ID A0A1M4Y1D2_9BACT Unreviewed; 1322 AA.
AC A0A1M4Y1D2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05444362_10344 {ECO:0000313|EMBL:SHE99499.1};
OS Dysgonomonas macrotermitis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC Dysgonomonas.
OX NCBI_TaxID=1346286 {ECO:0000313|EMBL:SHE99499.1, ECO:0000313|Proteomes:UP000184480};
RN [1] {ECO:0000313|Proteomes:UP000184480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27370 {ECO:0000313|Proteomes:UP000184480};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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};
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DR EMBL; FQUC01000003; SHE99499.1; -; Genomic_DNA.
DR STRING; 1346286.SAMN05444362_10344; -.
DR OrthoDB; 9811889at2; -.
DR Proteomes; UP000184480; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 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; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
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; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12833; HTH_18; 1.
DR Pfam; PF07494; Reg_prop; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF07495; Y_Y_Y; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00342; HTH_ARAC; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Kinase {ECO:0000313|EMBL:SHE99499.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000184480};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:SHE99499.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1322
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009908370"
FT TRANSMEM 772..791
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 824..1041
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1062..1177
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1209..1308
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1110
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1322 AA; 152124 MW; 8CAAE14A1B36A824 CRC64;
MYLFHSSYMK RILPILFVIL SAVSVQSQEY THYTTIDGLS GTDVTAICEN ENFLWIATND
GLNRFDGREF KVYRNDNTSA NSISENNIET LMFDSQGFLW IGFKTGGVDI FNPRKNKFIH
ISDVIKDYPQ RVICIYEDSK KNIWLGTWED GLYQLTPTNE GDLSYHVSKH YPKNIVSSIV
EKPKGKLWIG TYYGFFLYDI ENKRDVPLKE NYYAVTQFLD TGEKNSLWFS VWTNGLYKLE
WDEKTFRTKE TSMTKNMEDV YRIFPATDNK LYLGTWGNGV KVTQMLSDAY PESLQIDAPV
ILSFYRDRHR RFWVGTYGTG LFRLNDKSRG ITNLSPINTN GLSAAYSLRY FGSGQLLIGT
QGDGLYLYDI KNHNLRPQFI KNTGSLFHKY ILSLYRDNEV LIVGNDDTGL QYAPLKGTDN
TNFTLRTYHV DKNFGKVTAI FKSSNSTFWI GTKQYGLVSM KYDPAKENFT NYIHYDSFGM
DEITGFSETI DGQIWVSSHS GIYLFDPVTN KVQKYNNASE MIYSLADDQK NKCLWLGTSG
GLRKLSYTGD NKIENPFSSE VLPDGAIRDV ILDTYNNLWF SASNRIFCYT DSSRELKEIN
PGTPNQQLLF STTRCETGGK QYVIFGGTNS ILLIDPQVVL NQPEHTKILL TELQIDHQTV
DVGEKIYGKI VLNEDTEYIN SITLSYLCKW ISLSFTEVGW DNYYNSYQYQ IKGFSDDWQY
LDITKPITFS QLPPGNYTLQ IRLNNTSLND KNEPLWSLHI AITPPWWQTG TFYLVLSLAI
FMILLSLFFI IKNYYKKRQL QKLGEIEKKK KEELLQEKES FFAGLSHDLL TPFSLIIAPV
SDMMRDETMN EEQHEKLEII SKNATFLSDV FSTILDFKRA EQIDTEIKEK NIELVSFVNI
IVNAFDYLAK SDKIKLSYHS AIPNLYISID SIKLERILYN LISNALKFTK EEGEVDVLLD
YDEVAEVFYL KVKDTGIGIR QQNQEKVFEK FYREDKDSDT QGLGLGLYST RKFLHMMGGE
VHIESIPEKG TAFTINLPAK RINEPKPILD IKETVDTDGL FTILLVEDNT QLRDYLRKKL
AVHFEVAVAS NGAEALDFIK SNLPEIVVSD VVMPEMDGLT LCSIIKNTPM YSEVFVILLS
ARSSSEDEMQ GYKAGADFYI KKPFDPEILI KQMVNVYATR QQRRKQIITD LLSPQNDSAK
SHPKDDFLGK AVKIIEEHIM DENFKIDEFA AEMNLSKTVL HRKFKLIVGE TPNIFIRNIR
LHKAANMLKE TDLSISEIGY LTGFSQAHYF IKCFKELYQY TPKNFRVKNK TGDTHTETNE
SN
//
