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Database: UniProt
Entry: A0A3N2KPK0_9BACT
LinkDB: A0A3N2KPK0_9BACT
Original site: A0A3N2KPK0_9BACT 
ID   A0A3N2KPK0_9BACT        Unreviewed;       910 AA.
AC   A0A3N2KPK0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-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=EEL39_09360 {ECO:0000313|EMBL:ROS87548.1};
OS   Muribaculaceae bacterium Isolate-080 (Janvier).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae.
OX   NCBI_TaxID=2486468 {ECO:0000313|EMBL:ROS87548.1, ECO:0000313|Proteomes:UP000277934};
RN   [1] {ECO:0000313|EMBL:ROS87548.1, ECO:0000313|Proteomes:UP000277934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate-080 (Janvier) {ECO:0000313|Proteomes:UP000277934};
RA   Clavel T., Strowig T.;
RT   "Sequence and cultivation study of Muribaculaceae reveals novel species,
RT   host preference, and functional potential of this yet undescribed family.";
RL   Submitted (NOV-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   -!- 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:ROS87548.1}.
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DR   EMBL; RIBG01000007; ROS87548.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N2KPK0; -.
DR   OrthoDB; 358279at2; -.
DR   Proteomes; UP000277934; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd06308; PBP1_sensor_kinase-like; 1.
DR   CDD; cd17574; REC_OmpR; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 3.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
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; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR018060; HTH_AraC.
DR   InterPro; IPR018062; HTH_AraC-typ_CS.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   InterPro; IPR025997; SBP_2_dom.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF12833; HTH_18; 1.
DR   Pfam; PF13407; Peripla_BP_4; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00342; HTH_ARAC; 1.
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; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR   PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000277934};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..910
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018281751"
FT   TRANSMEM        334..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          400..616
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          654..769
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          807..906
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   COILED          359..393
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         702
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   910 AA;  102428 MW;  4A75DD2ED178DBA6 CRC64;
     MKRIYLLFLT IISFSALLSS CHEKKTYRIG VSQCSQDDWR AKMNDEINRE IMFHPEATVE
     IRSADDSNEK QISDIRYFKD NGFDIIIAAP NEADAITPII KEVYESGTPV IIFDRNINGD
     SYTAYLGVDN FGIGKSAAHY GRHLIGKGGK VIEIYGLAGS TPAKERHDGF IEGATEEGIS
     VIASAYGNWN YDDAASVCDS MFTVCKDIDL IYAHNDRMAI AASEMAKKHG LDIKVIGIDA
     APEIGIKAVA DSVIDATFLY PTEGYRVIRT ALAILKGEPY ERVSTFPISS PVDISNADIL
     LLQNESLKED SAKIKTLKSQ VDDFWNKHSA QTSLFYAAIA IVVLLLGVLF LFLRIFWQRQ
     RHQKELMEQN RLLEEQRDTQ KALNEQLNVA TQSKLIFFTN VSHDLRTPLT LIAEPVEQLV
     KADNLTPQQH TLVKIAHKNV RILHRLINQI LDFRKYENGK LDINLEEVSL KPLLADWADS
     FLAIARKRDI KLNIAIHLPD NFSIAIDVEK IERVFFNLMS NAFKYTPDNG KIKFSANCDG
     SEKLVLSVAD TGRGIAAEDI DNIFDRFYQV DKIHPNGSGI GLSLAKAFVE LHEGSIEVES
     RLNEGSRFTV KLPIRHVAET RNFTTKKAIS GTDVETELGE IDTNRQQTDT DKPLLLVIDD
     NEDIRNMLRQ LLSDEYTVIF ASNGREGLRL AAKYVPDLIV CDVMMPVMDG LECCRKIKDE
     ISTSHIPVLL LTACSMDEQR AQGYESGADG YVAKPFNTTV LKSRCRNLIE NRRRIKNIWG
     NPSPMSVKTA ETPKPKVNPD TENEFYARFL EIVSAEMGNP DLNIDRLASD MGLGRSQLYR
     KIKALTNYTP VELLRNIRLK RSREMLTTTQ KSISEIAYEV GFSTPAYFTR CYKEAFGETP
     SELRDRIAAK
//
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