ID A0A1Y2Q2K8_9BURK Unreviewed; 710 AA.
AC A0A1Y2Q2K8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CAP38_14875 {ECO:0000313|EMBL:OSZ62555.1};
OS Hydrogenophaga sp. IBVHS2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hydrogenophaga.
OX NCBI_TaxID=1985170 {ECO:0000313|EMBL:OSZ62555.1, ECO:0000313|Proteomes:UP000243193};
RN [1] {ECO:0000313|EMBL:OSZ62555.1, ECO:0000313|Proteomes:UP000243193}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBVHS2 {ECO:0000313|EMBL:OSZ62555.1,
RC ECO:0000313|Proteomes:UP000243193};
RA Orr R.J.;
RT "Draft genome sequences of novel bacteria, isolated from environmental
RT samples.";
RL Submitted (MAY-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};
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:OSZ62555.1}.
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DR EMBL; NFUT01000007; OSZ62555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2Q2K8; -.
DR STRING; 1985170.CAP38_14875; -.
DR OrthoDB; 9808408at2; -.
DR Proteomes; UP000243193; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
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; 3.
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; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR42878:SF7; BACTERIOPHYTOCHROME; 1.
DR PANTHER; PTHR42878; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000243193}.
FT DOMAIN 124..176
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 319..375
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 399..451
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 480..696
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 22..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 435..473
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 710 AA; 78528 MW; 35AF06F2D47D5882 CRC64;
MSPALGTAES LRVADMHSGV ARTSTPAYID PTPPATIDLS PPMSSPTTPS ADPAFELAPC
ALIELDPAGL VLRINRAGRQ MLAWSDQDPL AGRHLSVLLR LEGSPGESLL PSHLALVRPA
VDVPPLELRV RLPSGEIHVL QLSLGAVPDA SGQVQRLLVS LLDVGERRVL EQRLAAQVEF
LSSLTDRTPS RLTYFDRDLV CRFANRAQAD RYGRTPQQMV GVHLSELVPA PHLPRVMARV
TRALAGEAQT FEADGTDADG QPSWHEVHYV PDLQHGEVVG IFMELNDITE RRRTEDIVLG
ANLELEERVQ QRTAELHASE QRFRLMVDAV RDSCIYFVDA EGFIVEWSES AQRLHGFDRV
QVLGRPLAML LPPDEGVDLA LDPEQPEVLV HQAVDHGHAD TQGWRLRADG SRFFAHVSLT
ALRNPAGELQ GISVIERDMT AAKQLEDVMN DLNKELERRV EERTRQLVAA NKDLDVFSHT
ISHDLRAPLR HIGSFAGLIR EQLGEQGDPQ LLQYESAISR SARRMAGMVE GLLEYARLGR
ITVEYQPVPL LTLVQGVVAH LKAEHPLRDI AWDIESDLPV ARGDPMMLAQ LFAYLLENAV
KFTGRTAQAR VEIGWTVSEQ GVRTFHVRDN GVGFDLQKAA NLFVMFQRQH HSMDFEGLGT
GLALAQRIVE RHGGRIWCET AVGQGCSFLF TLPFEGEEAG DSRFGAVDTL
//
