ID A0A3P2AM56_9FIRM Unreviewed; 474 AA.
AC A0A3P2AM56;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Histidine protein kinase SaeS {ECO:0000256|ARBA:ARBA00044126};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE AltName: Full=Sensor protein SaeS {ECO:0000256|ARBA:ARBA00044288};
DE AltName: Full=Staphylococcus exoprotein expression protein S {ECO:0000256|ARBA:ARBA00044353};
GN ORFNames=EII17_02575 {ECO:0000313|EMBL:RRD95676.1};
OS Clostridiales bacterium COT073_COT-073.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=2491044 {ECO:0000313|EMBL:RRD95676.1, ECO:0000313|Proteomes:UP000266937};
RN [1] {ECO:0000313|EMBL:RRD95676.1, ECO:0000313|Proteomes:UP000266937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT073_COT-073 {ECO:0000313|EMBL:RRD95676.1,
RC ECO:0000313|Proteomes:UP000266937};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Member of the two-component regulatory system SaeR/SaeS
CC involved in the regulation of staphylococcal virulence factors in a
CC strain-dependent fashion. Probably functions as a membrane-associated
CC protein kinase that upon sensing the appropriate signal,
CC autophosphorylates and in turn activates the cytosolic response
CC regulator SaeR. {ECO:0000256|ARBA:ARBA00043865}.
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 -!- 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:RRD95676.1}.
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DR EMBL; RQYD01000004; RRD95676.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P2AM56; -.
DR OrthoDB; 9786919at2; -.
DR Proteomes; UP000266937; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR45528:SF13; HISTIDINE KINASE; 1.
DR PANTHER; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RRD95676.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000266937};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 197..249
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 264..473
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 474 AA; 54039 MW; D015F483A1983F80 CRC64;
MKTSLKKKIF EMYFNMWIPF LVTLILAFYL LISHQLVQLR VEHLKNQSYQ SQIYAIQYLK
NAGKENGEVQ ALKKGAKHFA VYMAGVTGYR IQIYDKDGLL ADSDSQSGQL PETKDIQKSF
ETKAYSFFLQ HGMKYLSFSS PIISLLDNRM GQVIGSIRYV YPLQEERMFL LQVMGAICLL
SLGILIINGY FLRKNADSIT ESVRLLKEAA IQMQNGDLSQ EILISSADEM EELGVTFDLM
RCRLKEYISR LDEQSNQLQR FYNNVAHQLK TPLTSIIGYS QMIQISNDFD SICEDAFIIE
ESGEKLLHSI DVLLKGAKRE ALYVPLHISR FMIFEVVEDA ARLLKPRLDR LKVAVMNNCD
QAMIQSDREK IIEIILTLMD NALIHSECRQ IEFWTEVKAE KILLHFKDDG KGIAAQDEEF
IFNAFYQGDS SKGMGSGLGL SICFALAKDL AGSLQLKKSE RGAEFVIEIP NLKL
//
