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Database: UniProt
Entry: A0A0A2TLC4_9FIRM
LinkDB: A0A0A2TLC4_9FIRM
Original site: A0A0A2TLC4_9FIRM 
ID   A0A0A2TLC4_9FIRM        Unreviewed;       892 AA.
AC   A0A0A2TLC4;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=JT05_02375 {ECO:0000313|EMBL:KGP76877.1};
OS   Desulfosporosinus sp. Tol-M.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=1536651 {ECO:0000313|EMBL:KGP76877.1, ECO:0000313|Proteomes:UP000030439};
RN   [1] {ECO:0000313|EMBL:KGP76877.1, ECO:0000313|Proteomes:UP000030439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Abu Laban N., Tan B., Dao A., Foght J.;
RT   "Draft genome of Desulfosporosinus sp. Tol-M obtained by stable isotope
RT   probing of toluene- degrading methanogenic culture enriched from oil sands
RT   tailing of Alberta, Canada.";
RL   Submitted (OCT-2014) 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   -!- 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:KGP76877.1}.
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DR   EMBL; JQID01000039; KGP76877.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2TLC4; -.
DR   STRING; 1536651.JT05_02375; -.
DR   Proteomes; UP000030439; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd01987; USP_OKCHK; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; IPR038318; KdpD_sf.
DR   InterPro; IPR025201; KdpD_TM.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR   InterPro; IPR006016; UspA.
DR   PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR   PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR   Pfam; PF13493; DUF4118; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF02702; KdpD; 1.
DR   Pfam; PF00582; Usp; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KGP76877.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030439};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        389..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        412..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        438..461
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        467..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          663..879
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          361..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..382
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   892 AA;  98521 MW;  7DB58B81557F1461 CRC64;
     MATGKLTIFL GAASGVGKTY AMLEAALSRL SEGMDVVVGQ IETHGRAETE AMLKELTVIP
     ARSLVYEGRI VGELDLDAVL ARRPQIVLID GLAHTNIPGS RHKKRYMDVQ ELLTAGISVY
     TTVNIQHLET LKDIVAQITG VTVRETVPDQ VLETAFQIQL IDIPPEELIQ RFQDGKINVS
     DQAAAELKKF LRPGNINALR ELALRYTAQR VDRQLESYMQ VHGIGGPWPT GEKILVCISA
     SPFSTQLIRI AKRMAERVQG EWFAVHVETL QRFPISEAEK DSLTQNFRLA EELGAEIIGL
     TGNNVVEEIL ELARKRNVSQ IIIGKPEHSR FREIMHGSIV DKVIRQSHGI SIHVIPGSRQ
     KAEFSRNQAG TKRDEAGTRT KRRKSLSPVF PYLASSLIVI LMTWGITLIS SFLGLVNISL
     LYLLPVLISA ARWGTYPAIV TAVLGILTFD IFFVPPIFSI TVADLRYLIS FAIFILVGLI
     IGTLSLRLKR QVTYSRQREN SISALYALSR DIAAVDNLDA VLECIVSNVS NTLDGQVMVL
     LPNEKAQLVL RKDSGYNNFY NDHELAVAAW VYARGQKAGN GTETFGAAAA LYLPLSTEQG
     THGVLGICFN EAAAQFDAER IRILEAFTRL AGMAINRVKL TEQARETLAL VESERLRTAL
     FNSLSHDLRT PLSSIIGAVT GLLEDQNVVY SPEVRSELLH TILQGAERMN RFVSNLLDMA
     RLESGMLRLN KEWCDLQDII GVSINRLGVA FNHRPLDIDI QDELPLVQAD GILIEQVFIN
     LLDNALKYSE KGSIIAVSIR QLEKKLVIEV ANRSQGIPET DLSKIFDKFY RLNSPLQVSG
     TGLGLAICKG LIEAHGGDIW AENNKLGGVT ITFTLPLTNQ FTGRVPAMDE GD
//
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