ID A0A061P9V3_9BACL Unreviewed; 378 AA.
AC A0A061P9V3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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 ORFNames=JCM19039_1334 {ECO:0000313|EMBL:GAK11627.1};
OS Geomicrobium sp. JCM 19039.
OC Bacteria; Bacillota; Bacilli; Bacillales; Geomicrobium.
OX NCBI_TaxID=1460636 {ECO:0000313|EMBL:GAK11627.1, ECO:0000313|Proteomes:UP000027177};
RN [1] {ECO:0000313|EMBL:GAK11627.1, ECO:0000313|Proteomes:UP000027177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19039 {ECO:0000313|EMBL:GAK11627.1,
RC ECO:0000313|Proteomes:UP000027177};
RA Kudo T., Nakahara T., Zhang X., Taniyama S., Arakawa O., Murase S.,
RA Nakata H., Oshima K., Suda W., Kitamura K., Iida T., Oshida Y., Inoue T.,
RA Hongoh Y., Hattori M., Ohkuma M.;
RT "Draft Genome Sequences of Geomicrobium sp. Strains JCM 19037, JCM 19038,
RT JCM 19039, and JCM 19055, Isolated from Aquatic Samples.";
RL Genome Announc. 2:e00622-14(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAK11627.1}.
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DR EMBL; BAXB01000004; GAK11627.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061P9V3; -.
DR Proteomes; UP000027177; Unassembled WGS sequence.
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:UP000027177};
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..377
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 4..56
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 93..134
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 378 AA; 43511 MW; C9068971CBD2FD3B CRC64;
MSSKKSLDQI IEQMMETVRD SKEQIFEICE KTRKEYAGLE VELKDLRLKV ARLFDKQDYK
EMHARLARNR LAEVSKEFGK YSNEEVRKAY EHANEHQIQL AVLNQEEKQH RERRDHIERR
LLELEDTISR AELLVGQVSV VHNFLIGDLR EVGEIVEDAK EKQEFGLKII EAQEAERKRV
ARDIHDGPAQ LLANVLLRAE LIERAYNDQG IESALKEVKD VRHAIKASLA DVRRIIYDLR
PMALDDLGLI PTLKKYLSSV SERVEDKTEV RFIVIGNETR MEPNLEVALF RLVQEAVQNG
LKHAEANQIL VKVQVTTDRI MLIISDDGKG FDHTEKKDDS FGIMGMKERV NMLKGEFAIE
SVMGRGTKLV ITVPTSDD
//
