ID   U2EJR4_9FIRM            Unreviewed;       567 AA.
AC   U2EJR4;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=HMPREF1547_02627 {ECO:0000313|EMBL:ERI93126.1};
OS   Blautia sp. KLE 1732.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX   NCBI_TaxID=1226324 {ECO:0000313|EMBL:ERI93126.1, ECO:0000313|Proteomes:UP000016485};
RN   [1] {ECO:0000313|EMBL:ERI93126.1, ECO:0000313|Proteomes:UP000016485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLE 1732 {ECO:0000313|EMBL:ERI93126.1,
RC   ECO:0000313|Proteomes:UP000016485};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA   Wilson R.K.;
RL   Submitted (JUN-2013) 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:ERI93126.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AWSY01000129; ERI93126.1; -; Genomic_DNA.
DR   RefSeq; WP_021650824.1; NZ_KE993319.1.
DR   AlphaFoldDB; U2EJR4; -.
DR   PATRIC; fig|1226324.3.peg.2368; -.
DR   HOGENOM; CLU_020473_6_0_9; -.
DR   OrthoDB; 9809348at2; -.
DR   Proteomes; UP000016485; 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, ECO:0000313|EMBL:ERI93126.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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        281..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          300..352
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          463..562
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   567 AA;  65430 MW;  926623F65C783C4B CRC64;
     MKSLLKKYNN MKYRYKLTNL LVVVSLVPMT VLALYSHSRM SSLVRKNEME DMYSILEQTR
     ENIDGQIEIY ASLLNYLTYS PEIQEVIFNK DMDRYTAYEQ YTEVVDPLLT VPKSYHEAIL
     GIHLFAESIP VRHEYTLAPL SEVDGEWWSD KLNNTVTVQW IVDRDNRQIA AVREIYDGKI
     REAVLCILLD YGKVFQPLAN IIERNSGGFV VDDQQNIVYH GENLAASDIS AQKETAKKLD
     RLREEYTYVS SSGHETRWTY YFYKPPAVIE SSVSKVLISE IPLIGFCVVI IIVLGMTFSK
     LFTRKIEQLT RNMEQVNQGS REVTVYSDSG DEVGQLVRSF HHMMDEINRL IEEVYENKIA
     LKEFELKALT AQINPHFLYN SLSIINWMAI KSRQKEISRV TLALSTFYRT ALSKGADMVT
     VETCIRNIEA YLEIQLIMHD NDFKVEWNID PSVQQELVPK LALQPIVENA LEHGLDVKEE
     GEKLLKLYFF EENGDVVIRV EDNGIGMEQE QAEKLLTYQA KGYGLKNVND RMCILYGEKY
     AIRILSKVGE GTSVDMRIPK EVKKDET
//