ID A0A2U1JWW4_9BACI Unreviewed; 1031 AA.
AC A0A2U1JWW4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DCC39_13170 {ECO:0000313|EMBL:PWA09444.1};
OS Pueribacillus theae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pueribacillus.
OX NCBI_TaxID=2171751 {ECO:0000313|EMBL:PWA09444.1, ECO:0000313|Proteomes:UP000245998};
RN [1] {ECO:0000313|EMBL:PWA09444.1, ECO:0000313|Proteomes:UP000245998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T8 {ECO:0000313|EMBL:PWA09444.1,
RC ECO:0000313|Proteomes:UP000245998};
RA Niu L.;
RT "Camelliibacillus theae gen. nov., sp. nov., isolated from Pu'er tea.";
RL Submitted (APR-2018) 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:PWA09444.1}.
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DR EMBL; QCZG01000029; PWA09444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1JWW4; -.
DR OrthoDB; 9809348at2; -.
DR Proteomes; UP000245998; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR008979; Galactose-bd-like_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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF83; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF02518; HATPase_c; 2.
DR Pfam; PF06580; His_kinase; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 2.
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; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PWA09444.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000245998};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 211..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 277..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 362..384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 438..656
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 700..816
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 749
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1031 AA; 117900 MW; ECC0F65030E7E95D CRC64;
MTKRKIFLFT SLFLLIITSF RIVWITSNLM PDQPQAKRGV LDLRKWDFSE SPILTLDGEW
EFYPNTLLTA EQIESHSFTE QKELIPVPRK WNKFIPNETN SPSDFGTYRL RILVNEDTKQ
LYGLKTPSIR TAYTVFANGH AIIANGHPSE KFNKHQANYT PDFASFTAGS NEEIEIVIHV
SNYEFPNTGG ITKSIKFGTD SSISNKNMLS IGLQVLMSVI MLIHGIYTLI LFFLRPRKKE
FLFFSLAMFC AALSIMLTDD KLLVAWLPTT FEWTFKLARL SYAGIALFFL LFIKHFFPLY
KKNRIIHFFS IFLITEAIFI VVTPLKYTML ALPVFFILSA LSYFAISIFI LKILLKGTQQ
YLLLWFAAIS TSSSVIWGII HTSFFTYEPT FYPFDLIFAL FTFSAYWFKR FFQTTDENEE
LVKKLQNEDK RKDGFLANTS HELRNPLHGM INIAESIVTH EKNTLNEKTK NNLELLITIG
RRLSLMLDDL IDITRLKEQG IRLNKQPVSI QTITSGAFDM IRFMAKNKNI KFNIEIPESF
PPVLADKNRL IQILYNLLHN AVKFTNDGVI SIHASVRNGM ASIHIKDTGI GIDKETQKRI
FQPYEQGNPN VTANEGGLGL GLSICKELIE MHDGMLQVNS VPGKGSEFTF TLPLAETSEH
FNEQQHKTVK EEMAVDTDSP LTYVDATNIA TDNQLIERPK ILAVDDDPVN LKILSDILPP
EQYELVTATS GKKALSYLNQ KEWDLMIADV MMPIMSGYEL TRKTRELFSI TELPILLLTA
RSQPEDIVSG FLSGANDYVT KPLRGLELKT RVNALTNLKQ SINERLRMEA AWLQAQIQPH
FLFNTLNTIA SLSEIDSDRM TSLLEEFGNY LRRSFDPQNL QRVVPLEHEL ELLRSYLYIE
KARFGDRLHI EWDIDETIKQ IQIPPLSIQP LVENAIKHGI LKRIQGGTVQ IKITHFLNDT
IITIIDNGVG MDSEKVRQLL SEKTQGIGVN NTHQRLKKLY GRGLQIHSIP NQGTTIHFKI
PKMPPPLEQK S
//
