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Entry: A0A090AKA6_9GAMM
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ID   A0A090AKA6_9GAMM        Unreviewed;      1502 AA.
AC   A0A090AKA6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=THII_3682 {ECO:0000313|EMBL:BAP57979.1};
OS   Thioploca ingrica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Thioploca.
OX   NCBI_TaxID=40754 {ECO:0000313|EMBL:BAP57979.1, ECO:0000313|Proteomes:UP000031623};
RN   [1] {ECO:0000313|EMBL:BAP57979.1, ECO:0000313|Proteomes:UP000031623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kojima H., Ogura Y., Yamamoto N., Togashi T., Mori H., Watanabe T.,
RA   Nemoto F., Kurokawa K., Hayashi T., Fukui M.;
RT   "Ecophysiology of Thioploca ingrica as revealed by the complete genome
RT   sequence supplemented with proteomic evidence.";
RL   ISME J. 0:0-0(2014).
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; AP014633; BAP57979.1; -; Genomic_DNA.
DR   STRING; 40754.THII_3682; -.
DR   KEGG; tig:THII_3682; -.
DR   HOGENOM; CLU_000445_28_1_6; -.
DR   OrthoDB; 176203at2; -.
DR   Proteomes; UP000031623; Chromosome.
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   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; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
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; IPR013783; Ig-like_fold.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   InterPro; IPR011110; Reg_prop.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR011123; Y_Y_Y.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF07494; Reg_prop; 13.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF07228; SpoIIE; 1.
DR   Pfam; PF07495; Y_Y_Y; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 3.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000031623}.
FT   DOMAIN          859..1079
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1122..1239
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         1172
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1502 AA;  171690 MW;  4890E2F256EC7F89 CRC64;
     MNVYRLIWVL FLLLWPLSVV AYPPALKFEH LSLEDGLSQS TVYAILQDNK GFMWFGTQDG
     LNRYDGYQFT IYRHNPTDSN SLSHNEIFTL YEDRQNNLWI GTGGGLNRFD RQQERFIHYF
     HDPHNPNSLS HNTVWSIYED RQGRLWIGTN GGGLDQFDIQ HNRFIHYQHN PKDPQSLSHN
     RVWPIYQDKR GTLWVGTDGG GLNRFDPQTN KFMYYLLDMQ NPDCLNNYVT SIYEDQSGML
     WIGTVGGLHQ FDRDHEQFIP YYHDPQQPNS LSHDAVWAIR EDKQDNLWIA TDGGGLNWLD
     RQHKKFFHYQ NDPQNSASLS SDAVLSLYQD KAGTWWFGTG GGGVNFFNDE RKKFTHYFHD
     PNNPNRLNNN HVLSLYEDRQ RILWVGTRGG GLNRFDQPRD KVTHYLHDPN NLNSLSHNDV
     WSILEDSQGM LWVGTYGGGL NQFNREQNQF VAYLHDHQNP QSLVNNYVLS LYEDSTKTLW
     IGTREGLDQL DREHHQFIHY HHDPNDNTSL THNTILSIYE DRTQTLWVGT QQGLNRFDRQ
     RQRFTRYQFN QQDPTSLSHN QVSAIHEDNY GNLWVGTFGG GLNQLNRTTG TFTHYREADG
     LANDVIYGIL SDAKGYLWIS TNKGLSKFDP PAKRFRNYDT LDGLQSLEFN SAYFKNSRGE
     LFFGGINGFN VFNPQQVNDN SYIPPIVITD FEIFNQPVTI GKDSPLTQSI TETKKITLTY
     KQTFFSFEFA ALNFLQPSKN EYVYKLEGFD KDWNSVGNRR HAYYTNVPHG TYTFRVKGSN
     NDKIWNETGT FIELTILPPP WKTWWAYSLY ILTTLMVIAR YIHIQQQKLF AKQQELELEK
     KIATQLKEAN RLKDEFLANT SHELRTPLNG IIGIAESLLD GVAGPINQTL SNNLVMIVSS
     ARRLMTLVND ILDFSQIKRR KLQLQMGPVD IRTITEVILA LTRPLIGHKP VQLLQQIPTD
     LPLVRADENR VQQIFYNLVG NAIKFTESGT IIISAQYQEI SNYLTITIAD TGIGIPADKL
     ERIFDAFEQA DGSIARVYGG TGLGLTITRH LVKLQGGQLS VQSQVGVGSQ FTFTLPVLPL
     ESTETTLTPS PTFPLPLRGK STVSLVLVPE LPPVDVTQGN YHILIVDDDP VNRQVLINHL
     SLHNYAVSQA TSGQEALTLI VNGPKPDLIL LDVMMPHLSG YEVTQKIREQ WQANELPVLL
     LTAKNQIVDL VTGLEAGAND YLTKPVAKEE LLARIKTHLH LQQLRAENLR MHTELEVARR
     IQQMLLPTPP ELQCLTSLDI TGYMLPAEEV GGDYYDVLEH QGHILVGIGD VTGHGLESGV
     LMLMVQTAIR TLLEHGERDL TQFLNTLNRT LYKNIQQRMK VDKNLTLSLL QYFPLSATTG
     QVYLSGQHEE VIIIRNQGQL ECLNTESLGF MIGFMEDISA WLSQTQILLN SGDMIVLYTD
     GITEAVNSAG EYYGLERLCE IMLRHQQQTV AEIRQAVIND VHQHIGQQKL FDDITLLIIK
     QK
//
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