ID A0A1H7MYA5_9BURK Unreviewed; 1371 AA.
AC A0A1H7MYA5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05216319_1172 {ECO:0000313|EMBL:SEL16029.1};
OS Duganella sp. CF402.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1855289 {ECO:0000313|EMBL:SEL16029.1, ECO:0000313|Proteomes:UP000198529};
RN [1] {ECO:0000313|Proteomes:UP000198529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF402 {ECO:0000313|Proteomes:UP000198529};
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; FOBG01000001; SEL16029.1; -; Genomic_DNA.
DR STRING; 1855289.SAMN05216319_1172; -.
DR Proteomes; UP000198529; 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; cd01948; EAL; 1.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.20.20.450; EAL domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR InterPro; IPR000160; GGDEF_dom.
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; IPR019247; Histidine_kinase_BarA_N.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00254; GGDEF; 1.
DR PANTHER; PTHR44757:SF11; DIGUANYLATE CYCLASE DGCE-RELATED; 1.
DR PANTHER; PTHR44757; DIGUANYLATE CYCLASE DGCP; 1.
DR Pfam; PF00563; EAL; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 2.
DR Pfam; PF09984; sCache_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00052; EAL; 1.
DR SMART; SM00267; GGDEF; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 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; SSF141868; EAL domain-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS50883; EAL; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 177..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 201..253
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 268..487
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 515..633
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 697..790
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 807..923
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 966..1098
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT DOMAIN 1107..1362
FT /note="EAL"
FT /evidence="ECO:0000259|PROSITE:PS50883"
FT REGION 646..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 564
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 736
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 856
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1371 AA; 149777 MW; 4F72BC511A21009A CRC64;
MFRHFLRRTG FQRQLTIMVS AGILSLAVFS ALMNAWAANS RMRDHFIGQG QRIADNLARQ
STLALLFHSV ENARDVVGAT LAFPDVAGLQ IMDARRKVLL SRAQGGAKLD PAIFGAMPPS
HAGMAGENAD GWVFVAPVYG GQGEASPFEL QDNQQQLLGY VHVQLSKATL NKLTWSLLLG
NLGLTLSFAV ILLVLARFLT RHMLTPLNAL SRLMRRAESG ESGMRATPDG PRDLIEMGQA
FNQMMNVLEQ REAAAVNMAQ MKAQFAATVS HEVRTPLNGV VGMLDMLKET RLTQRQQEFV
DVAWNSSRTL IALINNILDF SKMEAGKLTL EETEFSLTAL LSEVTELLAG PAQQKGVTVS
WVVDSDVPER VCADALRVRQ ILINLTGNAV KFTERGEVAL RVSLAAADPL KLRFEVRDTG
IGMSAEVQRH LFEAYSQPDP GTTRRFGGTG LGLAICKQLA DLLGGEISVQ SAAGSGTTFH
FSIPCHPAQP VQPAQVVQST VLHAPPRPMP ERQYRVLIAE DNRTNQMVAA GMLAMNGCVC
EFAADGVEAV RATQRDRFDL ILMDCSMPEM DGYEATAHIR LLEQALGRRT PLIAMTANTQ
AGDAEKCLAA GMDDYLAKPI TLVELRHKLE KWLPHAAPVA ASPAANASAG NAAPAGGRAS
SGATSHAAGA PAFPPRSSTG GPAPVDLVVF DKLREVLGDS LPHAVTPYLE DMPACLDELA
QAVRSGDMKA ARIRAHTLKG ASGNFGAEAL AQLALQAEQL AAAGQPERIA PLLQPLNEQY
RAVAAFLRVE LSYTDADDLR PGDDLPQVLV VDDDRSTRST LRHTLQRDGF RVEEASDGQQ
ALSMLTRFQP DVILMDAMMP VMDGFTACAR MQELPNGADI PVLMITALQD NSSVERAFAA
GASDYIPKPI HYAVLSQRVR RIIEANRAEK RIRHLAYNDV LTSLPNRTLF FELLAKSIDH
ARSNEQQVAV LFMDLDRFKY VNDNLGHAVG DRLLQAVAQR VRQTVRSDDT VARLGGDEFT
VVLNQLDNPA AAATAAHNIV RSLSVPFPID GHEIFVTASV GIAMFPHDGS DVAALVKHAD
SAMYRAKRTN TGFQFYESSM EHSISEHVRL ESDLRRAMEQ QHQLEVHYQP QACVTSGRII
GMEALVRWRH PVRGMIAPAE FIPLAEETGI INQLGDWVLR TACAQLKQFI RNGLPEMRVA
VNLSVRQLLQ KDFAASVEAV LADTGLPPHL LELEITESTL MENAHDTLAA LHRLRELGVR
LSIDDFGTGY SSLSYLKRFP VDIIKIDRSF VQDLPQDPDD AAIVSAIIAL AHSLRLHVVA
EGVETDAQLD FLARRSCDMM QGYHLSPAIP ADQFEDFARR AQKRINREIA S
//
