ID A0A494Y3C3_9BURK Unreviewed; 662 AA.
AC A0A494Y3C3;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=D7S86_14410 {ECO:0000313|EMBL:RKP54822.1};
OS Pararobbsia silviterrae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Pararobbsia.
OX NCBI_TaxID=1792498 {ECO:0000313|EMBL:RKP54822.1, ECO:0000313|Proteomes:UP000270342};
RN [1] {ECO:0000313|EMBL:RKP54822.1, ECO:0000313|Proteomes:UP000270342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHC34 {ECO:0000313|EMBL:RKP54822.1,
RC ECO:0000313|Proteomes:UP000270342};
RA Gao Z.-H., Qiu L.-H.;
RT "Robbsia sp. DHC34, isolated from soil.";
RL Submitted (OCT-2018) 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:RKP54822.1}.
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DR EMBL; RBZU01000005; RKP54822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A494Y3C3; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000270342; 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; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; 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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
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; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000270342}.
FT DOMAIN 5..125
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 143..190
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 294..513
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 536..650
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 60
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 585
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 662 AA; 71537 MW; 992E7848902C2977 CRC64;
MTTLHVILVE DSALDAEFTL SALDRGGYHA ETTLVDNEAA FTRALDEAIG NDRLDLILAD
FVLPSFSGTE ALAIARARAP DVPFIFVSGV LGEEHAVDML KRGATDYVLK QRLSRLPAVV
ARALNERSVR LERIRIERTL HETETHFRLL VDALRDYAVM TLDAHGCVRT WNAASERILG
YTSAEVLGQS ARIFFSREDI EAGAFERELD EARRVGTSSD DRWLWRKDGK SFFAAGTTTA
ILSDDLRAGG ERTLLGFSKI IRDATQARFA ADALRLAKEQ AETANRAKDH FLAVLSHELR
TPLTPILAAV RLIEMKGPLP DGVNATLDVI RRNVELEARL IDDLLDLTSI ARGKLSLNFQ
AVSLDEVLMS ALEMSSADMH AKRLHISTRF EIEGTRVSGD AARLQQIIWN LVRNAVKFTP
EGGRVEVTVC RPDPQCVSVV VSDTGIGISA EALPRIFSAF EQADETISKG FGGLGLGLAI
ASTLAQKHGG TLSAHSEGRG AGARFTLTLP VLLDAGPVDD RAAGEEAAPE SSSSLRVLLV
EDNAFTSSAM ADLLSALGHQ VSVADTVHGA IELAGDRPFD LLISDIGLPD GSGLDVMHAW
TARQPGVPGV AVTGYGMDED VRRCRDAGFA DHLTKPVNVD RLEAMLRAIA RQVATQQSGG
RT
//
