ID A0A1I6KVT4_9BURK Unreviewed; 1028 AA.
AC A0A1I6KVT4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05428960_4023 {ECO:0000313|EMBL:SFR95333.1};
OS Mitsuaria sp. PDC51.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=1881035 {ECO:0000313|EMBL:SFR95333.1, ECO:0000313|Proteomes:UP000199246};
RN [1] {ECO:0000313|EMBL:SFR95333.1, ECO:0000313|Proteomes:UP000199246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PDC51 {ECO:0000313|EMBL:SFR95333.1,
RC ECO:0000313|Proteomes:UP000199246};
RA de Groot N.N.;
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};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FOZE01000002; SFR95333.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6KVT4; -.
DR STRING; 1881035.SAMN05428960_4023; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000199246; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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; 1.20.120.160; HPT 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; IPR036641; HPT_dom_sf.
DR InterPro; IPR005330; MHYT_dom.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
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; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF03707; MHYT; 2.
DR Pfam; PF08447; PAS_3; 1.
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; 1.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
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; PS50894; HPT; 1.
DR PROSITE; PS50924; MHYT; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00244};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000199246};
KW Transmembrane {ECO:0000256|PROSITE-ProRule:PRU00244};
KW Transmembrane helix {ECO:0000256|PROSITE-ProRule:PRU00244}.
FT TRANSMEM 30..52
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 64..87
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 93..116
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 128..149
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 161..180
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 192..213
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT DOMAIN 27..219
FT /note="MHYT"
FT /evidence="ECO:0000259|PROSITE:PS50924"
FT DOMAIN 284..358
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 361..413
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 431..647
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 668..787
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 831..924
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 793..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 404..431
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 717
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 870
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1028 AA; 110274 MW; E1C3249665A68E04 CRC64;
MSELSAALPQ FFLLRDGAPT LLLTGHYDGA LVLLSLAVAS LTSALALQVA GMAKPATGWR
RQSILATGAL ALGGGIWSMH FIGMLAFQLC AQIAFNAHIT AASMVPALIA SWVALALLSR
RELDRWRLVA GGVLVGAGIG AMHYTGMAAM EMSAALRYDP AWFGASIVVA VLLAMLALWI
RFGLAGRLSR PWAIALGGVV MGGAIAGMHY TAMGAARFVG LADGPCNTSI ENAGWLALAV
TVMALAISAI TAGANGLLVL RRLNTELVEE RGRMLVMETA LRDSETKYRT VIANSPGVTF
RCRLDENWSM LLINDAVEDL TGWTARDFLE GRQHFAALIH RHDQARVNAA VETAVAADTP
YALEYRVHTR DAGERWVSER GRAVRDAQGA PQWIDGVILD ITEPKRLQRQ LEEAKERAES
AAAAKSAFLA NMSHEIRTPM NAILGFTELL LDTTLTEAQR RHLTTVRGSA RSLLALLNDI
LDTAKLDKGA MELESVDFSL RTVCEQALNS LRLLAQRKNL VLHLDYPSAA PRFFQGDPLR
VQQVLLNLVG NAIKFTERGV VTLRMRHEGG QVHLAVVDTG IGIAPDRLDR IFDAFAQADA
STTRRFGGTG LGTTISRQLV ERMGGRITVE SELGQGSTFH VWLPLPAGNA ALAEAQASEA
AVALPPLRLL VADDVAQNGE LLQLILGREG HQVTLAADGL QALKAFSDER FDAVLMDVHM
PGLDGLGATR RIRNFEHAQG RGHTPVVALT ASVLEEDRQA ALAAGMDGFA VKPVEPARLF
AELARVLGLS PGRGAGEAGP APSTRHAAGL GSAGPGTEPL DWQQGLRLWG SVTAWQRGLR
RFAEEQREGV ARLHQLTQAR QWIELRGLVH RWRGVAGSLA MPRLLAHAQP VETALRLGRE
EDLMALVDTL ALTLQDTLDA VAELDGRPSG FAASAPMPMS ADRPADPSAE AAARDLRASK
QLVDRLAAAL KRSELDDESL SALRLALGAE ALGPLTRALD DFDFDAALLL LQSLRTRLST
PNAPQGLS
//
