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Database: UniProt
Entry: D6Z5S5_DESAT
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ID   D6Z5S5_DESAT            Unreviewed;       661 AA.
AC   D6Z5S5;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=DaAHT2_0094 {ECO:0000313|EMBL:ADH84807.1};
OS   Desulfurivibrio alkaliphilus (strain DSM 19089 / UNIQEM U267 / AHT2).
OC   Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC   Desulfobulbaceae; Desulfurivibrio.
OX   NCBI_TaxID=589865 {ECO:0000313|EMBL:ADH84807.1, ECO:0000313|Proteomes:UP000001508};
RN   [1] {ECO:0000313|Proteomes:UP000001508}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19089 / UNIQEM U267 / AHT2
RC   {ECO:0000313|Proteomes:UP000001508};
RG   US DOE Joint Genome Institute;
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Sorokin D.Y., Muyzer G.,
RA   Woyke T.;
RT   "Complete sequence of Desulfurivibrio alkaliphilus AHT2.";
RL   Submitted (FEB-2010) 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; CP001940; ADH84807.1; -; Genomic_DNA.
DR   RefSeq; WP_013162338.1; NC_014216.1.
DR   AlphaFoldDB; D6Z5S5; -.
DR   STRING; 589865.DaAHT2_0094; -.
DR   KEGG; dak:DaAHT2_0094; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_114_15_7; -.
DR   InParanoid; D6Z5S5; -.
DR   OrthoDB; 5378360at2; -.
DR   Proteomes; UP000001508; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; 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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
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; PF00989; PAS; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 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; 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   Kinase {ECO:0000313|EMBL:ADH84807.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000001508};
KW   Transferase {ECO:0000313|EMBL:ADH84807.1}.
FT   DOMAIN          31..104
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          178..401
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          432..551
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          567..661
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   MOD_RES         481
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         606
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   661 AA;  72532 MW;  893091191D3363FF CRC64;
     MALAEKFKMA WRALLGRSPV AFDAEERLRD SEGRLSAILQ SIGAGVIATD QQGRVAFLNP
     VAERLTGWDL VDALNRPVME VLNLVDEASG RPLTAPLQRV QEDGEIIDCS GELVLRSRQG
     KNYPVSCTVA PIASFSGIIG CVFVFRDTIR EREIQRNLLS AKEEAERASQ AKSEFLASMS
     HEIRTPLTTI LGMADLLDKT PLGAEQRQYV WASRAAGENL LDLINGILDL SKIEAGKLEI
     EVMEFDLDHL LRQTCEIMAL RAHQKGLEFT CRLSWQGSCL VLGDATRIRQ ILVNLIGNAI
     KFTERGKVTV EAVRWPAEES AENTWFGFVV SDTGIGIPPD KQEMVFEDFA QVDSSTSRRY
     GGTGLGLAIS RKLVQMMGGT IRLASREGEG SRFTVEIPLP WRGAILGASG KTSQEGALPA
     AGLPTAGAAT RRLLLAEDAP ENRLLFKAYL KGTPYLLDLA VNGEEAVVKF KQGHYDLVLL
     DIQMPGMDGY AAARAMRAWE AEQGREAIPI VALTAHAFRD DIRKSREAGC DGHMVKPIKM
     DDFLRTIRTY IGAAETATGD QPEIGQLDDL LADLVPGYLA RVRNDLTQMR KALSRRDYSK
     VCHLAHTIKG TGGGYGFNRL SELGAAMEEA AGGEDGEKIN FYLEELNLYL DKVEVLHGIK
     E
//
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