ID A0A1I2E981_9BACT Unreviewed; 1131 AA.
AC A0A1I2E981;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN04488541_100959 {ECO:0000313|EMBL:SFE89253.1};
OS Thermoflexibacter ruber.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Thermoflexibacteraceae;
OC Thermoflexibacter.
OX NCBI_TaxID=1003 {ECO:0000313|EMBL:SFE89253.1, ECO:0000313|Proteomes:UP000199513};
RN [1] {ECO:0000313|EMBL:SFE89253.1, ECO:0000313|Proteomes:UP000199513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GEY, DSM 9560 {ECO:0000313|Proteomes:UP000199513};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FONY01000009; SFE89253.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2E981; -.
DR STRING; 1003.SAMN04488541_100959; -.
DR OrthoDB; 9797097at2; -.
DR Proteomes; UP000199513; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR013783; Ig-like_fold.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
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; PF00512; HisKA; 1.
DR Pfam; PF07494; Reg_prop; 8.
DR Pfam; PF07495; Y_Y_Y; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; SSF63829; Calcium-dependent phosphotriesterase; 3.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:SFE89253.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000199513};
KW Transferase {ECO:0000313|EMBL:SFE89253.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 820..840
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 911..1130
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 849..904
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1131 AA; 128202 MW; 9AF95A0E7A7CF094 CRC64;
MSLKYIRIIL LLISCFSIYN TLLAQEKLLR FAQVYMEQKA ANSNILCIFQ DSKGFMWFGT
TDGLSKYDGY KFTIYKHIAN DSTSIINNQI HAIAEDSQGD LWIGTKSGLS KYRYAEEKFT
NIILDSQNQN INRIQTLAID NYGFIWLGTD GGGLMRFNPI DNKLSSFLYK LNDPRENAQL
KIRKISVDKL GNLWLATGYG LFHLDVKKQN QGTNAAFTHY VHNPSNNNSL ISNDLVSVLA
DQAGDIWVST SNGELNKLIF SEKKFLRQPY QVEGKNSQLF TNITSLCQSK DGIIWFGGYG
EGLNSISLTN GKLKRYLANK NELFSISSND ITAIYEDNAG ILWIATSGGG LHKLDRKASK
FEVYIRDEGT SNTLSQNNVK AVWEDKQGNI WIGTANNGLN RYNPTTKQYT LFENEPNNPN
SLSDNKINVL YEDTFGTLWV GTNGGGLNRL TFQDNQVKIV RYRYQEGSTN CIPNDVITDL
TSDADGNLWI ATADGLAKFK QRENIFTIYK RDIKFPNTLS SNSLRCIRFA STGDLWIGTD
GGGLNQMKVQ NAFFEEFRNN YLKQGSLPDD RIASLYIDRF GKIWVGTFDG DLNLLEPSKK
EFKNYASQHG IQSIVHGIIE DENNQFWLSG YNGLFIFDVI EQKVTRHYDI NDGLPSNEFN
LGAYHKGRSG KFYFGSLNGM IAFHPNYLEE SKSAPPIVIT DFKIANESVK LGKENSFFKK
NINIADEITL LDDNFSFSLE FAALDYTAPQ RIKYKYKLEA EGEENSQWVL TDASNRIATY
TNLPHGDYIF TVIATNSDGV WSTKGKSIKI YVKLPFWKTW WAKILLVLFI LTIVLVFYQY
RIYTIKKDKQ KLEQQVAERT EKVSQQKAEI ESQKHLLEEQ NHSLQQVNEK LRLSEQELSE
LNITKNRFFS ILAHDLRAPI NSMKGFSNLL ANFADQLSAE EIKSIAKNLD ETIIISSRYL
ENLLTWARSQ MNSIEFKPQP ILLKEAVYST TEVLKNNAQS KKITLEIEGD LEIKLFVDAN
QLNVILTNLV SNAIKFTYNG GKIIIGASMH EQDMAEIYVG DTGTGMPKEV VEKIFRIDSK
HTMKGTQGET GTGLGLLLCR EFVEKNGGKI WVESTEGVGS TFRFTLPIVH T
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