ID A0A0B4BTQ3_9RHOB Unreviewed; 827 AA.
AC A0A0B4BTQ3;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=RA20_07500 {ECO:0000313|EMBL:KIC20710.1};
OS Leisingera sp. ANG-Vp.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Leisingera.
OX NCBI_TaxID=1577896 {ECO:0000313|EMBL:KIC20710.1, ECO:0000313|Proteomes:UP000031177};
RN [1] {ECO:0000313|Proteomes:UP000031177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-Vp {ECO:0000313|Proteomes:UP000031177};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(2015).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KIC20710.1}.
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DR EMBL; JWLD01000019; KIC20710.1; -; Genomic_DNA.
DR RefSeq; WP_039126216.1; NZ_JWLD01000019.1.
DR AlphaFoldDB; A0A0B4BTQ3; -.
DR STRING; 1577896.RA20_07500; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000031177; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:KIC20710.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:KIC20710.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 180..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 215..286
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 294..344
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 362..580
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 600..716
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 734..827
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 649
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 775
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 827 AA; 89424 MW; 6B0F99AD167F24A4 CRC64;
MFRGFPIMPR WVLALVLALA AALAAQSVRL GHQVLQQLEG LSTAATDNMQ WNLSQAEVEH
LKLETAVLTA QRPDDLPKLR RQFDIYYSRI ATFRESPLFE GLRRSPAGAA LLQQMTGRLE
RMAAAVDSSD QSLIASLPDL AAELQQNSGD VRELALFGVV LQVADSKDKR LKLFSILARL
GWVVLALVLA LALATLLLGR LYRKGRQLAM DRSRAAARME AMIASSLDAI LVVGADGRIQ
AFNGAAETVF GYKSEEAIGQ PMVNLIVPDH LQEAHKVGMQ RFLQTGEARV AGKGRLQMEA
RRKSGELFPV ELSVSVSQSG TDIVFVSFLR DISDRIAAEK QLRRARDEAL AGEQAKQNLL
TVMSHEMRTP LTGVLGAIEL IENTGPTPEQ RRYLQAMRVS GELLLHHVND VLELSRLESG
AASEKLRIFD LEELVGSLVE SQQASAQGRG IDLSLHCSLN GKKIVAGRPR AVQQVLLNLI
GNALKFTGEG AVSVDVMRLP DGKTVEFHVA DTGQGIAPED LERIFEDFIM LDASYGRGSE
GTGLGLSITK RLVRAMGGTI SCESELGEGS LFSISLPLPA AKAPPPRAEK DRPKQNGACR
LLIAEDNDIN RELLATMLRQ EGHQVTAVPG GREAVQAAGE GVFDLILMDI SMPQVDGIEA
LRRIRAQKLA DGTDIVALTA HAAAEDHARI LEAGFAEVLT KPANKAGLAD VIARRAGGGG
KALPRAESDI QQFFDALGQE KARVFLQAFC KEVKQLQEEL GDCAALEEDH RKEAHRLAGS
AAVLGLPDLR AAMLAIETAN EDAEPPLAPF LQAWANAEAV LAPHLQP
//
