ID Q6ALX1_DESPS Unreviewed; 1018 AA.
AC Q6ALX1;
DT 13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2004, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=DP1925 {ECO:0000313|EMBL:CAG36654.1};
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439 {ECO:0000313|EMBL:CAG36654.1, ECO:0000313|Proteomes:UP000000602};
RN [1] {ECO:0000313|Proteomes:UP000000602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54 {ECO:0000313|Proteomes:UP000000602};
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(2004).
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};
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DR EMBL; CR522870; CAG36654.1; -; Genomic_DNA.
DR RefSeq; WP_011189166.1; NC_006138.1.
DR AlphaFoldDB; Q6ALX1; -.
DR STRING; 177439.DP1925; -.
DR KEGG; dps:DP1925; -.
DR eggNOG; COG2984; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR eggNOG; COG4753; Bacteria.
DR HOGENOM; CLU_000445_89_20_7; -.
DR OrthoDB; 5487437at2; -.
DR Proteomes; UP000000602; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
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; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR007487; ABC_transpt-TYRBP-like.
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; 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; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF04392; ABC_sub_bind; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
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); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000000602};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1018
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004270571"
FT TRANSMEM 354..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 391..430
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 456..508
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 509..551
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 656..878
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 897..1013
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 948
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1018 AA; 115028 MW; A79CAEF85693F85C CRC64;
MNFISRCVFK NKFPFFHLCL LIAFFLPSLP LLSAFPQKEV HNRQILIIQA GYEGYPWTDS
QHKGIQDVFS SVPEPTDLFF EYIDSKRNHG VTYFKNLQKF WEIKYSNQHI DLIITCDNQA
YEFFLKNRSA LFQDTPLVFA GVNRFDSASL KGKKLITGIV EENDLEATVE IALHLHPRTK
KIVFIIPGAQ SYRLQWVKDL PARYREEVEQ VILTVKELGE IDRELDALGP DIIAILLHNV
VSRDGIYMPV QKFVVHLAEN RPFPIYALWD STLGRGIVGG KLVNGELQGR EVAKLALKIL
RGTSVSELPV IEIPNQYMFD WQQLQRFNVD LSDLPAEAVV INRPISFYVQ NKRLVQMTLS
GISLLLLLVI FLTTALIYLK KAQNKVLLSD EILEQMPEAI VLTDLDGNIE KWLGRAEEIF
GYSESECLGR VLAFNQPLEL NITEQIEAGL KEKGRFLGEI SCLRKDGRAV PIEVTATRVF
SRSGIVVGTI SILQDITERR RAKEFLRVSE VRFRKMVAKS PMPTILTDQN QDLIFVNDKF
TELFGYRLED IDTEKKWWES AYPDANYRKM VKNIWRIAIK RAVADDRDIE VQEWDLTTRD
GRVSRCEFYM VPIEEQSLIV INDISQRIRD ASEKNKLEMQ LQQAQKMEAI GTLAGGIAHD
FNNILAVILG YAELAKDEVP ANSVIEKDLD QVIVGGNRAK ELVKQILAFS RQEKVERLPM
KVQVLLKEAM RMLRPSLPST IEIQTEIDPL CGFILADPTQ VHQIIMNLCT NANHAMDKSG
GRLHIELKRI SIDEENEHSS LRSGDYVVLV VADTGKGIAP DNIGKIFEPY FTTKEIGKGT
GMGLATIHGI IREYGGRIDV VSVPGHGAAF SVYFPVITAV ETTENAVIKE TPQGSGRILL
IDDEELLLTV GKKVLERLGY RVTTKSSSLE ALAIFKERPD AFDAIITDQT MPDMFGSDLA
QEILKIRADI PIILCTGYSD QFDTDMAHSL GIREFVLKPL TKVTLANLLS GVLGGQQE
//
