ID A0A410JZS7_9BACT Unreviewed; 719 AA.
AC A0A410JZS7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EP073_09695 {ECO:0000313|EMBL:QAR33664.1};
OS Geovibrio thiophilus.
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Geovibrionaceae; Geovibrio.
OX NCBI_TaxID=139438 {ECO:0000313|EMBL:QAR33664.1, ECO:0000313|Proteomes:UP000287502};
RN [1] {ECO:0000313|EMBL:QAR33664.1, ECO:0000313|Proteomes:UP000287502}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11263 {ECO:0000313|EMBL:QAR33664.1,
RC ECO:0000313|Proteomes:UP000287502};
RA Spring S., Bunk B., Sproer C.;
RT "Geovibrio thiophilus DSM 11263, complete genome.";
RL Submitted (JAN-2019) 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; CP035108; QAR33664.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A410JZS7; -.
DR KEGG; gtl:EP073_09695; -.
DR OrthoDB; 9805967at2; -.
DR Proteomes; UP000287502; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
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; 1.
DR InterPro; IPR029150; dCache_3.
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; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF14827; dCache_3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000287502};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 312..383
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 385..437
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 475..714
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 719 AA; 82855 MW; DDD45C5466DE9FD7 CRC64;
MMAIFMFTAL TVVHVRNDLS SAIDYKHKKI EFMLSYQSDQ LERSLRSRFR ALLSDYYLRE
AMASKDRERI RLYFNEKYGA LVAEYHTEII IHIHDENGSS FMRMHAPGHL NYSGYPRPML
EEVADKKEPR FGFDLGCYGL HYRYAEPVYY MGVFVGIAEV GIGVDYLLSL MKNTLDLEMG
LFIPADKAEN LCFEPRAESL DGERLINVSN DDFVTIFNKA DFSKGVLTEI NEDGKFYRVH
MDHFLKGYNG QKIASLVTFQ DITNEKMAIT HYLRLAVIMA VIFICLTILM MKNSFMRIIS
DLEKKYKESK SRENYLGDII ANSLNEIFIY DIDTLRFVEV NRGACKNLGY SHEEILQMTT
LDIKPQMTFQ SFRKQILPVI EGEKETVMFE TVHRRKDGTL YPVEIHIQKT FVEGREVIMA
VVLDITQRKD AENRLKALNE ALEKKVDQET ERRLFSEKIM MEQKKFIDMG QMINAVAHQW
RQPLNALGLY VQDMRETHFS QGLDDSYVNQ IEKDCMHIIN HMSDTIDDFR RFFAPDKSSA
PFEIIRSVLE TIRLVSAQLM ASSIDYRIIC RCGDDSYFSE NSVESPGCLS RKTLVRGYEG
EFKQVMLNII HNARDAIIER RQSEAEGFQG FIEFDLDACG DNIVLSIKDN GGGIPENVIQ
KVFDPYFTTK EEGKGTGIGL YMSKNIVEQH MKGYLTAESK DGCAVFRLVL RSAAVKDDG
//
