ID A0A1E4J738_9BURK Unreviewed; 635 AA.
AC A0A1E4J738;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Histidine kinase {ECO:0000313|EMBL:ODU18359.1};
GN ORFNames=ABS94_04770 {ECO:0000313|EMBL:ODU18359.1};
OS Variovorax sp. SCN 67-85.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1660152 {ECO:0000313|EMBL:ODU18359.1, ECO:0000313|Proteomes:UP000094461};
RN [1] {ECO:0000313|EMBL:ODU18359.1, ECO:0000313|Proteomes:UP000094461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
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:ODU18359.1}.
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DR EMBL; MEFM01000011; ODU18359.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4J738; -.
DR Proteomes; UP000094461; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR Gene3D; 1.20.5.1930; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR PANTHER; PTHR24421:SF37; SIGNAL TRANSDUCTION HISTIDINE-PROTEIN KINASE_PHOSPHATASE UHPB; 1.
DR Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ODU18359.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:ODU18359.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 200..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 255..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 317..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 376..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 443..630
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 635 AA; 70617 MW; 17A3210B27340EE9 CRC64;
MTLLAVIGAF FGGSSGLQKS NAALHLKQAD WQVEDTTGFS APPLRQQAGD LPDAWQPIEL
PLAPPIALLR QADSDAAVGM SRAARPTRTT WLRVSTRHLP PSNGPLALYG ARIKTDGTVA
VYADGRLVHR AQQLGPLWNS TRTPLWVELD RGPENTPPHE ILIRLEHSRN AQIAVSSLWV
GPIEALRGRH GLRQWLQQEL PAMLSAAFMA VGVFALFVWL RRRDEVGYLL FFNLSATSFM
RGLHFYVGQP IANDWFAWLT VNSLFWLVLV VHFFLRQLHQ RRLKWLTWAV VLATSAVGVL
TMPGLNLVQN TPRVTPLIYA VAALMGTAVC LIGSISAWRR STEGRLVAAG IGICVLLGIT
DWLLQNNFIS PEGWYLGAYT NAVSFSVFGV LMYRRYVHAI GAVEQLNDSL AERLRKREAE
LELSHQRLRD VERLRTISEE RQRLMQDMHD GLGSSLVSAI RSVEGGGMSD EKVSQILKSC
LDDLKLTLDS LEPVDADLLL LLATLRYRLA PRLEGTGVSL RWEVQELPAL PWLDPSSALH
ILRIVQESIS NILRHTRATE IRVETALVDS GVRVTIEDNG PGFDVDKVLA SPSGRGMQNQ
RRRARSIGGA VSWESRPTGT RFMLWLPLIR EAEAA
//
