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Database: UniProt
Entry: A0A1M3DBA7_9SPHN
LinkDB: A0A1M3DBA7_9SPHN
Original site: A0A1M3DBA7_9SPHN 
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
//
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