ID A0A0S2I3S4_9BACT Unreviewed; 869 AA.
AC A0A0S2I3S4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=barA_7 {ECO:0000313|EMBL:ALO16887.1};
GN ORFNames=L21SP5_03273 {ECO:0000313|EMBL:ALO16887.1};
OS Salinivirga cyanobacteriivorans.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Salinivirgaceae;
OC Salinivirga.
OX NCBI_TaxID=1307839 {ECO:0000313|EMBL:ALO16887.1, ECO:0000313|Proteomes:UP000064893};
RN [1] {ECO:0000313|EMBL:ALO16887.1, ECO:0000313|Proteomes:UP000064893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-Spi-D4 {ECO:0000313|EMBL:ALO16887.1,
RC ECO:0000313|Proteomes:UP000064893};
RA Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT "Description and complete genome sequence of a novel strain predominating
RT in hypersaline microbial mats and representing a new family of the
RT Bacteriodetes phylum.";
RL Submitted (NOV-2015) 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; CP013118; ALO16887.1; -; Genomic_DNA.
DR RefSeq; WP_057954231.1; NZ_CP013118.1.
DR AlphaFoldDB; A0A0S2I3S4; -.
DR STRING; 1307839.L21SP5_03273; -.
DR KEGG; blq:L21SP5_03273; -.
DR PATRIC; fig|1307839.3.peg.3441; -.
DR OrthoDB; 9796457at2; -.
DR Proteomes; UP000064893; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; 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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF13426; PAS_9; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 4.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ALO16887.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000064893};
KW Transferase {ECO:0000313|EMBL:ALO16887.1}.
FT DOMAIN 251..286
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 315..369
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 370..418
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 491..562
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 563..615
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 654..869
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 606..647
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 869 AA; 98452 MW; 7738EB4D9995976A CRC64;
MPGKTNNIEE LKKLAKAFEW EIDLHKNTIW LEKNFGIQTG IDIASEVTIS ELSNYLLPHS
AKELSDQIIA IKEGLIEDLN INLSLKVQQN KIQKVQFNGR PNGEAKLIHG IGMAGTIEEK
SALTINLSNV LRHSEEGIII LDENDKIIEI NQAALGFASI NTEEFKNQNI GWYYKALNPE
GKQTGKALNF KQKNEGDSVV LQLKAANERK KHLKIKEKNL KEDNQNYKVL YISDITAQKK
AEAQSFLHSV ILEKAPVAII FTNPEGAIQF VNTAFSKITG YKLDEVKAQN PNILQSGVHD
DAFYDKLWST IKSGRTWQGK MLNKKRNGVL YWERAIITPH INEEGDLEGF IKVAEDITTQ
IETKQKLKES ETKYRDVFET AGVGIIYINK EGRVLDTNKK FNELLNTSEE SLINKSAIEL
INNKLPRPLA KELLSELFHV LKGNRIRPRA IQVYDKFYEI QSDYNPTLES NIGIIRDITD
KKLAEQKLKK SEAKYRYLVE NINDGLAITN KNNEITFMNP AAEQIFEVQP HQVGSKTLKD
IATPTSQEII SHEEEQRRMG NSSTYYIEVI TRKNSKKNLE INASPIYDTE RNFSGSFAII
RDITEKLKAE MEIKSANSQL KNINKKLQEH ATELEMAKDK AEESEKLKSA FLANISHEIR
TPMNGIVGFA QLAMNSSLSN EKRNSYLKIV SDSTMQLESV VMDIIDLSKI ESGESKFSKK
TTDLKEIIDS IYDFYIAEAR EKGLEFNMQY EGDIPKIKTD PIRYKQVVKK LVHNALKFTP
EGMVSVSAKL EKTSIAIIVK DTGIGIAAEY HDIIFEPFRQ VEQAMKRRFG GTGLGLTIAR
EIAKNLNSEI ELRSAPGQGS TFIFRHPMS
//
