ID A0A2D1U4G1_9SPHI Unreviewed; 1334 AA.
AC A0A2D1U4G1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CPT03_08345 {ECO:0000313|EMBL:ATP56482.1};
OS Pedobacter ginsengisoli.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=363852 {ECO:0000313|EMBL:ATP56482.1, ECO:0000313|Proteomes:UP000223749};
RN [1] {ECO:0000313|EMBL:ATP56482.1, ECO:0000313|Proteomes:UP000223749}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T01R-27 {ECO:0000313|EMBL:ATP56482.1,
RC ECO:0000313|Proteomes:UP000223749};
RA Weon H.-Y., Lee S.A., Sang M.K., Song J.;
RT "Whole genome of Pedobacter ginsengisoli T01R-27 isolated from tomato
RT rhizosphere.";
RL Submitted (OCT-2017) 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; CP024091; ATP56482.1; -; Genomic_DNA.
DR KEGG; pgs:CPT03_08345; -.
DR OrthoDB; 9809670at2; -.
DR Proteomes; UP000223749; Chromosome.
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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
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; IPR013783; Ig-like_fold.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
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; PF07494; Reg_prop; 4.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF07495; Y_Y_Y; 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; SSF63829; Calcium-dependent phosphotriesterase; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 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; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Kinase {ECO:0000313|EMBL:ATP56482.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000223749};
KW Transferase {ECO:0000313|EMBL:ATP56482.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 776..797
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 829..1045
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1082..1197
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1229..1328
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1130
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1334 AA; 152277 MW; 5D4213AB6FEC1944 CRC64;
MKKLITTALF LFVFLNLIKA QPYYFRHYQV EQGLSYNSVF SIVQDSKGFL WFGTKDGLNR
FDGYSFKVFR SKPGDTTSLR NNVIRAIFED AKKQLWVGTS NGLYCYNDTT QQFKLVPITI
NKGVWDMKSH GNGEICFIAD RKLYKYNKSK GAFQEFSKHQ DFEATATTFS KDGTLWVSSP
DGLLRKYNKA NDTFTSFNVF KDSAPVISHW IDKIYATESN SILIATSHQG VKLFDLATLS
YKDILTFNKD KTSIYAKNFI HNEGDEYWVA TESGVFVCNI KTGKYTNLRK NPNDPYAISD
NAVYTFAKDK EGGIWVGTYF GGVNYYPKPF TFFDKFFPQN NKRSLSGNAI REICNDKYGN
LWVGTEDVGV NKISSNGDFS AYIPDGSKTS IAHTNIHGLK AIGDELWIGT YEQGLDILDI
KSGQVIRHYD KSNQPNALKS NFVDCIYQTR SGEILVGTSY GLHRYNKATR DFSLITQVPH
DFHYTAITED DNGTIWTATI GGGLLYFNAK TNRQGIYKND PKNENSLSDN FVNGVFISAN
KMLWITTENG LNQFNPSDKT FKRYGTKDGF PSDVFYKTEE DKAGNLWISS SKGLISYNPA
SKKIRIYTTA NGLLSDQFNY NSSFQDAAGQ IYFGSVNGLV SFNPAKFKQN TIIPQVYITG
FQVFNQELLI NTEGSPLKKS ISYTDKIKLK YDQSTFSIDF AALAYTDHET AEYAYKLEGV
DKDFTYLKKN RRVFYTKLSP GNYTFLVKGA NSSGVWNETP RKLIIEISPP FWLSGWAYFL
YLILSIATVY ALVLYTNNKI KLRNKRRIEQ LENQKEKEIY EAKIEFFTQI THEIRTPLTL
IKGPLETVIK KYAPAPEVLN YLLTMEKNAD RLLHLTNQLL DFRKIESREY SLNLMKSNIS
EILREHYLRF KNAAEEKQIY FQLNLPQTEF YSNADEEALN KILSNLLSNA IKYSEKRVEV
LLLNPEPNTN QYTITVKNDG FLIPQEMRER IFESFVRLKE TSNQIGTGIG LALARSLSIL
HGGTLTFHAD ENDMNVFELN LPFYPSTPTF TEKPVQQEVI TIPIQQEQDF ETENITKEGR
PLILLVDDNA DILQFIAKEL GDTYNCITAS NGQVALDMLK DNAVQLIVSD VMMPVMDGYE
LCRQVKTNLD YSHIPLILLT AKSAFQSKIE GLEIGADAYI EKPFSPQHLQ VQIQNLLFNR
NQLKDYFVRS PLIHIKSIAH TKPDEILLEK LNDFIVKNIA NRDLDVDKLA ETLNMSRATF
YRKIKSVSNL SPNELINITR LKKAAELLVE TNYKIQQIAD LTGFTSQSQL GRAFTKQFGV
TPSEYANNFF RKNE
//
