ID D1PPI5_9FIRM Unreviewed; 477 AA.
AC D1PPI5;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SUBVAR_06300 {ECO:0000313|EMBL:EFB75447.1};
OS Subdoligranulum variabile DSM 15176.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Subdoligranulum.
OX NCBI_TaxID=411471 {ECO:0000313|EMBL:EFB75447.1, ECO:0000313|Proteomes:UP000003438};
RN [1] {ECO:0000313|EMBL:EFB75447.1, ECO:0000313|Proteomes:UP000003438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15176 {ECO:0000313|EMBL:EFB75447.1,
RC ECO:0000313|Proteomes:UP000003438};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2009) 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:EFB75447.1}.
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DR EMBL; ACBY02000026; EFB75447.1; -; Genomic_DNA.
DR RefSeq; WP_007047665.1; NZ_GG704769.1.
DR AlphaFoldDB; D1PPI5; -.
DR STRING; 411471.SUBVAR_06300; -.
DR GeneID; 78306444; -.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_6_9; -.
DR OrthoDB; 9813151at2; -.
DR Proteomes; UP000003438; 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; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EFB75447.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000003438};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 201..253
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 261..477
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 477 AA; 51603 MW; AEA75E43544C0A2F CRC64;
MSRRNTISRE FFSTIAVVLI LGLSVMCAIQ TALSAAYFVN ERRAALTAIL DGASALSQRF
AEGGDIVTKP LGDDRAQDAR SGFELFNTTS GALVFVAAED GQVLLHTDGG DFTEQAVPRE
LLDEMDAGGD VFDAGTLGGV YKDKYYTAGR RIDVGGSVGY LFAASPMTAL GSYILDMLVM
FGISAAAILL LCSLLCWVLA KRITGPIEDI SEAARRLGSG DFTARAPVDG CVELADFATT
FNNMAMRLQT IDNSRGQFMG NIAHELRTPM TTIKGFIDGM LDGTIPPEEN QHYLTIVSQE
TGRLARLVQN MLDITKLEAG EVPVHAQNYD LWKTVTDVVL SDEQRIEDGK IDIQGLGGPP
LAIYADPDFV HQVVYNIVDN AIKFTPEGGT ISFAAQKKGN MVEVRIENTG AGIAPEALPF
VFERFYKEDR SRGMNTRGSG LGLHICKILI NLSGGQIHAE SEEGKWCRFV FTLPAGN
//
