ID A0A1G6I2C5_9BACT Unreviewed; 1114 AA.
AC A0A1G6I2C5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05216323_101422 {ECO:0000313|EMBL:SDC00225.1};
OS Williamwhitmania taraxaci.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Williamwhitmaniaceae;
OC Williamwhitmania.
OX NCBI_TaxID=1640674 {ECO:0000313|EMBL:SDC00225.1, ECO:0000313|Proteomes:UP000199452};
RN [1] {ECO:0000313|EMBL:SDC00225.1, ECO:0000313|Proteomes:UP000199452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A7P-90m {ECO:0000313|EMBL:SDC00225.1,
RC ECO:0000313|Proteomes:UP000199452};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FMYP01000014; SDC00225.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6I2C5; -.
DR STRING; 1640674.SAMN05216323_101422; -.
DR OrthoDB; 717811at2; -.
DR Proteomes; UP000199452; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd14686; bZIP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
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; 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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
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; PF07694; 5TM-5TMR_LYT; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 2.
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; 2.
DR SMART; SM00091; PAS; 4.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000199452};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 126..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 198..254
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 326..396
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 399..451
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 572..647
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 651..705
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 758..975
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 998..1113
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 703..751
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1048
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1114 AA; 124950 MW; AE89611EB93D7CD5 CRC64;
MNLVSLVNNI TLLISISIVY SFISRRWNSH TSYHRILTGL LFGLTAIIGM LTPAQAIPGI
IFDGRTIILA VTGLFTGGLA TIIAMVIAMA YRISIGGPGI YMGVSTIITS GGIGLFFAYL
RQRKIIQYNW VTLLSAGIVV HIAMFLCTLL LPTSIRYEIT KGLIIPLTTI YPIGVLLVGN
LFLNQEQRIK SEQDLVSSQN SYENLVENVK SVIIKLNKEA QVIFINNHGI EIFGFETNEL
MDKMPLDTFI EKEDPAAKYF SPLGCSLIQV HESITVEGVS HTKSGDKLFL IWTFTAYTTD
DGTDEILCIG NNVTSLKGIQ NALRESKQIL KNIMDNTKDF ICQIDNEGNH LFVNRSYTTG
LGYAPDDLIG KPIIDFVHPE DRAIVIDSFK SVLMKKDNYL LTFRFRNANG EYTWIESIAT
TTYDSDGNVT GAVASSRDIA ERMEQQKALE YSELRYKALL FAIPDILFVQ SMDGFYLDVH
CSDPSKLLLP TEEFLGKHYS DVLPQYIIEK FEEKFELIKK KSQVELFEYS TEHNSSVLYF
VARIAPFGKD KFITIIRDIT DRKTAETQVK IEEEKYRLLA ENSSDVIWRM DAATQKITYV
SPSVFKLRGY TPEEAMAQTL EESMDKESFQ QIQSELPGRI HDFITGKEGA RTSITQIQQS
CKDGSWKWVE IATNIVTNEK GEISEIIGVS RDITLRKKDQ FELLENEQQL KQQNEEYLSI
NEELNESNTT IQAINEELTL AKEKAEESDR LKSAFLANMS HEIRTPMNGI LGFADLLRRP
NLSSEKSAKY IDIINTNGHQ LLSIINDIID ISKIEAKLIH VEQHPVNIGD LTNALNDQFK
PLAKAKGISF DAVNQFNTTT VVLTDEVKLK QIIFNLIGNA LKFTHSGNIK VSVIKADANL
LFSIKDTGIG IPKSHHELIF ERFRQVETTI TQQYGGTGLG LSISRSLVEL LGGNIWLESK
EGEGSNFIFS IPCIEIEDLN TKIAPQKDYE NINLSGKIIL IAEDEENNFL YLQEILQPTE
VTVIRAKNGE EAVRLAQTKP TPNLILMDIK MPILDGFEAT MKIRSTNASI PIIAQTAYAT
PSDRNKAINA GCNGFLAKPI SSQLLLQIVC DYIC
//
