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Database: UniProt
Entry: A0A1H0U6W8_9CLOT
LinkDB: A0A1H0U6W8_9CLOT
Original site: A0A1H0U6W8_9CLOT 
ID   A0A1H0U6W8_9CLOT        Unreviewed;       592 AA.
AC   A0A1H0U6W8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN04488529_109100 {ECO:0000313|EMBL:SDP62017.1};
OS   Clostridium gasigenes.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=94869 {ECO:0000313|EMBL:SDP62017.1, ECO:0000313|Proteomes:UP000198597};
RN   [1] {ECO:0000313|EMBL:SDP62017.1, ECO:0000313|Proteomes:UP000198597}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12272 {ECO:0000313|EMBL:SDP62017.1,
RC   ECO:0000313|Proteomes:UP000198597};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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};
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DR   EMBL; FNJM01000009; SDP62017.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0U6W8; -.
DR   STRING; 94869.SAMN04488529_109100; -.
DR   OrthoDB; 9762826at2; -.
DR   Proteomes; UP000198597; 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; IPR008358; Sig_transdc_His_kin/Pase_MprB.
DR   PANTHER; PTHR45453:SF3; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR01780; LANTIREGPROT.
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:SDP62017.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198597};
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..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        273..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          295..347
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          376..587
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   592 AA;  67915 MW;  60E951CB2B213C43 CRC64;
     MILNKLFKKS IFYKLFFMNL IILVCIVVSQ LFFQTVYFEK YYLNEKAKDL KIEVNKFSTL
     LNYENDKVKI MDYIRTVNKE SGITLAFRSK DYNENINMND YMQSENIIVN DDISGNEYRI
     VLGDQFKNVK VKKGDRVETY GMSDDYGYVF LSKIFVNNVE IKPIYDIVPS ELNVAAEILK
     PAYSLNSSNS NINVSGVVSN IKYESKSYFI NIDLYLSLDE NNYILNNKNY EAKLKSPSGD
     NEILLNSESR GNGSVVAFSN LSQVNDIMGT MNGFYFIIFF IILILVIIIS IVYSKFMIRP
     LLDMSKVAKR ISECDFNHNY EVDREDEIGT LGNSLNLISD NLQGALNELK SSNIKLKEDI
     NIQSIQEEKR KELVANISHE LKTPITIIQG VIGGIKNGIY TTEMYDDILE ETGKMNDLVK
     EMLEISKLES PAFKLKKEPF DLCRVILKEN DKLRSMINKK KLNFNIDIND EAIAVGDEKR
     INQVITNLFT NAIKYTPCGE NINLKVELDG KKYKFTIENF GVTLEEEDLK NIWNSFYRGE
     KSRNKKYGGT GLGLFIVKII LELHGSNFGV ESGSNSVIFF FDLECYENNL SN
//
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