ID A0A0J1IY13_9FIRM Unreviewed; 615 AA.
AC A0A0J1IY13;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=RHS_4521 {ECO:0000313|EMBL:KLU69651.1};
OS Robinsoniella sp. RHS.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Robinsoniella.
OX NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU69651.1, ECO:0000313|Proteomes:UP000036477};
RN [1] {ECO:0000313|EMBL:KLU69651.1, ECO:0000313|Proteomes:UP000036477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHS {ECO:0000313|EMBL:KLU69651.1};
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:KLU69651.1}.
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DR EMBL; JNGB01000077; KLU69651.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1IY13; -.
DR PATRIC; fig|1504536.3.peg.5955; -.
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 SMART; SM00387; HATPase_c; 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 313..332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 343..392
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 503..607
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 615 AA; 69956 MW; 3216529FB565A1BB CRC64;
MAGGAMFKNL RIYFERMNFD KKMKFFLSMA VVVSTMCILS ISTISSVKSV REKTMALAME
QINTLAENYQ SGLNNYKAIA WSIVMDKNVQ AYLKYNNAAG KDTDKNSVQS SEEKAQSAIT
QVENTNKATN TLSNVKNLQS NLNFLGVVSN TGSYLYKGDN GLAVTGFEET YQKDYVNSSF
AGYGEMRYTY NNAYFKGSRY TLNIYQPIYD TSYVGKKLGL LCMNINETTL IQIGSKANQK
IDSITCLVGL EGNVVTSSEP DSVMDEVDYK NLLTGTEGNF KKSGKLYLYK RLGIWDFYMV
MVIPEFELYR DSIMTMAMLS VVILFLVAIV LVQSSRIVHK AYQPLDKVIS KMDSVSEGKF
DTRIKEEKMG QDFQKLSHGF NEMMDRIVEL MEQVKVEQHQ MEQIRFNALQ SQIQPHFLYN
TLDCIHWQTL ANGDLESSTM VKALASYYRI CLSKGKDIIQ LSQELEHIKS YLTIQNIRYD
HIIQSEIDIS EEYFNVKIPK MTLQPLIENS IYHGLKIKEG KKGKVTIRAN QDGEDLIIIM
ADSGTGMTRD QIDEMNASIS QYDETFGYGV RNVNKRIEIL YGDGYGLRYS CNEQGGVTVR
IRLPLEQEIQ YKGVL
//
