ID B8GLL8_THISH Unreviewed; 497 AA.
AC B8GLL8;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE Flags: Precursor;
GN OrderedLocusNames=Tgr7_2496 {ECO:0000313|EMBL:ACL73573.1};
OS Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=396588 {ECO:0000313|EMBL:ACL73573.1, ECO:0000313|Proteomes:UP000002383};
RN [1] {ECO:0000313|EMBL:ACL73573.1, ECO:0000313|Proteomes:UP000002383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-EbGR7 {ECO:0000313|EMBL:ACL73573.1,
RC ECO:0000313|Proteomes:UP000002383};
RX PubMed=21475584;
RA Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL Stand. Genomic Sci. 4:23-35(2011).
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; CP001339; ACL73573.1; -; Genomic_DNA.
DR RefSeq; WP_012639048.1; NC_011901.1.
DR AlphaFoldDB; B8GLL8; -.
DR STRING; 396588.Tgr7_2496; -.
DR KEGG; tgr:Tgr7_2496; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_89_23_6; -.
DR OrthoDB; 9804645at2; -.
DR Proteomes; UP000002383; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 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; PTHR43711:SF16; SIGNAL TRANSDUCTION HISTIDINE-PROTEIN KINASE BAES; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 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; 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:ACL73573.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002383};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 183..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 203..255
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 263..479
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 478..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 497 AA; 55235 MW; 0A9D92FD0D0A8EB6 CRC64;
MASPLSFYRS LTILQLILLG FSLVTLPLAY ALTTALLSVE RLTDQSQQAV LDAVQAIQAS
RTLVEDVTAL ERHARQYQVL GDPALMEAYE ARRETLGAAL ERLYRLDLGP RVWEQLRLLE
RRETGAFEVL QGQAHDSEAV REALSVYPVL GELARGVFQD STRAVSREVE AMQAHSAEVS
QTLLWQASAL IPAVLALAAV FTVLIARPLR QLKFSIRALG AGRFDRPIRV TGPYDLADLG
ARLDWLRRRL VELEQQKVTF LRHISHELKT PLTNIREGAD LLSDQVVGRL NDQQAEIARI
VHDNSLQLQK LIEDLIRFSV ANTAMPVIES RPIRLDALIA ELVEQHKLAA RSRGVEIELA
LSGETVNSDR EKIRVILDNL LSNAIKFTRE HSSVQIHTGH YGEHVFVEIL DQGPGIPPAD
RERVFEVFYQ GDVRPRGHVR GSGMGLSIAR EYAKALDGRL MVMDADNGAR LRLELPRLGM
APPDQAGTQA QASGRAA
//
