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Database: UniProt
Entry: A0A161IV67_9GAMM
LinkDB: A0A161IV67_9GAMM
Original site: A0A161IV67_9GAMM 
ID   A0A161IV67_9GAMM        Unreviewed;      1441 AA.
AC   A0A161IV67;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ATSB10_11850 {ECO:0000313|EMBL:AND68639.1};
OS   Dyella thiooxydans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dyella.
OX   NCBI_TaxID=445710 {ECO:0000313|EMBL:AND68639.1, ECO:0000313|Proteomes:UP000077255};
RN   [1] {ECO:0000313|EMBL:AND68639.1, ECO:0000313|Proteomes:UP000077255}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATSB10 {ECO:0000313|EMBL:AND68639.1,
RC   ECO:0000313|Proteomes:UP000077255};
RA   Lee Y., Hwangbo K., Chung H., Yoo J., Kim K.Y., Sa T.M., Um Y.,
RA   Madhaiyan M.;
RT   "Complete genome sequencing and analysis of ATSB10, Dyella thiooxydans
RT   isolated from rhizosphere soil of sunflower (Helianthus annuus L.).";
RL   Submitted (FEB-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; CP014841; AND68639.1; -; Genomic_DNA.
DR   STRING; 445710.ATSB10_11850; -.
DR   KEGG; dtx:ATSB10_11850; -.
DR   PATRIC; fig|445710.3.peg.1180; -.
DR   Proteomes; UP000077255; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 4.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.10.70.100; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 6.
DR   InterPro; IPR006189; CHASE_dom.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 4.
DR   PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 3.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 4.
DR   SMART; SM00091; PAS; 6.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 6.
DR   PROSITE; PS50839; CHASE; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 4.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AND68639.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077255};
KW   Transferase {ECO:0000313|EMBL:AND68639.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        233..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          106..173
FT                   /note="CHASE"
FT                   /evidence="ECO:0000259|PROSITE:PS50839"
FT   DOMAIN          287..322
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          484..534
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          535..605
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          821..891
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          1081..1130
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          1199..1419
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   1441 AA;  157679 MW;  A3E68898037B7026 CRC64;
     MLVVLLTTIL WSVLDRRQAS LEAALARSRQ QGLTTALRAG MDVQATAVQR LAKRLGMVDE
     PLRGELFKLD AAAFLADMPG LRALAFADND RVLRLNLVRS APGVGLGAKL DEAPDRRAVF
     DAVDAEGVVH LSAPVQLLSG QPGELLVAPV VSSGSRVGYV VAVVAFDRFF PSLLASQEGA
     DSLLIKQGRQ TIFARGFVRV PGSAPAATVS LYGQQWSVTS SAPGRIADQR PTWMVLLLGI
     ALAVLLTWAL SLSGLARARE RQAMLMSARL RDQVHAREAM QAALADAEKD MIAVLESISD
     GVFMVDPTWR FTYVNPQAAR MLQADVGALQ DVSCWSVLGG LLDDAGTGGA MHRRWQDAMR
     DGRPVTLEAT NEVGGCWYEM RAYPHARGLT VYMHDISERK RRERELLKRD ADSRHALQLG
     RMGSWELYLR SGYLHWSPET CAIFGVEESP GEKGIEALRR RVHPEDWQAL LDDQRRLEHG
     DDRIDRRYRM IRPDGEVRVI RALAELVVKE GDPIVAGAVQ DITEQERVRE ALSQAMEATQ
     LVMDSAPDVI IVLDREGRLL RVSAAAERLW GYPVESLVGE SITRLVHPDD VAATFEAAAD
     IAAGHPNPNF RNRNLTNDGR VLHMQWSGIW SERAQCIYAI GRDHSELHRV EELEAAQRQV
     LTAIASGRSL PDVLEAIVRA CEAQQPESLC SVLLLEDGRL RHGAAPHLPR QYMKAIDGAA
     IGPEAGSCGT AAWRRERVVV SDIATDPLWA NYAALALPHG LQACWSTPIM ARNGSVLGTF
     AVYYGEIREP GTEELAAIDG LAALASIAIE HEQAFRQLSE SEQRFRSLFD HHPDAVFALD
     AEGRIAQSNA AASALLGATP AELRQRLFAR FFTEDEHSRI EAALASAAGG EAGRLQVELQ
     GAEDRFPGYL VTLPIMVEQR AHGLFAVLQD HRQLRSAQQA TVNQLALLSA VAESVGEGLL
     AVDASGVPTF LNRTAARLLD LPSYGLPHPE ALPPEARSAV AGILDGRDLA GNDDASFSLG
     DGHRLDVAYV ATPLRIGGRL AGAVLAFRDI GDIKEARRSL LDRQRFFELS LEVFCIFDAG
     SGHFVQVNPA FCRLLGHDEA TLLGMPLVEL VHPQDRMATE DAVTWQYESG EPLSHFVNRL
     RRADGSDVWL EWTSRRSPEG QIFAVARDVT AKRQADQALE KAMDDLRIRN RELQDFAYVA
     SHDLQEPLRK IQAFSDRLQS RLAGQLDDSS SDYLQRMGDA ASRMQTLIDD LLAYSRVGTR
     PAALVPVDLS AELATVLDDL DARVQEAGAR IDAGPLPKLQ ADPSQMRQLL QNLLANALKF
     RAPDRPCLIR VSARPLGEAG ITTERWEISV QDNGIGFDPS YVERIFAPFQ RLHPRNVYPG
     TGIGLAIVRR IVERHGGTVW AEGVSGQGAR FVVVMPAHAA GPVRELPDAP LSNRDLPGAS
     S
//
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