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Database: UniProt
Entry: A0A1J0GEQ7_9CLOT
LinkDB: A0A1J0GEQ7_9CLOT
Original site: A0A1J0GEQ7_9CLOT 
ID   A0A1J0GEQ7_9CLOT        Unreviewed;       486 AA.
AC   A0A1J0GEQ7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=A7L45_07105 {ECO:0000313|EMBL:APC39852.1};
OS   Clostridium estertheticum subsp. estertheticum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1552 {ECO:0000313|EMBL:APC39852.1, ECO:0000313|Proteomes:UP000182569};
RN   [1] {ECO:0000313|Proteomes:UP000182569}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8809 {ECO:0000313|Proteomes:UP000182569};
RX   PubMed=27891116;
RA   Yu Z., Gunn L., Brennan E., Reid R., Wall P.G., Gaora O.P., Hurley D.,
RA   Bolton D., Fanning S.;
RT   "Complete Genome Sequence of Clostridium estertheticum DSM 8809, a Microbe
RT   Identified in Spoiled Vacuum Packed Beef.";
RL   Front. Microbiol. 7:1764-1764(2016).
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; CP015756; APC39852.1; -; Genomic_DNA.
DR   RefSeq; WP_071612146.1; NZ_CP015756.1.
DR   AlphaFoldDB; A0A1J0GEQ7; -.
DR   STRING; 1552.A7L45_07105; -.
DR   KEGG; ceu:A7L45_07105; -.
DR   OrthoDB; 9813394at2; -.
DR   Proteomes; UP000182569; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR007891; CHASE3.
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; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF05227; CHASE3; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182569};
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..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        185..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          236..459
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   486 AA;  55268 MW;  5B8258E17491A361 CRC64;
     MNKTDYRSKK VMLLGCFSAA CLSLIIILFS TYSMNKVRIE SDFISQRILP SKIFTLEILT
     SLINQETGIR AYIISENKVF LEPYYSESIG IQKYYNSLNK LKEVGLNNDT INRIDKQRQY
     IQRFFYQQIL LVESGESDQA KLNLTKGKKL VDEFRVTDNI LLNDINSQIN SSSNKVIKTQ
     RIHKYLLAFL GVILIACNCI FINCIWNCMH KQIKKKDEVN EDLQKVLTSQ EEYITSISHE
     LKTPLNVILS AAQLLDMYSD SGLLYENKKS TIKHIDSIKQ NAYRLSKFIN NIIDLSRIES
     GIFKLNLSNN NIVEIVEDMV IAVTEFTKSR GLNIIFDTDV EEKIIACDPE KVDKVVLNII
     SNAIKFSSDG GQIFVNIKND IEFVEISVED NGIGIDTKYF NSIFNKYSQI DKSLSRNAEG
     TGVGLTLVKS IVELAGGSIN VESELGIGSK FTVRFPSKQV LNEKIQSNNA MRNEKQNVKV
     EFSDVY
//
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