ID A0A1I5SF32_9BURK Unreviewed; 848 AA.
AC A0A1I5SF32;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05443579_11413 {ECO:0000313|EMBL:SFP69364.1};
OS Variovorax sp. PDC80.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1882827 {ECO:0000313|EMBL:SFP69364.1, ECO:0000313|Proteomes:UP000199369};
RN [1] {ECO:0000313|Proteomes:UP000199369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PDC80 {ECO:0000313|Proteomes:UP000199369};
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};
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DR EMBL; FOWG01000014; SFP69364.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5SF32; -.
DR OrthoDB; 9792270at2; -.
DR Proteomes; UP000199369; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16919; HATPase_CckA-like; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; 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; 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; IPR013655; PAS_fold_3.
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; PTHR43065:SF49; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
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); 3.
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 Kinase {ECO:0000313|EMBL:SFP69364.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000199369};
KW Transferase {ECO:0000313|EMBL:SFP69364.1}.
FT DOMAIN 192..262
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 266..318
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 483..707
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 730..845
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 780
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 848 AA; 93602 MW; 55F31DE3A5C022A7 CRC64;
MKNGETHGGP GTALQHEGHF RPDGTLAATF LREHDWARSA LGPPQGWSGA LRHAVSLMLD
SALPMWLAWG DGLGMVYNEP YARVLGGKHP AALGAPLAEV WAEIWSEVGP LVETALAGSP
VHREDLPLVV NREGLEEQTW FTFSYAPLRD EQGAVRGLLC TVWETTAQVL ARRQLADKED
EATRRQAQRT ETEERYRLAV LATNDAVWDW RLSDGHVVWN QALTTLFGHT EEETSADWWL
DHIHPEDRAR VETGIHAVID GGGTAWTQEY RFLRKDGSHA EVFDRGTVLR DAQGRPLRMI
GAMLDLSERK ASELALRESH RQFRTLFETI DEGFCVIEFL DGPHGPMSDY VHVTANPAYL
ANAGIADVVG QRVREMVPDE ADGWVDIYRR VLLTGEPVRF ERELVRTGRF LELAAFRVEP
PERRQVAVLF QDVTQRHRAE RALLELNDSL EHRVAEEVAQ RLKTEEALRQ AQKMEAVGQL
TGGIAHDFNN MLAVVIGSLD LLGRQLAADD VRARRYVEAA RDGAKRAALL TQRLLAFSRQ
QPLRPESLDA NRLVAGMSDL LRRSLSGAIQ LETVLAGGLW RTHADPNQLE NVILNLAVNG
RDAMPDGGRL TIETANTHLD ERYAVEHLGL SSGQYVMIAV SDTGSGMPAE VVAKAFDPFF
TTKEVGRGTG LGLSQVYGFV KQSGGHVKIY SEVGEGTAVK VYLPRLLGAP AEDEKAEAAP
DTPLGGTEEL ILVVEDEPAV RQLTVAALTE LGYRVLQADG AVAALKLIDA HPEIQLLFTD
VVMPETNGRK LADEALRRRP ELKVLFTTGY TRNAVVHNGV LDAGVHLIGK PFTIEELAVR
VREVLDAS
//
