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Database: UniProt
Entry: A0A368JSD4_9BACT
LinkDB: A0A368JSD4_9BACT
Original site: A0A368JSD4_9BACT 
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
//
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