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Database: UniProt
Entry: A0A2C9CH87_KUEST
LinkDB: A0A2C9CH87_KUEST
Original site: A0A2C9CH87_KUEST 
ID   A0A2C9CH87_KUEST        Unreviewed;      1193 AA.
AC   A0A2C9CH87;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=KsCSTR_44950 {ECO:0000313|EMBL:QII13874.1}, KSMBR1_2528
GN   {ECO:0000313|EMBL:SOH05015.1};
OS   Kuenenia stuttgartiensis.
OC   Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC   Candidatus Brocadiaceae; Kuenenia.
OX   NCBI_TaxID=174633 {ECO:0000313|EMBL:SOH05015.1, ECO:0000313|Proteomes:UP000221734};
RN   [1] {ECO:0000313|EMBL:SOH05015.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kuenenia_mbr1_ru-nijmegen {ECO:0000313|EMBL:SOH05015.1};
RA   Banno H., Chua N.-H.;
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000221734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Frank J.;
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:QII13874.1, ECO:0000313|Proteomes:UP000501926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSTR1 {ECO:0000313|EMBL:QII13874.1,
RC   ECO:0000313|Proteomes:UP000501926};
RA   Ding C., Adrian L.;
RT   "Newly sequenced genome of strain CSTR1 showed variability in Candidatus
RT   Kuenenia stuttgartiensis genomes.";
RL   Submitted (FEB-2020) 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; CP049055; QII13874.1; -; Genomic_DNA.
DR   EMBL; LT934425; SOH05015.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C9CH87; -.
DR   KEGG; kst:KSMBR1_2528; -.
DR   OrthoDB; 3272385at2; -.
DR   Proteomes; UP000221734; Chromosome Kuenenia_stuttgartiensis_MBR1.
DR   Proteomes; UP000501926; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 3.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 4.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 3.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 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; PF08447; PAS_3; 1.
DR   Pfam; PF13426; PAS_9; 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; SM00086; PAC; 3.
DR   SMART; SM00091; PAS; 3.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
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   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   SUPFAM; SSF103190; Sensory domain-like; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 3.
DR   PROSITE; PS50112; PAS; 3.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:QII13874.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000221734};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        314..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          338..390
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          395..452
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          471..523
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          542..579
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          615..667
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          830..902
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          907..959
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          972..1185
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   1193 AA;  134616 MW;  251B87F343F9EF00 CRC64;
     MFRSIRIKLI FFFLLAVLTP LLVMRLIAYP TARKAIHETT INNLQLITSK KAFLLNDRLK
     KIRRDAEHLA KNPFMAAAVC LAKADNTTTT RFVSLLSTEN NLHEFIISDI DGNICVSTDG
     SIIGLNIAGS KGFLQAGGGE ICFSETPPIT TFDTLEAQNW QAIFNTLYAY IPIKENGHIV
     GIVVLKSDLS FLSKEILEIP HGDNYAVHII NREGQFIAGL APGKLLHTTG NFAKEMPLKT
     LLTEPGTNQF TRSVKACLAG ANGYDMIGYV NNAGKTVLGA WHWVPELQWG IIVEVDADKI
     SLVMNELKNS ISKILSYLTV AGIIMAISGI AFAFITGQKI GTPILTLTKA TRKMSAGDFS
     QRVEINTRDE IQELGDAFNV MSASVQGKTT ALEEATNFLK SILVSSTEHS IIASDLCGNI
     LEFNEGATRM FQYAPEQMIN KSNIKMLYTR EEILSGKFQK ILKSALFTGS YKDEMKLVRK
     DGKTFTGYTT ITRRNSFSGS PTGYVIIIRD ITEQKLLEEE VNNYTVHLER IIEERTHKLI
     ISEEKYKRLF ESSKDVVFFC DINCQFVDIN QAGIELFGYD TKNDILQLNL IHHLFYKASE
     GKIIKETINK NGYVKDFEIA LKRKDGSKIP CMMTGSLRRD MRNNIIGYEG IIIDLTEWKK
     IEQEKDILNN INKILASRLD IREVYKSLSE EFHKVIAFDR LSIALLDEKR VEFLTFAVSK
     DYRFSELEEG VQYSKQGTLA GKVVEDGEFF VVHDTSRGPF STDPILSKEG IKSRLSVPLI
     CKGEIIGSLN FGSKKVNNFT EAHVDVINKI VPQLAIAIDN TRLFDRIKYS EEKYRNLVED
     IEDIIFRLDK NGRFMFLNNA LKNVTGYLPQ EFYDAPSLAF KIIHKDDVAL VKHITKEIIG
     GRTKVFKGLE YRVYCKNGKE LWFSQNTYPI KNKNGCVIGV EGIIQDITEK KKIEEQIRRS
     ERLASIGELA ASIAHEIRNP LGAISNSVCM LKRDLVLSDD DKNLFNMVVE ETEWLNNIIS
     NFLTFAHPAE YHFTKSDIAK MVEETLILLK KDARFNGNIR IKKNYSKALP KIFLDRIWIK
     KVFWNLLINS IDAMPNGGEI SISLKKTGVP NDDKIEIIIS DSGIGIPPER IKKIFEPFFT
     TKKSRGTGLG LSIVHRILDN HDGTIDVKSI QNRGTIFTIR LPLNNKKSRT VSV
//
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