ID A0A6N9PW14_9BACL Unreviewed; 382 AA.
AC A0A6N9PW14;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 18-JUN-2025, entry version 21.
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=ERL59_01940 {ECO:0000313|EMBL:NBI27721.1};
OS Chengkuizengella marina.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Chengkuizengella.
OX NCBI_TaxID=2507566 {ECO:0000313|EMBL:NBI27721.1, ECO:0000313|Proteomes:UP000448943};
RN [1] {ECO:0000313|EMBL:NBI27721.1, ECO:0000313|Proteomes:UP000448943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YPA3-1-1 {ECO:0000313|EMBL:NBI27721.1,
RC ECO:0000313|Proteomes:UP000448943};
RA Yang J., Lai Q., Shao Z.;
RT "Chengkuizengella sp. nov., isolated from deep-sea sediment of East Pacific
RT Ocean.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000085,
CC 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:NBI27721.1}.
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DR EMBL; SIJB01000005; NBI27721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6N9PW14; -.
DR OrthoDB; 9781904at2; -.
DR Proteomes; UP000448943; 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; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR050482; Sensor_HK_TwoCompSys.
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; SENSOR HISTIDINE KINASE YDFH; 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:UP000448943};
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 176..377
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 54..131
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 382 AA; 44473 MW; FDA6CF211767FE70 CRC64;
MDAIDKVITR TMEVMDDSKY QIYEISESAR SELEVLNNEL IKVMGEIDKV ISIVDEFELK
FRDARNRLSE VSRDLHQYGE NDIRKAYETA NSFQIELIVY REKEKNLKDR RDELHQRIKN
IEGTIHRAEN VVSQMNVVVD YLKGDLNQVS RILETAKNRQ LIGLKIILAL EEERKRISRE
IHDGIAQSMA NLVLRTEIVE RMVSKKKYDT LMDEFIDFKN QMRSGLEEVR KIIFNLRPMA
LDDLGLVPAL RKYLHDFEEK YVINTSIDVH GHEIRLSSAM EVAIYRFVQE FCSNTYKHAE
ASQIKLDITF EEEMISITLE DDGLGFDVEQ MELKILGGSH YGIIGMRERV ELLEGEFEIR
SASNRGTQIT MKVPVNASEE KE
//
