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Database: UniProt
Entry: C5DH38_LACTC
LinkDB: C5DH38_LACTC
Original site: C5DH38_LACTC 
ID   C5DH38_LACTC            Unreviewed;      1177 AA.
AC   C5DH38;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=KLTH0E01100g {ECO:0000313|EMBL:CAR23099.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR23099.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR23099.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
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; CU928169; CAR23099.1; -; Genomic_DNA.
DR   RefSeq; XP_002553536.1; XM_002553490.1.
DR   AlphaFoldDB; C5DH38; -.
DR   STRING; 559295.C5DH38; -.
DR   GeneID; 8291674; -.
DR   KEGG; lth:KLTH0E01100g; -.
DR   eggNOG; KOG0519; Eukaryota.
DR   HOGENOM; CLU_003731_0_0_1; -.
DR   InParanoid; C5DH38; -.
DR   OMA; WGDSNRI; -.
DR   OrthoDB; 1222064at2759; -.
DR   Proteomes; UP000002036; Chromosome E.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00082; HisKA; 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   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        29..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          487..519
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          552..943
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1038..1159
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          715..838
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          955..1005
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        733..765
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        776..798
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        799..827
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        969..983
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        984..1005
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1093
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1177 AA;  130007 MW;  86C7A8E940447EF0 CRC64;
     MARLKKFDLG AYAKRKLKPP FLISIRTQLT ALVCLVALLS LIILAVITGV YFTSSFKSMR
     AERLYVASQL KASQIDQNLY YLYYQCYYLS TRDVLQNALT QYLAGNTTTE NWADAVTTLD
     KFLGSSNLFS LARVYDSSFQ DVLNASNNAS GNLVPESVLT QLFPLSTNVS LPSSLEVKGM
     LTDPVLNDTG YLMSMSLPIF ANPSIILSTS KVYGYITVVI SAEGLKTVFN DTTALEDSSV
     ILVSTVYDNR ELAGYHLVFP PYGMPSDIID KRYTIGNDSF LMDAFKQSKG GSIKSTHFLY
     SKAVAIGYSP CSSDLVQWVA IITQPESKFL YPSTRLARII VGTCVAIAVV TCAVTFPLSH
     WAVQPIVRLQ KATEIITAGR GLRSDNGSTL YSHKRSSTAE SFSSALHPAS IRRSGSVARS
     SKHKYIPESA KGTLNKNDFE EIQPDGIENN EDAALQKVHS PTPGSLFSEQ RSARSERYIT
     STNLIEARVP TYNRLFSDEL SELTETFNTM TDELDRHYAL LEDRVRARTR QLEAAKIEAE
     GANEAKTVFI ANISHELRTP LNGILGMTAI AMAENDMQKV KSSLKLIFRS GELLLHIMTE
     LLTFSKNVLK RTKLEERDFT VHEIALQVES IFGKLAKDQH VNLTISIIPN VLRTMVLWGD
     SNRIVQIVMN LVSNALKFTP VDGRVNVKFT LLGEYDESKA SNGCFDRAAV VPIQESEKES
     STLGPTEKGG IKDVTESASS SNATWPPSPS TSETSNGSKA ETTSGKLTES SEEDEKEEKL
     DHDDKDEGDE ESEEEEYRGE AEVSGKDDTN NETQREDSNE NQNEDARSIE SENASSYDDA
     IFHSRLRKGN SGENEDGRPL EHPRRLAIAM EVQDTGPGIE PALQESVFEP FVQGDQTLSR
     QYGGTGLGLS ICRQLAAMMN GSMSLDSKVG VGSKFTFTVP LTQTKELCFE EDENPFEDEF
     NPDSKKNRKV KFKVSKNNKR KKSHSSSSGQ NSSVGTPTVS ESEVSVGSVR VDRPFLQSTG
     TALSTRSVTT TSVANKCKVL VAEDNNVNQE VIKRMLNLEG LDDVDLACDG QDAFDKVKAR
     NEAGKFYDLI FMDVQMPRVD GLSATRMIRN ELSYTHPIVA LTAYADDRNI KECIDAGMNG
     FLAKPIRRPK IKEILSEYCP TYFKADGEKK GKTEGQA
//
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