ID A0A401U929_9BACT Unreviewed; 631 AA.
AC A0A401U929;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SanaruYs_16330 {ECO:0000313|EMBL:GCC51408.1};
OS Chryseotalea sanaruensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC Chryseotalea.
OX NCBI_TaxID=2482724 {ECO:0000313|EMBL:GCC51408.1, ECO:0000313|Proteomes:UP000288227};
RN [1] {ECO:0000313|EMBL:GCC51408.1, ECO:0000313|Proteomes:UP000288227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ys {ECO:0000313|EMBL:GCC51408.1,
RC ECO:0000313|Proteomes:UP000288227};
RA Maejima Y., Iino T., Muraguchi Y., Fukuda K., Ohkuma M., Moriuchi R.,
RA Dohra H., Kimbara K., Shintani M.;
RT "Chryseotalea sanarue gen. nov., sp., nov., a member of the family
RT Cytophagaceae, isolated from a brackish lake in Hamamatsu Japan.";
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:GCC51408.1}.
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DR EMBL; BHXQ01000003; GCC51408.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401U929; -.
DR OrthoDB; 9811889at2; -.
DR Proteomes; UP000288227; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19410; HK9-like_sensor; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR007891; CHASE3.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000288227};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 272..328
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 346..398
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 416..631
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 234..261
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 631 AA; 71392 MW; 16B21AB689629CE2 CRC64;
MRTDRIKILL VFSIILTVLS GIITYFAVIE SRKRVDLVLH SYSVLEKSED LLSMVSTAES
GLRGFILTKD STFLDNYSVA KNQYKALVED LKKLCLDRPG QLKIVNNGIE LYVSYKIRQL
AIVGTISQQY GLQKAIDYSY ARKDSLTINN LKNAIQDFNK NEEILLDERL TALNQTLATQ
TKIRYLSFFL IGLTLVFAYI TINEKQKKNN ELIDTLNKSN AVLEQKVKER TLELDRKNTI
VNELNAELQK SVEQIQAFYE SLQLKNRKTE DALIEVKDLY DNAPCGYHSV DQEGKIVRMN
RTELEWLNYS ADEVINKLAF TDLVTTESAI LFSRLYPEFK KSGSINNVEF ELKRKDGSTI
PIVLSATAIY DEAGNYLMSR STVFDISRRK DLEQKIIKVN DALIQLNVEK DHFLGIAAHD
LKSPLNSVLG LINLLKHEDS LNETQKEYLS IMERSCIGMK SLVSNLLDIN RIEQGGAALQ
KEKIEISHLL NTQKDIFKDV ALQKGIKLTL EDQTQNMSVH ADKDAMNRIL ENLISNALKF
SPASTQVKLE VSEVPTHVKF KIKDHGPGIS KNDLPKLFGK FQRLSAQPTG GESSSGLGLS
IVKELVELMK GKIRVETIEN EGTTFIVEIP K
//
