ID A0A1H8QXN6_9BURK Unreviewed; 783 AA.
AC A0A1H8QXN6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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=SAMN05428959_110118 {ECO:0000313|EMBL:SEO58761.1};
OS Duganella sp. CF517.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1881038 {ECO:0000313|EMBL:SEO58761.1, ECO:0000313|Proteomes:UP000198691};
RN [1] {ECO:0000313|Proteomes:UP000198691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF517 {ECO:0000313|Proteomes:UP000198691};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FODC01000010; SEO58761.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8QXN6; -.
DR STRING; 1881038.SAMN05428959_110118; -.
DR OrthoDB; 9146932at2; -.
DR Proteomes; UP000198691; Unassembled WGS sequence.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR CDD; cd00088; HPT; 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; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
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; IPR036641; HPT_dom_sf.
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 PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:SEO58761.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000198691};
KW Transferase {ECO:0000313|EMBL:SEO58761.1}.
FT DOMAIN 7..117
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 307..502
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 504..638
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 661..777
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 53
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 710
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 783 AA; 85159 MW; C084E232AC7A465A CRC64;
MSQDNNGDLS QFSMMDLFRM EADSQTQILT DGLLAMERLK DAAAVESMMR AAHSIKGAAA
IVGLEVVVQL AHRMEDAFVA AQHGKLALTP NRVDVLLAGV DLILQLSRLQ DSGLDAWLGA
NADDVTRTLD AITTIAFLPE PINLQAEAGL LPPIPAPVTA PPYFPPGELP VAAVSPAPAP
VPAPLSAPVP APAADEPPAA PAARMHAAPK AAQNFDKLLS LASESRINAH QMHPFVQNMQ
RFKRNQSSLF AVIEQLHEAI ANSTDAKLKE QSLVALQKTH PLKQFVLEHI ADIEAYERRL
LAVSQAMVDE VLTLRMRPFR DGVQSFPRMV RDLARTMGKD VRLEIVGEDT LVDRDILARI
ESPLNHMLRN AIDHGMDTAS ARIAAGKPGT GTIVLEAKHR AGMLSIEISD DGRGVDLEKI
RRRVIERKMA SAQMAGSLSP AELLEFLFLP AFSLKESTTE ISGRGVGLDI VHETIRSQNG
TVRIESELGV GFRTCITLPL TQSIVRALVV DVKGEAYAMP IAQVERVIKI PQSTIHTLEN
KQFFDFGGEH LGLVSASQVL ELGDTDAGGG ELAVVVIGTG ARRYALVVDT IRGEQSLAVQ
SIDPIFGKMR DISAAALLDD GEPVLILDVP DLLLSIEKLL HEGGLHQLTK SDHAERRKTK
RILVVDDSLT VREMERKLLL GRGFQVDIAI DGIDGWNVVR SGDYDLVITD VDMPRMDGIE
LVTLIKKDIH LHKLPVMIVS YKDRPEDRAR GLSAGADYYL TKGSFHDETL LDAVSDLIGD
ASR
//
