ID A0A368JSD4_9BACT Unreviewed; 1240 AA.
AC A0A368JSD4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DUE52_08515 {ECO:0000313|EMBL:RCR69876.1};
OS Larkinella punicea.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Larkinella.
OX NCBI_TaxID=2315727 {ECO:0000313|EMBL:RCR69876.1, ECO:0000313|Proteomes:UP000253383};
RN [1] {ECO:0000313|EMBL:RCR69876.1, ECO:0000313|Proteomes:UP000253383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=zzj9 {ECO:0000313|Proteomes:UP000253383};
RA Zhou Z., Wang G.;
RT "Genome analysis of Larkinella rosea.";
RL Submitted (JUL-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:RCR69876.1}.
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DR EMBL; QOWE01000006; RCR69876.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368JSD4; -.
DR OrthoDB; 9811889at2; -.
DR Proteomes; UP000253383; 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; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 3.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 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; 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; 3.
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; SM00086; PAC; 3.
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; SSF55781; GAF domain-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); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 3.
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 Coiled coil {ECO:0000256|SAM:Coils};
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}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 54..109
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 168..238
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 532..585
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 586..641
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 656..708
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 726..947
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 974..1096
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1137..1237
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 689..716
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1029
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1176
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1240 AA; 139969 MW; FE4495260DA9988F CRC64;
MSWTAKTKNE LVAEIRRLSK EVDIRNSLDG SSQLSHASVF DVSKTVDQLN LIGLTIEKDG
TVTFCNQYTL RITAWQPTDV IGKNFFEIFI PAGERVQMQR DFDDAIARGG VVEQKEINLL
AKSGAVRNVQ LNSFIINTVA DHTSVPSYTI IGEDVTNKKR VASALSYSNS QLQDLVDNTS
DLIQLVTLDG KFMFVNRAWR EVLEYSSDEI ASLTLQDVLH PDYAESTLMR LQRVRDGEKF
PYFETVFQSK KGKTVFVSGS VNCRYDQGKP TAYRCILHNI TSRIRAEKAQ KLYYSIANWT
LNAPNLDELY QNIHDELSNI IDARNFFIAL YDQSKSFLYF PYYVDEYFTG MRFTKRRLGN
GLTEYAIRAN RPLFLYEQDI QQLADTQNLY LYGQIPKAML CVPLRIGDRI TGIIGVKAYD
KADTYNIRDL ELLEFISGQV ALAIARKQDE AAINKQTARL NAIFDSSSHL IWSVNKSFQL
TSFNRNYTRL IENQLGEIPQ LNVTTEKLGW RIIGAENRRL LEEKYRLAFR GLPQTVELHY
QTTKSEAWLE VHLNPILLSG GVIEEVSGIA RDITARKRTE LELRGSEEKF RGIFVNLQDI
YCRVDREGLV TMISPSVLKR TGYTPEEVLG QPITNFIDKQ DIRRALVRLI RNKSLRNFEA
TLHRKDGTIR QIMLNMLTLN DKNGRVDEVA ALARDITELK RNAQELMKAK DEAERSLKVK
ERFLANMSHE IRTPMNGVIG MIDLLNDTPL DQDQKDYVQT IKKSSETLLN ILNDILDLSK
IEAGKMVLHE APILFREVFD KLVSLFGQQA SVKGNKLSYH LDDKLPQFVI ADQTRLLQIL
SNLTSNAIKF TENGAVTVEA SLVSRKGKFN RIKVEVKDSG IGIAKDDLGL LFNSFSQVEM
SSRKSFGGTG LGLAISKELA ALMKGTIGVE SVTGKGSNFW FTIELKETLI SPTNQKSDQA
EISLQNVFID HHPYLLLVDD NAVNRKVATE ILKKSGCQVE TASSGQEAID KVTVAMAENG
KPYELIFMDI QMPDMDGVET TVKLRSLFGP QLPPVIAMTA YSMREDRDRF LSQGLDDYIA
KPIRAQSLIS KVKETVDARK DFREAAQMRS KQLETIRELE MPMVDTEIIG QLEQVGGWDL
VTSIYEDFEI EATTLVQESL DAFAIGDIPT VKSHLHTLKG SAGTIGVARI AQVAREAEGK
LKLSDSSTLA DDLHLLDKEF KLFLSEYKNT LEKLVAEKAG
//