ID A0A3D8LEY6_9BACT Unreviewed; 1747 AA.
AC A0A3D8LEY6;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DXT99_07675 {ECO:0000313|EMBL:RDV15866.1};
OS Pontibacter diazotrophicus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=1400979 {ECO:0000313|EMBL:RDV15866.1, ECO:0000313|Proteomes:UP000256708};
RN [1] {ECO:0000313|Proteomes:UP000256708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4X {ECO:0000313|Proteomes:UP000256708};
RA Liu Z.-W., Du Z.-J.;
RL Submitted (AUG-2018) 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: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDV15866.1}.
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DR EMBL; QRGR01000007; RDV15866.1; -; Genomic_DNA.
DR OrthoDB; 9797097at2; -.
DR Proteomes; UP000256708; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 5.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
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; 6.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR013767; PAS_fold.
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; 4.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13426; PAS_9; 4.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00086; PAC; 5.
DR SMART; SM00091; PAS; 5.
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; SSF55781; GAF domain-like; 2.
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); 6.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 4.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000256708};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 137..183
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 557..611
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 632..684
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 685..755
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1103..1170
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1174..1226
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1244..1465
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1494..1610
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1651..1747
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 1543
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1690
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1747 AA; 199157 MW; 9F21E94E8DA4E1C7 CRC64;
MPFLPNPKTG ATLTQNANAL LQVLEQLTEP SHGLAIAQPD GCMLAVNAQA KNFTSNNLNG
NGSTAYNLQE LLHLTQEECS MMLESLMQQR VLSGKTLNIP TQTYPAFTYN ARLMHYQEEA
FVCVELALIT QPAEFVSDDS YHHVFDGSTE PLFLLDSAGC FIDINQNALN LLQLEKEALI
GKSVSNSFQL NLFERVALKK QLQLALQGTK QKFEWWLHET DNNLLPVEIT LQKGVFQNQE
VLYGAVKNLN EVIHSEQDIR FRNHQLEFVN QLITNLSSSD SQYEVLHNTL NELLEKSDAS
GGCVFTCVPD AGKFILSYSA GEPGSHPLPD ELPVEQTLMS QLLTKDKPKA LASLQEHLVA
TMHRQVTLVP ITTEKEVLSL ILVWTGDDHR MTPSFVALLD FIGTAIGQYI ARHQLEEQLT
FSEDKYRLLF ESSYDAILLF KNGVVVECNE KAIEFFRCTR EDLIGHGPSA FSPELQPDGT
NSTQKAERLM QEVLSTGRPM TFEWKNRRKD GTLLDAEISV SRLLLNGEYY LQAFKRDITQ
RKQTQLAKRR EEVLRESMDQ FRNFLDKVNL IYYSLDKNGN IAFTNNYFLK YVEYSHEELI
GKNFFDILVP EHERAQRLQD HFNRLETKQL NSYYERDIIT KSGQLKTLRW NSMFEYNQEG
KVTGVTSVGK DMTDKRIAME ALKDNKIRLQ DLFDNAHDLI QNISVDNKFI FVNKAWKDRL
GYTDEDIESL TLNDIVHPYY KAKLIYQLRN LYKGENVNKI ETVFLTKAGK PVHLIGSITC
SWQDGRPVAT RAILHDITDR IKAERLQKVY YSIANLAISS KDLNSLYSAI HRELSKIIET
RNISIALVEH EQKYLNFVYL VDQYIDKAAR PHLGRPFSTG LSEYIIQTGK PLYMQKQALL
DLEVRENLTL FGATPEVILC SPLAIGDRII GVIMLQDYQN ADAYVPTDIE ILHFISNQVA
LAIERKRNEE QINNQNARLN AIFESGTHHM WSMNRHYELT SFNRNFADSF ESRSGQVLQP
YTRIDDNSIV AVHESTYEFW EEKYKQVFNG HPQHFEVYIQ QTGIWREVFL SPIYLSDGTF
EEISGMALDM TDKKMAQLAL ANNEKKFRRI FESFQDVYYR SSLEGVIELV SPSIAQLLGY
TEEEVLQKKT INFFANLKDL ARLRRRVLEE QSFRDMEVEL ICKDGEHKTV LIDSRLTYDE
HGKPAALEGV ARDVSELKRT QKALLKAKEE AENLLKVKTQ FLANMSHELR TPMNGIIGMI
DLLNQVNTDP EQSEYIDTLR KSSDALLAIL NDILDLSKIQ AGKLVTHDSG VDLHETLGKI
HSLFVNRAQQ KDLSFDYTIS PNTPRYVYTD ETRLTQILSN LTSNAIKFTN AGNVSISVDA
EQLDQTYYRL HVRVKDSGIG ISPEDQQLLF NDFMQLDNTS TKTFGGTGLG LAISKQLTHL
LGGDIGVESE GRAGSVFWFD IKVRQANAAE VKEQQQRQQL HESTEPKTLS NPPFVLLVDD
NQINQRVAQK LLERLGCIIN TASNGYEAIE LATSNQYNII FMDIQMPEMD GVTATRIIKE
KLGKACPPIV AMTAYSMKDD AEKFMGQGMD DYVSKPVKGA DLHAIIVKWE QHGRYDQHNT
GAQHDIAPEE VPAVESIIDL EVVDQLKQIG GPDFVHQLYA EFEEEAALLL EEVKKDLESQ
HYNGILSTLH QLKGTGFTLG IVLLAELAKQ LEHDIKQNHL EHIDENFSKL QSHYENYRKS
YKEIILC
//
