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Database: UniProt
Entry: E4KWT8_9FIRM
LinkDB: E4KWT8_9FIRM
Original site: E4KWT8_9FIRM 
ID   E4KWT8_9FIRM            Unreviewed;       602 AA.
AC   E4KWT8;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=HMPREF9286_1618 {ECO:0000313|EMBL:EFR33769.1};
OS   Peptoniphilus harei ACS-146-V-Sch2b.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Peptoniphilus.
OX   NCBI_TaxID=908338 {ECO:0000313|EMBL:EFR33769.1, ECO:0000313|Proteomes:UP000003705};
RN   [1] {ECO:0000313|EMBL:EFR33769.1, ECO:0000313|Proteomes:UP000003705}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-146-V-Sch2b {ECO:0000313|EMBL:EFR33769.1,
RC   ECO:0000313|Proteomes:UP000003705};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (OCT-2010) 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:EFR33769.1}.
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DR   EMBL; AENP01000004; EFR33769.1; -; Genomic_DNA.
DR   RefSeq; WP_005955412.1; NZ_AENP01000004.1.
DR   AlphaFoldDB; E4KWT8; -.
DR   eggNOG; COG5002; Bacteria.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000003705; 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; cd00075; HATPase; 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   Gene3D; 3.30.450.20; PAS 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; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 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:EFR33769.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003705};
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        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          202..254
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          376..593
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   602 AA;  67679 MW;  7022D7F59D00F632 CRC64;
     MNHSIKSRFI LIYVVLVLIS MFIASTFIID RLENVQIETA TSSMVKTMDT LATTTSAFFK
     DNNYKTLPQL DATLKDWGIS SEETAYVISP DKAPKILAST QNISPKEAED AYSVKFIEPK
     LVMDAAGGKT REKIVEYKNL GDVEKHIARP ILSGDGDILA IIYMTRNLNS IYSVIEDSKV
     IITYATLISL LTTSILGYFI ANSITGPIRT LTKKAKALAK GNFNQSIEVK SNDEIGELGM
     MFNFLTKELR ESIEKMDLER SKLDTIFNYM AEGVIAIDRK NRLIHANSIA KKILNISEKD
     FNRVINLKSI NLYNIDYKNE ESLRGEELTK IANSFYKIKY APYKSDAFIN SGLIIVLQDV
     DKEHMLDIMR KEFVANVSHE LKTPITTIKS YTETLLDSDL DKKSQRNFLK IIDRENSRMS
     RIVTDLLYLS NIDYNKDNLT LSSIDTYEFI AEAIESQSIL IVQKNHKIEL NIDMDIKDIY
     ADRSGADQIL TNIISNACKY TPENGKIVID ATNKGDLVEI KVTDNGIGIP KEDLPRITER
     FYRVEKGRSR QMGGTGLGLS IANEMIKSFG GSLKVDSVFG EGTTITLLFK ASEGDNNDEE
     LA
//
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