ID A0A0S2I3U3_9BACT Unreviewed; 801 AA.
AC A0A0S2I3U3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=zraS_2 {ECO:0000313|EMBL:ALO16948.1};
GN ORFNames=L21SP5_03335 {ECO:0000313|EMBL:ALO16948.1};
OS Salinivirga cyanobacteriivorans.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Salinivirgaceae;
OC Salinivirga.
OX NCBI_TaxID=1307839 {ECO:0000313|EMBL:ALO16948.1, ECO:0000313|Proteomes:UP000064893};
RN [1] {ECO:0000313|EMBL:ALO16948.1, ECO:0000313|Proteomes:UP000064893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-Spi-D4 {ECO:0000313|EMBL:ALO16948.1,
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; ALO16948.1; -; Genomic_DNA.
DR RefSeq; WP_057954287.1; NZ_CP013118.1.
DR AlphaFoldDB; A0A0S2I3U3; -.
DR STRING; 1307839.L21SP5_03335; -.
DR KEGG; blq:L21SP5_03335; -.
DR PATRIC; fig|1307839.3.peg.3504; -.
DR OrthoDB; 1931120at2; -.
DR Proteomes; UP000064893; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
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; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
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; 3.
DR SMART; SM00091; PAS; 3.
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; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000064893};
KW Transferase {ECO:0000313|EMBL:ALO16948.1}.
FT DOMAIN 3..44
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 78..130
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 208..257
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 258..330
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 569..801
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 491..553
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 801 AA; 92075 MW; FAD7783F36586829 CRC64;
MNEFKNIEQL FENAPIGIFE TTIDGKFVDL NTEFVRILGY ESKQDVFQHI KRLEYDLYEF
PGLRNEILES IAQKNKLSVF EVRFKQKNGN LIDVRMSIRH HYNEQMKQTN NIGIIEDITE
KVRTEAKRKE QEKKYKTLFE NSTDAILIIK HPDIIEWNTK AHDLFCGNIE CNGIPDFNTL
HPEKQPDNQN SLKKATRLIE KTLNGEPQFF EWELKKVSGE TFFAEITLSL LDSEKKLTQA
IVRDITERKK AEQKLSESEH KYRKIVETAP DGIITVSKAG IMLDVNNSFC ALTGYPKEKY
LNNHYDVFTG LTEESKKSSY ALFNSLLNNE PVKPIEIQWT HQKGELKTGE VRAIAFYDQN
RDFVMQVNLR DITLQKRAMQ TIVKRESLLN SIFNSIPLEL WVLDKNKNIL AQSGFSKNKW
GDYIGKNATE FPAIVDKERY DEILKQVNKG EVVEFVGEFS LENKRKYFKS VLAPYYENAE
IKGHIAFSLD ITELKQMQKE LESHKHNLEA LVEQRTEEIQ ALNEQLTDSN EKLEFQRDEL
KNALSKLQST QNQFIHTEKM ASIGILTAGI AHEINNPVNF IHSGIMGLEI MLSDLMTELK
DVIKTKKQST NNLNINRYSE KTTELVKAIK TGVNRITNIV NGLRTFSRMD NEEKSPVDIE
ETINSSLIIL QNKFKYNVEI SKKLAENNTV NGFPGKMGQV ILNIIMNAIQ AITDTGNIEI
RTRRNDQKNE FKIIVQDDGI GMDKTTQEKL FDPFFTTKKP GEGTGIGMSI VHTIIEDHNG
KIHIDSEPGK GSVFTIVLPI E
//
