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Database: UniProt
Entry: A0A0D1EIN3_9RHOB
LinkDB: A0A0D1EIN3_9RHOB
Original site: A0A0D1EIN3_9RHOB 
ID   A0A0D1EIN3_9RHOB        Unreviewed;       699 AA.
AC   A0A0D1EIN3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=barA_2 {ECO:0000313|EMBL:KIT15695.1};
GN   ORFNames=jaqu_25720 {ECO:0000313|EMBL:KIT15695.1};
OS   Jannaschia aquimarina.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia.
OX   NCBI_TaxID=935700 {ECO:0000313|EMBL:KIT15695.1, ECO:0000313|Proteomes:UP000032232};
RN   [1] {ECO:0000313|EMBL:KIT15695.1, ECO:0000313|Proteomes:UP000032232}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GSW-M26 {ECO:0000313|EMBL:KIT15695.1,
RC   ECO:0000313|Proteomes:UP000032232};
RA   Voget S., Daniel R.;
RT   "Genome Sequence of Jannaschia aquimarina DSM28248, a member of the
RT   Roseobacter clade.";
RL   Submitted (FEB-2015) 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   -!- 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:KIT15695.1}.
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DR   EMBL; JYFE01000046; KIT15695.1; -; Genomic_DNA.
DR   RefSeq; WP_043919371.1; NZ_JYFE01000046.1.
DR   AlphaFoldDB; A0A0D1EIN3; -.
DR   STRING; 935700.jaqu_25720; -.
DR   PATRIC; fig|935700.4.peg.2654; -.
DR   OrthoDB; 9801651at2; -.
DR   Proteomes; UP000032232; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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; 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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; PF12860; PAS_7; 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; 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; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000032232};
KW   Transferase {ECO:0000313|EMBL:KIT15695.1}.
FT   DOMAIN          225..448
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          574..690
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          195..225
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         623
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   699 AA;  76289 MW;  266FE471AA8AF225 CRC64;
     MDGFREDDVI LAERRKRLAA EQMLDHVRGE LLAAHRSLSD HVERVTAQYM KEREARIAET
     GLVDRVSAER RVAETRADRA GRRLWHAIEA IRDGFAVWDP DGTLVQCNQP FQMLFDGALD
     PLPGTTFTDL FRAAAEDGIF DPGESEVDDW VDTILARRKA ETDTPVLLRL FDGRSISLHD
     RVTEDGDIVS LAIDVTAEEE RAAALEAARR EAEDANRAKS RFLARMSHEF RTPMNGVIGV
     SDLLLEGDLD EETRLYIQTI RDSGLSLLEI VNDVLDAARL EAGKLTLRPA PFDLEQTLTQ
     VVRLAAVSGG AAAGIALDYP LDAPTRFMGD EARIRQIVTN LVGNAVKFAA GGDVLVTFRA
     TRPGGEETAR LEIEVRDTGP GIPADRREQV FGEFTRVEGR SGEGTGLGLS IARDLAHLMG
     GTIALLDDPE AEAQGACFVF SATLPTTRKW PSRPDLPDAV RMPVAETLVG RALRTRLRAS
     DVDVLGGWDS GDGKAPMILP TDLDPELQVR ATAGAGTAPL IIVGRRQDAA ADALERADFV
     LPDPCDGPTL LAALNGRHDR AREGTDVQSE RKLRILVADD VATNRLLMSK MLADPAHEVE
     VLDDGDVAVE AFEADPHDLV LLDISMPRMD GREAAKRIRE LPSGAAVPIV ALTAHADPAE
     AERILTFGLD EVLVKPVRRA DLRALLDRLA HRLPRSPRK
//
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