ID A0A1H6J8U9_9FLAO Unreviewed; 1198 AA.
AC A0A1H6J8U9;
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=SAMN05421793_11351 {ECO:0000313|EMBL:SEH58481.1};
OS Epilithonimonas hominis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Epilithonimonas.
OX NCBI_TaxID=420404 {ECO:0000313|EMBL:SEH58481.1, ECO:0000313|Proteomes:UP000198555};
RN [1] {ECO:0000313|Proteomes:UP000198555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19326 {ECO:0000313|Proteomes:UP000198555};
RA Varghese N., Submissions S.;
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; FNWX01000013; SEH58481.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6J8U9; -.
DR STRING; 420404.SAMN05421793_11351; -.
DR Proteomes; UP000198555; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19410; HK9-like_sensor; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR007891; CHASE3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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 InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SEH58481.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 220..272
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 532..754
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 811..924
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 933..1049
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1078..1195
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 432..508
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 860
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 982
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1128
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1198 AA; 135243 MW; 8BC6B3BE0C46B9A8 CRC64;
MPKKIIRNLQ VGVGFSLVIL IASSIASYLS IQNQMENREK LTASRRSITA AKDILVALLD
IETGNRGYQL TGRVSFLEPF NKGLEELPKS INRLKALNTD NNNQREVLDK LENNVKYNID
NIKIFVENRR KGIIMTQQQF MMSKSYMDRC RMLVNDFVRN EEKNLEIKNK DLTKSSNTTV
LFIILSAIAA IIVTAFFYRK MRADLIRRDK LEKELKAKDL EITRRVNAIK QIANKVASGD
YSQKATDNAQ DDLGDLVESL NHMTDSLKKS FDKINDSEWR QTGLVLLNES LVGNKSLKDV
SNESLKHFIE YTNCINGALY LNDDGRLKLK AAYGLEDRMK KIFDSGEGMV GQVFLEKKIK
VFNNINDSDF AVSFASSKVQ VNSILLLPIV SGEHNFGVIE LSSTENFSDQ KLEYFAEGSR
NIAVAIGAAK GREQEQRLLE ETQTQSEELM VQHSELENLN TELEAQTQKL QASEEELKVQ
QEELMQTNAE LEERSKLLEE KNMLIAERNA EIQRKVEELA LSTKYKSEFL ANMSHELRTP
LNSILLLSRL MAENPDENMN EDQVESAKVI QSSGTSLLTL IDEILDLAKI ESGKMTLEHQ
TIMLNDVVKD LKNLFDPILK QKSLQFNIII DEDVNKSIET DRLRLDQVLR NLLSNAAKFT
SKGSITLHIK NDPKQKGFVI FSVKDTGIGI PADKQKVIFE AFQQADGSTR RKFGGTGLGL
SISREIARLL GGELTLTSKE NEGSDFSLII PVIKKDDIEI TETDQNIVEI IKDDAEIIQN
ILSDNIISSK SLKIPDDVDD DREAIKEGDK VILIVEDDTN FAKALLKYSR LQDYKGVVVV
RGDLALSAAM QYHPSAILLD IQLPVKDGWQ VMDELKSTTA TRHIPVHMMS SLKAKQESLM
KGAVDFINKP VAMEEMNKVF RKIEETIRKS SQKVLIVEEN ARHASALSYF LSSYDIGLSV
ENNVEDSVKA LYSDKVDCVI LDIGAFRGKE YEIVESIKSN EGLENLPIII FTEHSLSTSE
ELKIKQYADS IVVKTAHSYQ RILDEVGLFL HLVAEKNNTE ETRSKTLGSL TEVLSGKKVL
ITDDDARNIF SLTKALEKYK VEVILAMDGK QALEQINKNP DIDVVLMDMM MPEMDGYETI
REIRKMPEYK RLPIIAVTAK SMIGDRDKCI TAGASDYISK PVDIDQLLSL LRVWLYES
//
