ID A0A370DVD2_9GAMM Unreviewed; 1014 AA.
AC A0A370DVD2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DIZ78_01175 {ECO:0000313|EMBL:RDH88573.1};
OS endosymbiont of Escarpia spicata.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=2200908 {ECO:0000313|EMBL:RDH88573.1, ECO:0000313|Proteomes:UP000254771};
RN [1] {ECO:0000313|EMBL:RDH88573.1, ECO:0000313|Proteomes:UP000254771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1462 {ECO:0000313|EMBL:RDH88573.1};
RX PubMed=30022157;
RA Li Y., Liles M.R., Halanych K.M.;
RT "Endosymbiont genomes yield clues of tubeworm success.";
RL ISME J. 0:0-0(2018).
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:RDH88573.1}.
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DR EMBL; QFXE01000001; RDH88573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370DVD2; -.
DR Proteomes; UP000254771; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; -; 2.
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; 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 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; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 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; 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; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000254771};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 165..195
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 223..275
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 293..514
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 530..653
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 682..798
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 837..926
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 124..162
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 586
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 731
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 876
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1014 AA; 113641 MW; B068C2EEDBED198A CRC64;
MHPLLTRQLK RLFGISDEPK LTAALLELRR LANSDGLQEE ARNLLGGLDR LLGQIDNTYQ
QHEADITLRD QSLEISNEEI LQANEKLRRK ERRQHAIIES LRHTANELLR STHLPELSDD
ETSLEKLSLL MSDLVKERQQ VQNKLERTLS ELERQKSAID QHAIVSITDT SGKVTYANEG
FCRVSGFQRH ELIGKKHPQF DQTDQSAAII KNIWSTIRRG HTWKGEFANR NKTGTPYWLD
ATIVPFLDSQ GEAFQYIIIC TDITERRIFQ EQLKDAIHRA ESANKAKSEF LANMSHEIRT
PMNAIIGLSH LAIEGKTDQR QHEYLSKIQS SAKTLLSIIN DILDFSKIEA GEMTLETVDF
SLSELLEQVC TIFCFSAEKK SLEVVYSIAP DLPDRYFGDP LRLGQVLTNL ASNAVKFTEQ
GEIVISVTAE ESQQGKIRLR FDVSDTGIGL SEDKLAVLFD SFSQADSSTT RKFGGTGLGL
AISKSLISIM EGEIGVESTE GEGSNFYFTL PLQIDPERET PKNLQLHGIR AMVVDDLAKS
RDTILKTFRF HGANAIGKAC GETCIEELQR CCREEPTRPY QLTLIDWSMP GMDGLQLLRT
IQSDPLIDPK PRIILMSKYN NDQAIRQTET RNTILLTKPI IPTAFLNAVL KALGRPTLRI
RHEATSVSGR DVENIQGILG AHILVAEDNP VNQQVTRALL EHYGLKVKIA EDGRAAIEAL
AKTRFDLVLM DVQMPDIDGY EASRIIRQDA TYDEIPIIAL TANAMSGDRE ESLASGMDDY
LPKPIEPDAL YAMLLKWIQP GQAGHIFNDE YTSSAILLPE HLPGIDVEAG LKRMRGNQAL
FRDLLLRFRA DYEHWSGRIS MAILENNREE ALHLAHALKG VSATIGAMDL STAGASLEKH
LKTDMEDLTE IHNRVTDQLY QVLDGLKSLD KPPESATSRP VSTLDQQTLQ TLLSNMKPLL
LNGDLQALQL VEQLHEMVRG TEMVSTALEL KKHVDAFDFE KALNTLESHS PSTQ
//