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Database: UniProt
Entry: T0GNC9_9SPHN
LinkDB: T0GNC9_9SPHN
Original site: T0GNC9_9SPHN 
ID   T0GNC9_9SPHN            Unreviewed;       868 AA.
AC   T0GNC9;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=L485_09260 {ECO:0000313|EMBL:EQB02192.1};
OS   Sphingobium baderi LL03.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1114964 {ECO:0000313|EMBL:EQB02192.1, ECO:0000313|Proteomes:UP000015524};
RN   [1] {ECO:0000313|EMBL:EQB02192.1, ECO:0000313|Proteomes:UP000015524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LL03 {ECO:0000313|EMBL:EQB02192.1,
RC   ECO:0000313|Proteomes:UP000015524};
RX   PubMed=24051322;
RA   Kaur J., Verma H., Tripathi C., Khurana J.P., Lal R.;
RT   "Draft Genome Sequence of a Hexachlorocyclohexane-Degrading Bacterium,
RT   Sphingobium baderi Strain LL03T.";
RL   Genome Announc. 1:e00751-13(2013).
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:EQB02192.1}.
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DR   EMBL; ATIB01000050; EQB02192.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0GNC9; -.
DR   PATRIC; fig|1114964.3.peg.1811; -.
DR   eggNOG; COG4191; Bacteria.
DR   Proteomes; UP000015524; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16919; HATPase_CckA-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   CDD; cd18161; REC_hyHK_blue-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.10.70.100; -; 1.
DR   Gene3D; 3.30.450.40; -; 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; 2.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 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; 2.
DR   SMART; SM00091; PAS; 2.
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; 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); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 1.
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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000015524};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          54..104
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          105..159
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          252..304
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          505..729
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          752..867
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          446..489
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         802
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   868 AA;  95928 MW;  A485FE2AAE6BA861 CRC64;
     MSDQKQISHR SWKSIADDQR IENELSGLDP FTDPFVAAVH ATRMPMIITN PRLADNPVVF
     ANDAFCRLTG YERDEILGRN CRFLQGEATD QETRRQLHQA VEHAHPVEVD IRNYRKNGEP
     FWNRLLMAPV FDADKKLSYF FASQVDVTLE RERLSGLERD NAALVAEVSN RLRTQEERER
     ELALALRAGG FGTWSFELQS RTLTASEDCK ALFGRALDQP FTFEDRIAAV HDDDRRRAID
     NMIEAGTQGR EHQEEYRIIW PDGSTRWISS RGQPFFDVAG RPVRVAGVSM DITHAKRAEL
     KRQALVRLND LFRDLDQSAD ISHAAAEILG QTLDVSRAGY GMVDRINETI MIERDWNAPG
     VTTIAGTLQF RAYGSYIEDL KQGETVCVDD SRLDPRTADT SAVLEAISAR AFINMPLHEQ
     GGFVALIFVN NDTPRHWSDD DVAFVREVAE RTRDAVERRR AEHELAELAA SLERQVAERT
     AELLRAEDAL RQSQKMEAVG QLTGGLAHDF NNLLTGIGGG LELIQLRLAQ GRAAEIGRYM
     DAAQDAVKRA AALTHRLLAF SRRQTLDPRP TDANALVSGL EDLVRRTVGP AILVETRLAA
     DLESILVDPS QLENAMLNLC INARDAMPDG GRLMIETQDR LLDDQAGRKY DITPGNYICL
     SVSDTGTGMD PETMSRAFEP FFTTKPIGSG TGLGLSMVYG FARQSGGHVH IHSTPGMGTT
     VAVYLPRNGR AVMAEASPAL LSAAPHAQGS ETVLVVDDEA SIRMLIIEAL ADLGYDVLEA
     PDGPTAMELL AQGRMIDLLV TDVGLPGMNG RQLADALRTT RPGLKVVFIT GYAENAVLNH
     DHLEAGMQII TKPFTMEVLA SRITALLS
//
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