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Database: UniProt
Entry: A0A370DVD2_9GAMM
LinkDB: A0A370DVD2_9GAMM
Original site: A0A370DVD2_9GAMM 
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
//
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