ID A0A1Y2Q8X6_9BURK Unreviewed; 753 AA.
AC A0A1Y2Q8X6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CAP38_11385 {ECO:0000313|EMBL:OSZ63890.1};
OS Hydrogenophaga sp. IBVHS2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hydrogenophaga.
OX NCBI_TaxID=1985170 {ECO:0000313|EMBL:OSZ63890.1, ECO:0000313|Proteomes:UP000243193};
RN [1] {ECO:0000313|EMBL:OSZ63890.1, ECO:0000313|Proteomes:UP000243193}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBVHS2 {ECO:0000313|EMBL:OSZ63890.1,
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:OSZ63890.1}.
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DR EMBL; NFUT01000004; OSZ63890.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2Q8X6; -.
DR STRING; 1985170.CAP38_11385; -.
DR Proteomes; UP000243193; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 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; IPR003660; HAMP_dom.
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; IPR017232; NtrY.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 1.
DR PIRSF; PIRSF037532; STHK_NtrY; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-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; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OSZ63890.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000243193};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 22..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 336..388
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 400..448
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 536..753
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 753 AA; 81358 MW; 2625A328D11C53C4 CRC64;
MVERPPVSAA PNSRRQAVAA RWAVGAALVF MTGVGMVLLF LLTLATRNRA LYEQNFTWLV
AVNVAVAGFL LLVIGWLAVR LFLRLKRGKF GSRLLIKLAG IIGLVGVLPG LLIYTVSYQF
VSRSIESWFD VRVESALAAG LNLGRTTLDT LMADMSNKAR VAAEGLSRLS STSAVFALDD
VRNQLGASDV VLWGASGRPL GSAGVSRFDL SPERPSAALL RNVREARVVA TVEGLEEGAD
SELDAALAAR EARIRVTALV PPPTFAFGGE PRYLQAVAPL PSALVVDALA VQLANREYQE
RALAREGLRR MYIGTLTLAL FLAVFGAVLL AVLLGNQLVR PLLVLAEGMR EVAAGNLSPK
QALTSRDELA GLTRTFAHMT QDLSDARAAV QRSMSEVDAA RDNLQTILDN LTAGVVVLDE
AGALRSVNPG AERILHIPLA LHIGRPLVEL PGLEAFGSGV LQQFERFLGD QTPHEGGYWQ
QSFELSASGT TPFQQGITLI ARGALLPRNE RLLVFDDVSD MVSAQRAQAW GEVARRLAHE
IKNPLTPIQL SAERLAMKLD GKVAPPEQAV LDKSVRTIVD QVDAMKRLVN EFRDYARLPA
AQLVPVDLNA LLRDILALYD HAAVPVRLEL ADDLPMAMAD AQQVRQIVHN LVQNAQDAMT
AQPGAEVLLR TRRSDSGQWV RLSVLDQGPG FAEHILKRAF EPYVTTKSKG TGLGLAVVKK
IMDEHGGRVD LSNRLVEGRI TGAQVSLSFA VAN
//
