ID A0A0J1J2J3_9FIRM Unreviewed; 577 AA.
AC A0A0J1J2J3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=RHS_2820 {ECO:0000313|EMBL:KLU71346.1};
OS Robinsoniella sp. RHS.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Robinsoniella.
OX NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU71346.1, ECO:0000313|Proteomes:UP000036477};
RN [1] {ECO:0000313|EMBL:KLU71346.1, ECO:0000313|Proteomes:UP000036477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHS {ECO:0000313|EMBL:KLU71346.1};
RX PubMed=25284151; DOI=10.1016/j.cell.2014.09.008;
RA Seedorf H., Griffin N.W., Ridaura V.K., Reyes A., Cheng J., Rey F.E.,
RA Smith M.I., Simon G.M., Scheffrahn R.H., Woebken D., Spormann A.M.,
RA Van Treuren W., Ursell L.K., Pirrung M., Robbins-Pianka A., Cantarel B.L.,
RA Lombard V., Henrissat B., Knight R., Gordon J.I.;
RT "Bacteria from diverse habitats colonize and compete in the mouse gut.";
RL Cell 159:253-266(2014).
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:KLU71346.1}.
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DR EMBL; JNGB01000024; KLU71346.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1J2J3; -.
DR Proteomes; UP000036477; 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 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; IPR010559; Sig_transdc_His_kin_internal.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR SMART; SM00304; HAMP; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000036477};
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 278..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 303..355
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 464..568
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 577 AA; 65311 MW; 0FF028FABB250316 CRC64;
MRLKEKLILT FSVLVIISSA GISFASMAVF QAVYKEKSRQ YIMDITRQTT NNLENNIDEM
ETITFNTLKN TKIQEQLGIV NTKTLSEYEK LLVKRSVEEE LIGDALYNKN VTSLSVISLT
EEAFTVQKQV GEQVIQMFSG NEVFDAKGST LWKLTDDGQN GICIERAIYD FKTQRPIGII
DLVCEEAYFS DILEDISNTY TSGTYIVDTD GIVVASNNRK HVGSYFPVEL ERLQNMENDS
RAEINEVDSY LYTGEKMPNG WMLVTTVAVG EIQKDIRYFA LFSGGIALLA IVVAVVAIIL
MIRHITFPLG QLSKSMTAVG QGDFSGRVHI AGNDEIGSLG RTYNDMAKNI ETLIEKVYKM
EISQKQAEIE FLKMQINPHF LYNTLDTISW MARSGGNNDI SDMAVTLADL LRATIKQDSF
ITIDEELKSV RNYLFIQEYR FGDKVEASYQ IDNLTRDYII PNFILQPLVE NAIIHGLEPK
LGKGNLNIEI RMQEQGIFFC VSDDGVGMTP EEVRRTYEQC ERDDGRESIG IKNVYRRLKI
YYGAEGTLKI ESAKDEGTKI TFCLSLKKLN EQLENEI
//
