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Database: UniProt
Entry: A0A2L0AFQ2_9SPHN
LinkDB: A0A2L0AFQ2_9SPHN
Original site: A0A2L0AFQ2_9SPHN 
ID   A0A2L0AFQ2_9SPHN        Unreviewed;       756 AA.
AC   A0A2L0AFQ2;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=C1T17_20685 {ECO:0000313|EMBL:AUW60624.1};
OS   Sphingobium sp. SCG-1.
OG   Plasmid unnamed {ECO:0000313|EMBL:AUW60624.1}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=2072936 {ECO:0000313|EMBL:AUW60624.1, ECO:0000313|Proteomes:UP000239825};
RN   [1] {ECO:0000313|EMBL:AUW60624.1, ECO:0000313|Proteomes:UP000239825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCG-1 {ECO:0000313|EMBL:AUW60624.1,
RC   ECO:0000313|Proteomes:UP000239825};
RC   PLASMID=Plasmid unnamed {ECO:0000313|Proteomes:UP000239825};
RA   Tavormina P.L.;
RT   "Members of Methylobacter and Sphingobium form part of a microbial response
RT   to natural gas loading in southern Californian soils.";
RL   Submitted (JAN-2018) 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; CP026373; AUW60624.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2L0AFQ2; -.
DR   OrthoDB; 9764438at2; -.
DR   Proteomes; UP000239825; Plasmid unnamed.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00156; REC; 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; 2.
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; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; NF041832; near_NosP_CTERM; 1.
DR   PANTHER; PTHR43047:SF9; 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; 2.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 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); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AUW60624.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Plasmid {ECO:0000313|EMBL:AUW60624.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239825};
KW   Transferase {ECO:0000313|EMBL:AUW60624.1}.
FT   DOMAIN          400..611
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          632..750
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          202..229
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         684
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   756 AA;  83145 MW;  6CF5E3743298FFE7 CRC64;
     MTKTFESLGR HANGSAEYEL QKLRRINTAL INRVERATDL QGNAFSLFET AITLESRVRD
     RTVELERTLS ELAAASASSL QARSIAEDAQ RRLRDAIDTI NEGFALFDQN DRLVLCNQTY
     LGLWPRIADR IHAGMAFSEI AQMIVTDGTT LGAMVAPDRW VSERSRQHAV AAGGHVHALA
     DGRWIQINER RTSDGGIVCL YTDITEAKAE DARQRAQELA EKSTLLQATL DNIPQGVCVF
     GPTGELVAWN GSLRALLDLP ADVADAIATH GRFLSLWNVR RADIGENDCV EWLGSEEKER
     IVQRSLSDGR SLEIRRARMP DGGLMITFSD ISESRRAATV LLEANDSLER RVAERTSEMA
     AVNSKLQREI AERLGVEAAL REAKGLAEQA NLSKTRFLAA ASHDLLQPLN AARLFVSALE
     DRRMALASRA LINQTSSALE SVEYLLEALM EISKLDAGAV VPELREFPIG DLLRNMKAEF
     LPLARAGGLE LRISDCGTWV RSDARLLRRV LQNFISNAIK YTKTGTVSVE WTIRGDVVRL
     SVTDTGPGIP AEHHVEVFQE FFRLDGGAPN RGMGLGLAIV QRASRMLDHP VHLESKQGVG
     STFSIDVPTT TAQATSIAIP ALAKRRDLSA LRILVIDNDI SILSAMTALL SGWGCEVLTA
     RAADEAVSYL RSHDAILPHL ILADYHLDCD ALGDDAVRLF RSEANAQIAA IIITADRSPD
     LRQHLMRNGF HVLTKPLKPA QLRAMLSRTV EDLHLP
//
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