ID A0A1M3DBA7_9SPHN Unreviewed; 794 AA.
AC A0A1M3DBA7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BGO24_05310 {ECO:0000313|EMBL:OJV31742.1};
OS Sphingomonas sp. 67-36.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1895849 {ECO:0000313|EMBL:OJV31742.1, ECO:0000313|Proteomes:UP000183964};
RN [1] {ECO:0000313|EMBL:OJV31742.1, ECO:0000313|Proteomes:UP000183964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=67-36 {ECO:0000313|EMBL:OJV31742.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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};
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:OJV31742.1}.
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DR EMBL; MKSU01000016; OJV31742.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3DBA7; -.
DR STRING; 1895849.BGO24_05310; -.
DR Proteomes; UP000183964; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 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; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF42; TWO-COMPONENT SENSOR PPRA; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
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); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:OJV31742.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:OJV31742.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 427..654
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 677..791
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 727
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 794 AA; 84469 MW; 469463150E1F85D0 CRC64;
MASRSPVSPT LLTPRTALPI AAAAALLAAL LVLWLVGNRV FAAGFGASAI VVVGAVIAWR
SLGQGRDEAD SEPDWGLARA VTQTSRDAVA ITDRGGRLVC ANDLYETLFG GFPTPPDLTA
KEGSVSALAS AGRAAWRDGE AQVAQLRLDR QTVSVEITRA GDRQDMLIWR FERAADANRV
DRLTDALAGD LGDRLGAAGI MAAMIAPDGH ILAANPVFSH RALGRIEGRV EGMDFARFLI
TDSRGLVRFE REGLDGNPLR LVQVPFADGD GGPILIAMLD DEEAPAHDGA TTSSHVSTLV
SLMPVGIALV DREGRFVQMN NAFARAAGID PAVPPLYPGD LVVREDKAAV ADAVRRFANG
AAQSSDMAVR LRDHPDEPVA LTIAGARGLG QAAAVVLSLK DNSEESRLKR EVAQATKMQA
VGQLAGGVAH DFNNILTAIL GHCDLMLMRH SPGDSDYDDI QQIRSNSNRA AGLTRQLLAF
SRQQTLRPQV LQLPDVVSEV SNLLKRLLGE TVTLNVSHGR DLGAVRADPG QLEQVVVNLA
VNARDAMMTK NPHGGGTLTI RTRSVGLAEV RGRGDIMPAA DYTALEISDT GTGIPPEVLP
KIFEPFFTTK EVGKGTGLGL STVYGIVKQS GGYIFADSRP GQGATFTIYL PVHNSGTVAA
ARAPARPRQT DLWGSGTVLL VEDEAMVRAV AERALSRQGY TVLSAENGEA ALELLESCQP
PDLLISDVVM PTMDGPTMAR HVRERYPHLP ILFMSGYAEE QLRRSIDLDN VAFLPKPFSV
QQLAEAARDA LTAA
//