ID A0A1I7LXN5_9BURK Unreviewed; 1321 AA.
AC A0A1I7LXN5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05216552_10422 {ECO:0000313|EMBL:SFV14360.1};
OS Pseudoduganella namucuonensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Pseudoduganella.
OX NCBI_TaxID=1035707 {ECO:0000313|EMBL:SFV14360.1, ECO:0000313|Proteomes:UP000199391};
RN [1] {ECO:0000313|Proteomes:UP000199391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.11014 {ECO:0000313|Proteomes:UP000199391};
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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FPBO01000042; SFV14360.1; -; Genomic_DNA.
DR STRING; 1035707.SAMN05216552_10422; -.
DR OrthoDB; 5290456at2; -.
DR Proteomes; UP000199391; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.450.350; CHASE domain; 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; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
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; IPR007895; MASE1.
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 InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF05231; MASE1; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000199391};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 615..632
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 446..552
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 657..729
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 731..783
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 801..1022
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1186..1302
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1302..1321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1237
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1321 AA; 139830 MW; E3EC2ABC210AC429 CRC64;
MDAHTQGTPE RKLPFVAGLL LCAAIYYCLA RLGLLLALES SNASPVWPPS GFALAIMLRH
GRRMWPAVLA GAFLANLAVF ANNQVAGAAV IAAASIAIAA GNALEGVAGA WLLGRAGVAG
ARLETHQDVY RYGAIIALAA ALAAAAGSCT LWASRIVRPE LLPHVAGTWW VGDFLGMLII
TPLLLALPRG RAHARRAIAD LKGALPLAAA TVAAASLLFL TPPDTWRVPP PMPYALLLPV
VWAAVRHGRA AVQLVLALIC GIAVPATATG HGAFVSGVLH HSLVSLCTFL AIVALVAMVL
GADAPRDGAA VLPERPRPSW TPVLALCICL GLTVLAWAFV NADTERRTRE RFGNAAEAVR
EKLAARITSY ETLLRSGAAL FDASSEVDRD EWRRFVDALD LRRNYPGVLG LGYARYVRSP
AVIGEQAWWR EYGQLGLRIW PKGERELYVP VTYLEPVNPR NIAAIGFDMM SEPVRRRALA
AAIQNGRLTA SGPVTLVQET TRDKQTGFLM YNPVYPTDTT AGPMFHPTGF VYSPFRMRDM
MEGVFGASLR ELRLEILDGS PNGAPMYDSR VAGDAPSYLA MASTAHVAVG ENGKLWALRI
TPTALFDASV DQAKSYIVLV LGTMISMLFY AVSRSLVRAR HQAQVDVVRS AASLEQSEAR
FKLLTANIRN HAIVLLDPDG AITTWNDGAV KLFGYPPERA IGQPVALLHG AAADAPRPGS
GLEVALRQGQ YEETSERVRQ DGGRFTALTQ IFPARGRDGA CIGYAMIVRD VTHELAAAKE
LDDARIQAEA ASAAKSAFVA NMSHELRTPM NAVLGLTQLL GKTPLTGEQS QFVQMISVAG
KSLLAVLNDV LDFSKIEANK LEVMIEDFYL DDVIDAVASV MAVNAGEKAL AVSIHVDADV
PASLRGDAQR LQQILINLAS NAIKFSEQGS VGLRIHTETD AGGRSWLRCE VSDTGIGMAP
EQIERLFIPF QQADASMARK FGGTGLGLTI SKSFAKMMGG DIGVRSAPGA GSTFTLSLPL
LEGALADKYA LPAALRGLRM LYLDTDARRR DGMRELAARW DLGFQAAATP GAAGPLLEEV
DAGGPAFDMI VFTAEFAPLV ATLRTSAGPS RLAGNGPLRV RVSRVFQPGH PAEAHAADAV
LAQPLTRSAL YSAMAAASAA VAASPPDDGA DAAGEGSADT PLAGLRLLLA EDNPLNQLVA
LSMLEGAGAA VEIASNGEEA VEYLRSNGAA IDLVLMDVQM PVMDGFEATR LIRELGLPLP
ILAMSAGVTL DEQAECQAAG MNAFVSKPVE WEDLLAAVLR HTGERSPASG TGTGTGTGTG
K
//
