ID G2E869_9GAMM Unreviewed; 311 AA.
AC G2E869;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Hpt protein {ECO:0000313|EMBL:EGV27705.1};
GN ORFNames=ThidrDRAFT_4483 {ECO:0000313|EMBL:EGV27705.1};
OS Thiorhodococcus drewsii AZ1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiorhodococcus.
OX NCBI_TaxID=765913 {ECO:0000313|EMBL:EGV27705.1, ECO:0000313|Proteomes:UP000004200};
RN [1] {ECO:0000313|EMBL:EGV27705.1, ECO:0000313|Proteomes:UP000004200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AZ1 {ECO:0000313|EMBL:EGV27705.1,
RC ECO:0000313|Proteomes:UP000004200};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V.,
RA Frigaard N.-U., Bryant D.A., Woyke T.J.;
RT "The draft genome of Thiorhodococcus drewsii AZ1.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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:EGV27705.1}.
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DR EMBL; AFWT01000066; EGV27705.1; -; Genomic_DNA.
DR RefSeq; WP_007043195.1; NZ_AFWT01000066.1.
DR AlphaFoldDB; G2E869; -.
DR STRING; 765913.ThidrDRAFT_4483; -.
DR eggNOG; COG2198; Bacteria.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000004200; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:UniProt.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR PANTHER; PTHR43395:SF8; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01627; Hpt; 1.
DR SMART; SM00073; HPT; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR PROSITE; PS50894; HPT; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 287..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..110
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 135..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 311 AA; 34244 MW; 83152F0BC88F60F5 CRC64;
MSTITLDADD QEIIEIFVEE AEEVLQEIDQ NLKALKGNPK DRNALGEVRR GFHTLKGSGR
MAKAMDLGEL AWKMENMLNR ALEGKIAIGE PMVTLLAHCH GAMPKLVDDF KRHRPSDMNA
DIQTMMAQAD AIANGEPQAA AAKRPSAAPS GGGNDIQAKL DELQRIVEQS ARRSDEALHR
AEMGLQQSRK LANQLDTIGA ELQGQPAGGI DLKPLFERVN TLTRDVRELR ELSRGAQPPA
GTPDTRELQH LIDQRIRERT HGKDRSRQEL EERLDAVLQA ALSARRLGVW ALTIGILLML
AAGGTAAYFF L
//
