDSK IGLGTFILIK VPLSL
//
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