ID A0A1M7RCP7_9BURK Unreviewed; 773 AA.
AC A0A1M7RCP7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05192549_12012 {ECO:0000313|EMBL:SHN44067.1};
OS Duganella sacchari.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=551987 {ECO:0000313|EMBL:SHN44067.1, ECO:0000313|Proteomes:UP000184339};
RN [1] {ECO:0000313|EMBL:SHN44067.1, ECO:0000313|Proteomes:UP000184339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sac-22 {ECO:0000313|EMBL:SHN44067.1,
RC ECO:0000313|Proteomes:UP000184339};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FRCX01000020; SHN44067.1; -; Genomic_DNA.
DR RefSeq; WP_072790250.1; NZ_FRCX01000020.1.
DR AlphaFoldDB; A0A1M7RCP7; -.
DR STRING; 551987.SAMN05192549_12012; -.
DR OrthoDB; 9146932at2; -.
DR Proteomes; UP000184339; 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:SHN44067.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:SHN44067.1}.
FT DOMAIN 7..118
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 295..492
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 494..628
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 651..767
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 54
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 700
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 773 AA; 84074 MW; 9809ED368294734B CRC64;
MSQDNNGDLS QFSMLDLFRM EADSQTQILT DGLLAMERLK DDASAVESMM RAAHSIKGAA
AIVGLEVVVQ LAHGMEDAFI AAQNGKLALT PNRVDVLLAG VDLILQLSRL QDSQVDAWLG
ANGEQIKRTM HAITTIAFLP EPVPLVPPPP PPAVAQPPAA KAAPEFPIGE LPIAPPPPAP
AAGAAEEAPA AAARHPAPMK HAQNFDKLLS LASESRINAH QMHPFIQNLQ RFKRNQSSLF
AVIEQLHEAI SNSTDASLKE KSLLALQKTH PLKQFVLEHI ADIEAYERRL LGVSQSMVDE
VLTMRMRQFR DGVQHFPRMV RDLARSLGKD VQLQIIGEDT LVDRDILAKI ESPLNHMLRN
AIDHGMDPAA DRIAVGKPGT GTIVLEAKHR AGMLSIEISD DGKGVNLEKI RARVIERKMA
PAQMASSMSG AELLEFLFLP AFSLKEGITE ISGRGVGLDI VHETIRSQNG TVRIESELGV
GFHTYITLPL TQSIVRALVV DVKGEAYAVP IVQVERVLKV PQSTIHTLEN KQFFDFGGEH
LGLVSAAQVL ELGATEAGSA ELAVVVIGTG ARRYALVVDA ISGEQSLAVQ AIDPVFGKMR
DISAAALLDD GEPVLILDVP DLLLSIDKLL HEGGLHQLAK SDAAERRKTK RVLVVDDSLT
VREMERKLLL ARGYLVDIAI DGIDGWNVVR SGDYDLVITD VDMPRMDGIE LVTLIKKDIH
LHKLPVMIVS YKDRPEDRAR GLSAGADYYL TKGSFHDETL LDAVNDLIGD AHR
//
