ID A0A1I2D3I5_9BACT Unreviewed; 1246 AA.
AC A0A1I2D3I5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN04488541_100649 {ECO:0000313|EMBL:SFE75076.1};
OS Thermoflexibacter ruber.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Thermoflexibacteraceae;
OC Thermoflexibacter.
OX NCBI_TaxID=1003 {ECO:0000313|EMBL:SFE75076.1, ECO:0000313|Proteomes:UP000199513};
RN [1] {ECO:0000313|EMBL:SFE75076.1, 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; FONY01000006; SFE75076.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2D3I5; -.
DR STRING; 1003.SAMN04488541_100649; -.
DR OrthoDB; 9797097at2; -.
DR Proteomes; UP000199513; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022519};
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000199513};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 17..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 44..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 73..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 261..314
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 388..440
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 462..532
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 532..588
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 589..663
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 665..715
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 732..955
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 979..1094
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1145..1240
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 438..472
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1028
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1184
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1246 AA; 142906 MW; A6F6E0204CBE3244 CRC64;
MFFSNNIQKQ DWQVIKIILL LGALMIPLAG HLCSFWLLDA KDSLVVRYFF ALESVLWVYF
FAQQKINDKV AYLWLYVHIF TLAIFFSFCL YINQLNYLYQ LQYLIVCVAL SFCIRSFRLI
LIFTLFNVAF LGFMAFSLED SLYTAYAFCI AALALMSITL AFHLPFIKLL SNLQNSWEAL
EKSQTALEDS ERYMKAFLNS TEEGIIILSI DKKVMIFNNI AKVLAKTFAN LTLEKGVLFD
KFFTSKSRLD SFKYSFNSAL SGERVKVIEK SYGGQKWNAY SYTPIYNEQE KIWAVGIAIA
DITKEKAYED ELRKAEEMYR QILNAVEEHI IVKERGSKYV WANQAFHDFY QMSLEQFSKF
SEGIFENKAI EQRHNQDDEY IFETGQSITT SESLRRYDGQ ERIFQTVKSP IKDAEGKVTM
TVSVARDITE QFKMEKALRQ SVEEVEELFK QLVKSRDELA ESERKLRLLA DNSAEMISLC
TPEGVITYLS PSSERLTGYS RTYLYGKNLV DFFHPDDIHP VQIASQEQVS QNIKEVHLTH
RFKCSAGNYI WVDSIFKYIF DEDGEVLNLQ TSSRDVSSRV AAERALQSSE AKFRELFNSG
YDAIFIFEIL ENGLPELIEV NQIACQMFGY TPEEFLRQKI RDLEPLLSRE VLQERIQILL
KEKSLSYETT LRSKQGNLVP VEIVNTFSKY ADHQVVQAVV RDITERKKIE KIQREKEIAE
QALKIKSNFL ANMGHEIRTP MNGIIGMAHL LTSTSLTAKQ AIYTKAILDS SQNLLNILND
ILTLSQIEAN KVVLNTKAFH LQRLIRNLKQ LFAPLLMQKH LHFFADVDDN VPAYIKADET
KLLQVLTNLL SNAIKFTHQG KISLRVEILN KDEISQHYWL KISVSDTGKG IPQSHQQAIF
EHFYQVENKS EGKNEGAGLG LAICKELVTL WKGEIGVKSI ENQGSTFWFT IPVQKEAKPQ
PQILTQKMDF SSIRFLETKV LIAEDKKVNQ EIIKIMLEEK GCVVEIANHG AEALQLAKEK
SFDLIIMDIL MPVMDGLEAT RQIKEKVSKS PIIIGLSANT VEAEVQNYLA QGMDDYLAKP
IVPDLLYEKM AYWLADKVSS SNNESDTEKN ALLEKMNLKK ESNHEEINLI NIKTVEKIKI
LSKNNQKYIA SLYQSFKEDV ENLIKEAHKS IHLQDKVQLA RHVHTLKGLT GTIGASALYS
IVSEFYIKLK NNELENETEE NLLATLQAIQ HTFQQTCPLL AQSLGI
//
