ID D5H7D3_SALRM Unreviewed; 851 AA.
AC D5H7D3;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=SRM_01017 {ECO:0000313|EMBL:CBH23938.1};
OS Salinibacter ruber (strain M8).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC Salinibacter.
OX NCBI_TaxID=761659 {ECO:0000313|EMBL:CBH23938.1, ECO:0000313|Proteomes:UP000000933};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M8;
RA Pena A., Teeling H., Huerta-Cepas J., Santos F., Yarza P.,
RA Brito-Echeverria J., Lucio M., Schmitt-Kopplin P., Meseguer I.,
RA Schenowitz C., Dossat C., Barbe V., Dopazo J., Rossello-Mora R.,
RA Schuler M., Glockner F.O., Amann R., Gabaldon T., Anton J.;
RT "Fine-scale evolution: genomic, phenotypic and ecological differentiation
RT in two coexisting Salinibacter ruber strains.";
RL ISME J. 4:882-95(2010).
RN [2] {ECO:0000313|EMBL:CBH23938.1, ECO:0000313|Proteomes:UP000000933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8 {ECO:0000313|EMBL:CBH23938.1,
RC ECO:0000313|Proteomes:UP000000933};
RX PubMed=20164864; DOI=10.1038/ismej.2010.6;
RA Pena A., Teeling H., Huerta-Cepas J., Santos F., Yarza P.,
RA Brito-Echeverria J., Lucio M., Schmitt-Kopplin P., Meseguer I.,
RA Schenowitz C., Dossat C., Barbe V., Dopazo J., Rossello-Mora R.,
RA Schuler M., Glockner F.O., Amann R., Gabaldon T., Anton J.;
RT "Fine-scale evolution: genomic, phenotypic and ecological differentiation
RT in two coexisting Salinibacter ruber strains.";
RL ISME J. 4:882-895(2010).
RN [3] {ECO:0000313|Proteomes:UP000000933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8 {ECO:0000313|Proteomes:UP000000933};
RG Genoscope;
RT "Genome sequence of Salinibacter ruber M8.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; FP565814; CBH23938.1; -; Genomic_DNA.
DR AlphaFoldDB; D5H7D3; -.
DR KEGG; srm:SRM_01017; -.
DR PATRIC; fig|761659.10.peg.1128; -.
DR HOGENOM; CLU_335203_0_0_10; -.
DR Proteomes; UP000000933; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:CBH23938.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:CBH23938.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 49..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 214..284
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 332..373
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 404..456
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 632..851
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 605..632
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 851 AA; 94960 MW; DCADC22074AEC823 CRC64;
MDGPLGPPRS EDCIRRPRSG PPWQCAKPLS PKDASQFMNL FHALDPTHVT YLLVFGAGAV
GGLLGLMAFG FVGRPAETRR REAAPDGRQA ARNARLEALT ETMPGVPCEF RVGPDGEQSI
AFIGDGATEL LGLAPEPDGF YERFVEHIPE SHRGEFLRSV EEAVTTRSRW RQEVPFDRPD
GERIWLLGSA EPDPQDKGVL FRGLLLNITE RIDEKRRREQ VIRRVTDAIV EVDAEWCFTL
VNDQAEALYG MKEEHLLGRT LWDAFPRTKG TRFEEEYRWV MRSREPVRFE EHFERMGAWF
DIQIYPNPDG GLAFYFDDVT ERKEREEKLR EREELLRSIT ENVTEGIYRS TSEEGIVYAN
SAFVEMFGYE SRDELRAADP STFYADPAER EALYRQEDEQ GGLDGVEVQF QRNDGSTFTG
LLSTQQVDAP DGNQVYNDGA VTEITQRKRQ EQMLKSRRRK IEALYRATSG LLSVENRDAV
PGRIAEVLQE VFGFPLRHIG LVEGEMLVPK KTVGEDLSRM PEPKAQPLSE DLMATRAIQA
GEAVVVESTG GLENDIDYGT LSTLAGIPIG GHGAVVVGKE AGTFDALDLR LLEVLGGYAT
LVLGRLEREE RLVQAREEAE EAAQLKSAML ANMSHEVRTP LMSMIGSADL LREDLEEAGL
EGEPAEMAEQ IFRSGQRLRE TLDSVLELSR LESGAYTLDD DSAYLGVIVR EVAQELHLRA
HEKGVRLEVG GPGASVEVRL DETAVRRIVR NLVENAIKFT PEGGEVQVRV EPEDEETALL
AVEDTGVGIA EEAREDIFDA FKQESEGLDR EYEGSGLGLS IVDRLTTMLG GTIEVESEKG
VGTRFAVRLP R
//
