ID A0A370WSR2_9GAMM Unreviewed; 895 AA.
AC A0A370WSR2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DWU98_18830 {ECO:0000313|EMBL:RDS79208.1};
OS Dyella monticola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=1927958 {ECO:0000313|EMBL:RDS79208.1, ECO:0000313|Proteomes:UP000254258};
RN [1] {ECO:0000313|EMBL:RDS79208.1, ECO:0000313|Proteomes:UP000254258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G-K06 {ECO:0000313|EMBL:RDS79208.1,
RC ECO:0000313|Proteomes:UP000254258};
RA Gao Z., Qiu L.;
RT "Dyella monticola sp. nov. and Dyella psychrodurans sp. nov. isolated from
RT monsoon evergreen broad-leaved forest soil of Dinghu Mountain, China.";
RL Submitted (JUL-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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:RDS79208.1}.
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DR EMBL; QRBE01000015; RDS79208.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370WSR2; -.
DR OrthoDB; 9764438at2; -.
DR Proteomes; UP000254258; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd12914; PDC1_DGC_like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.250.3020; -; 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; IPR033479; dCache_1.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; NF041832; near_NosP_CTERM; 1.
DR PANTHER; PTHR43047:SF9; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12860; PAS_7; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 300..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 526..739
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 764..879
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 478..519
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 814
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 895 AA; 99417 MW; 5D9E1B651FA854A1 CRC64;
MLIPLVTMRR LAKLLVCIVL SACIASSSWL AYRLVLRRAL LDQSRANIQQ LQLHSLALQR
LIDRYRVLPR MLALDPQLRA ALGSRPDDVT RRALNLKLET AGTASHTSTL TLLDRSGLAI
AANNWRGPGS NVGHRYDFRP YFQQARATGA GTFYAVGVST HEAGYFIAEA VKDARGDTLG
VISAKVPLAE LTREWLRSRN TILLSDKTGV VFLSSDSRWA YRVLNPLRAA DLARLAATRQ
YEGQRLEPVR YRTWETLEDG SSLVRTDSPA MTDTPLWTSL QVPVEDWTLH LLSSTQRSLA
AARVAAALAA LMWVPLVLLG LFLRQRHRLI QNRLHSRAEL ERLVTHYASE LRSAQDGLLL
AAQDASNQNA SLEHLPQGVS VVDGDLRIVA WNSRYVDLFK FPAGLIQVGC PIEDVLRYNA
SRGLLGSDAV DTAIHRRLDY MRNGSAYTFE RERPDGSVLE IRGNPLPDGG FVTSYTDITA
YKAAARDLRN LATTLEQRVE ERTRDLEAAK AEAEHANRNK THFTAAAVHD LLQPLNAARL
YAGALREMLS QSEARELVDR VENALDTQDQ LLASLLDVAR LEAGALRPRV ANVQLEPLLT
GLARQFSILA QARGLHLHYV PTRAVVQSDS LLLRRLLQNF LSNAIHYTPH GRVLLGCRRC
ADTLRIEVWD TGVGIPPTKQ QTIFEEFRRL NTGLEQSGRS VGLGLSIVDR IARLLGHSVG
LRSWPGQGSV FSVTVPWLSD APDADVPSPC ITTNEEDPVL HGRRVWCIDD SDQALQAIDA
LLRRWGCQPT LINDPHQCLY MARRNPAPEL LLLDYHLGAE TGMDLLGRLT QYWTQRPATI
VLTAQKDASI RAHVRAEGLH LLAKPVAPAS LRALMSQLLL AAMLEREGSR DESNQ
//
