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
//