ID A0A0W0GIC1_9CHLR Unreviewed; 932 AA.
AC A0A0W0GIC1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DEALK_11380 {ECO:0000313|EMBL:KTB48293.1};
OS Dehalogenimonas alkenigignens.
OC Bacteria; Chloroflexota; Dehalococcoidia; Dehalogenimonas.
OX NCBI_TaxID=1217799 {ECO:0000313|EMBL:KTB48293.1, ECO:0000313|Proteomes:UP000053947};
RN [1] {ECO:0000313|EMBL:KTB48293.1, ECO:0000313|Proteomes:UP000053947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP3-3 {ECO:0000313|EMBL:KTB48293.1,
RC ECO:0000313|Proteomes:UP000053947};
RA Key T.A., Richmond D.P., Bowman K.S., Cho Y.-J., Chun J., da Costa M.S.,
RA Rainey F.A., Moe W.M.;
RT "Genome sequence of the organohalide-respiring Dehalogenimonas
RT alkenigignens type strain (IP3-3T).";
RL Submitted (JUN-2015) 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:KTB48293.1}.
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DR EMBL; LFDV01000002; KTB48293.1; -; Genomic_DNA.
DR RefSeq; WP_058439304.1; NZ_KQ758903.1.
DR AlphaFoldDB; A0A0W0GIC1; -.
DR STRING; 1217799.DEALK_11380; -.
DR PATRIC; fig|1217799.6.peg.1174; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000053947; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 4.
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; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 5.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053947}.
FT DOMAIN 295..365
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 367..419
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 524..598
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 707..922
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 634..661
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 932 AA; 105483 MW; 03B330597EFAA408 CRC64;
MSAPIQPVIP YHDLFKHMLN GVAYCRMVFD TKDNPVDFVY LYVNPAFEKI TGLKQAAIIN
RRVTDAIPGI KTENPELFDT YGRVVLTGEP AEFEIYVKPL KRWLAVSAYR PKRGHFVAIF
ENITGRKLTE QALAASDAQA RLLLALSNDG IMVHGMTPDG QPEPFIEVNE SACQMLGYSR
SELLKMSPAD IDAPKNPDEI PVIDRLMSDG SVVFERFHIA KNGTRIPVEI SSRIADVNGN
KMVISIVRDI AERKKERMLL ERLVAERTQE LNDINLKLTQ EIEQRALAQR ALEASESHFR
SLYEKLPVGY QSLDAEARFL EVNPAWLKTM GYAKEEVIGR WFGDFLAGDQ ASDFREKFKR
FKERGEVETE FVLVRKNGSH ALVSVTGRID YDTLGAVRKT HCLIIDITER RRIEQEIYRL
ASFPLVNPNP IMRVSPQGEL LFANNASRPL MEHWHARIGG LLPEELRAEI TEAYSSGLVR
NLEVTVGEQT YDIKLYPNFE LGALNLYGID ISRRKKIARE LEISEANYRM LFNNASDAMI
LWKSIGNNTW QIIEANRVAC ERYGYSRDEM LALTGQQLNA PGSYSSLSPA IEQMRRTGYA
TYELKHITKK GVVIPVEVYG HQFELNGDIV ILAVVRDISE RKRLEAEKEK YQDRLEAMVE
ERTRSLTEEI ASRHRAEAEL QRLYEHEKSL SYALKKQMDE RVFFTRALVH ELKTPLTPLL
GSSEMLVNLA REEPLISLSR NVQSGAVKLR KRIDQLLDLA KGEVGLLKLK FAPVDLGNLL
KELVSFISPS AVKKGLAIRL DLPPSLPPIE GDRDYLYRVI LNLLDNALKF TSSGGQVTIK
AFVSGDAIEV WVSDTGIGIP KEKQERLFVP YSRVASDDTE FAGLGLGLSL CKNIIELHGG
RIWIESQKDK GTTVRFTLPV IHPKQEKGET RS
//
