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Database: UniProt
Entry: A0A0S2I3G4_9BACT
LinkDB: A0A0S2I3G4_9BACT
Original site: A0A0S2I3G4_9BACT 
ID   A0A0S2I3G4_9BACT        Unreviewed;       681 AA.
AC   A0A0S2I3G4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE   Flags: Precursor;
GN   Name=evgS_3 {ECO:0000313|EMBL:ALO16963.1};
GN   ORFNames=L21SP5_03350 {ECO:0000313|EMBL:ALO16963.1};
OS   Salinivirga cyanobacteriivorans.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Salinivirgaceae;
OC   Salinivirga.
OX   NCBI_TaxID=1307839 {ECO:0000313|EMBL:ALO16963.1, ECO:0000313|Proteomes:UP000064893};
RN   [1] {ECO:0000313|EMBL:ALO16963.1, ECO:0000313|Proteomes:UP000064893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L21-Spi-D4 {ECO:0000313|EMBL:ALO16963.1,
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; ALO16963.1; -; Genomic_DNA.
DR   RefSeq; WP_057954302.1; NZ_CP013118.1.
DR   AlphaFoldDB; A0A0S2I3G4; -.
DR   STRING; 1307839.L21SP5_03350; -.
DR   KEGG; blq:L21SP5_03350; -.
DR   PATRIC; fig|1307839.3.peg.3521; -.
DR   OrthoDB; 1116352at2; -.
DR   Proteomes; UP000064893; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF13181; TPR_8; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00028; TPR; 6.
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; SSF48452; TPR-like; 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000064893};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:ALO16963.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..681
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006599533"
FT   TRANSMEM        388..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          458..676
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          414..444
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   681 AA;  78126 MW;  C2195B6DE8F8630A CRC64;
     MKMSRFLFLA FIGALLFVLQ AANAQRPVEE EVKRVYHVAD SLYKLEDSHK ALDTLLSVLP
     DFNEFHNDSL ESKVLGLFGH LQKNMGNDTV GIGKFMQGLK SRQLRKYLNA VEAMGLYFER
     REHYTKALSY YKKMILFART LNDTLKLGEG YFKTGKMFKA LLNFPKANQY FNEALIYYKS
     SNAQQQIIKL YNQLGDMSAE MGQPDSAKIF FRKAISFARN TESATSRIIA YHRLAIIAGD
     NGNFNEALIY YENSKELATQ KEPKYLPSIY FDLASFFEKF GKTGKAEKAY KESMIYAAEY
     NNTAIQINAA KKLAELYALK NMNSRAVKYY QLSIMLADSM QQINSIQEMA RFEARYNLMQ
     KEQEIALLDR ERKLKAVKLK NQELRSKLYI GGLILLALLA AVLFYHIVTH IKKNRLLSEQ
     NAKINEQNEE LSQINQQLSE SENHLMQALS TKNKLFAIIG HDLKSPLMDI KNLIFILKNN
     AGQFGKDALK NHTGQIENRL ISLLELLNNL LNWGMTERDA LKYTPQKVDL VQLISKTIRL
     FDGMTANKNI SVRSNLPESI SWYTDFNMME FVLRNVLSNA IKFSEKDSQI DITATLDYDR
     LYISIADYGM GMTRDQLKKV FDRTSEKVRA GTQNEKGTGL GMSLTYEFVK QMNGVIDIDS
     RPNKGTRVEI TFEANDKRAI H
//
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