ID A0A1H9TVG2_9BACI Unreviewed; 1112 AA.
AC A0A1H9TVG2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05518684_106125 {ECO:0000313|EMBL:SES01360.1};
OS Salipaludibacillus aurantiacus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX NCBI_TaxID=1601833 {ECO:0000313|EMBL:SES01360.1, ECO:0000313|Proteomes:UP000198571};
RN [1] {ECO:0000313|EMBL:SES01360.1, ECO:0000313|Proteomes:UP000198571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S9 {ECO:0000313|EMBL:SES01360.1,
RC ECO:0000313|Proteomes:UP000198571};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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};
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DR EMBL; FOGT01000006; SES01360.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9TVG2; -.
DR STRING; 1601833.SAMN05518684_106125; -.
DR OrthoDB; 9809348at2; -.
DR Proteomes; UP000198571; 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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 2.
DR CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 2.
DR Gene3D; 2.60.40.2380; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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; IPR004358; Sig_transdc_His_kin-like_C.
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; PF07696; 7TMR-DISMED2; 1.
DR Pfam; PF02518; HATPase_c; 2.
DR Pfam; PF00512; HisKA; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 2.
DR SMART; SM00388; HisKA; 2.
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; 2.
DR PROSITE; PS50109; HIS_KIN; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SES01360.1};
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}; 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 188..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 254..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 342..364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 429..647
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 686..803
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 871..1102
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 391..418
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 809..864
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 736
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1112 AA; 125929 MW; D313B3E51BB4D9A8 CRC64;
MKNISITLLI LTVLTGVIHF FPSNISAESV VLNDSRGEID LAPYIEVLED KNNEWTINDV
AEGEISEKFE LNQGGAPSFG YTSSVYWVRF QLHNQYSGGE WYLKLDNPTM DYTSLYLSEN
GEFEAWEMGD LYPFGQREVT NRNFIFPLNL SEENDYVIYM RFQSEGAMQL PLTMMDRDSF
LSITQQDYII LGLLAGLAFV MALYNLFVYF SLQHKSYLFY VFFIIVNLLT FLSFSGLAYQ
FIWPEAVWWN NRSIVFFMAV SNILAILFTN SFLEPEKLVP RSVKWSIALL LMNFSVLIVL
VFSYPLALDF VVLATGISVG FILTVSLITL KNGFRPARFF SLAWYIFIAG VVVSILTDVG
VLPFTFMTKY AWQITTSLEL ILLSFALADK ITIMRKEKDQ AKREAIESQQ EMLEHLKRTD
KLKDEFLAVT SHELRTPLNG IIGIAESMKD GAAGEINDSA RKNLMMIITS GKRLAHLIND
IIDFSKLKNN DMDLHIKEVD VKETGDMVVN MCQSLVKSKP VIIENHLEKG LPAIAADENR
FQQVLYNLIG NAIKYTAEGK VSIYAYEKNG FMKIEVADTG PGIDEEELES IFFPFERGGA
NSDEHDEGMG IGLNISKRLV ELQGGRMNVR SGKGRGSVFT FSIPLYRGQE KRNVAAGTVH
PLSVEKEAFT FFSQPETSGS KKTGKKILVA DDEPVNLQIL INYLSLEGYE VKTASSGEQA
LRLLEDEKDF DLVILDIMMP KISGYKVCQD IRKTYSLTEL PVLMLTAKNQ IEDRLAAFEA
GANDYLVKPC DKRELLARTE TFLHLSRAVK EIKDRAEELN NMNLKLKEMN DILEVKVEDR
TKELALKNKE MNSKNEKLIK LEEARIQLLS NISHELGTPI TFLQSYVQTV KEGIIDANNP
KYLEIVQNKV KLLDRLINDL FDLVKFESGK MSLNIETINL KDWLQHIHET FMLDVETHRL
SFPLPVIKND RLDTEGVLSV DGERMEQVFY NLINNAVKHS LPGGKIEISA SICPYDKNKT
ASEFDGNVII EVKDNGTGIE EEALPYIFER FYKGGIAENS ESGTGLGLAI TKEIIDYHKG
EIWVTSTKNA GTSFFFSLPL ILKRAGQKNV HL
//
