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Database: UniProt
Entry: Q97J32_CLOAB
LinkDB: Q97J32_CLOAB
Original site: Q97J32_CLOAB 
ID   Q97J32_CLOAB            Unreviewed;       441 AA.
AC   Q97J32;
DT   01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2001, sequence version 1.
DT   24-JAN-2024, entry version 119.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=CA_C1454 {ECO:0000313|EMBL:AAK79422.1};
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK79422.1, ECO:0000313|Proteomes:UP000000814};
RN   [1] {ECO:0000313|EMBL:AAK79422.1, ECO:0000313|Proteomes:UP000000814}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
RC   {ECO:0000313|Proteomes:UP000000814};
RX   PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA   Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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DR   EMBL; AE001437; AAK79422.1; -; Genomic_DNA.
DR   PIR; C97079; C97079.
DR   RefSeq; NP_348082.1; NC_003030.1.
DR   RefSeq; WP_010964763.1; NC_003030.1.
DR   AlphaFoldDB; Q97J32; -.
DR   STRING; 272562.CA_C1454; -.
DR   GeneID; 44997957; -.
DR   KEGG; cac:CA_C1454; -.
DR   PATRIC; fig|272562.8.peg.1657; -.
DR   eggNOG; COG4585; Bacteria.
DR   HOGENOM; CLU_000445_20_15_9; -.
DR   OMA; PELTICS; -.
DR   OrthoDB; 9781904at2; -.
DR   Proteomes; UP000000814; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR   Gene3D; 1.20.5.1930; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   PANTHER; PTHR24421:SF10; NITRATE/NITRITE SENSOR PROTEIN NARQ; 1.
DR   PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AAK79422.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000814};
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..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        97..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        132..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        181..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          244..311
FT                   /note="Signal transduction histidine kinase subgroup 3
FT                   dimerisation and phosphoacceptor"
FT                   /evidence="ECO:0000259|Pfam:PF07730"
FT   DOMAIN          351..424
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|Pfam:PF02518"
FT   COILED          208..235
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   441 AA;  50737 MW;  F963B315510C88E6 CRC64;
     MESDRNLNYI NLFMIFVNLI IIVFTSEIMT ITLYKISSEF MARDFLDQIT VIPWKPQNIT
     IVSIGAYIIL IILITVKKKY AKFLNKWEIA ALLLCEIFFS VAIMTALNMS YNGIILFIIA
     DLVTNTKDKS NKIIFLILMI IIYIFSVYDF ISLKIKMVSF ENFLYYYTAN RRSYLMELKS
     ILNSINIIVF ILYMIVFIQV QMRENEKITS LNKKLNLANE KLEVMNVQLK EYAVKIGSMA
     ETRERNRMAR EIHDTLGHAL TGISVGIDAC LTTIDVSKEL TKKQLNIIAD VAREAIKDVR
     RSVKKLRPDA LENSSLQDAL NNMISRISKA TKTKVFLNAN IKLLKFGHDE EDTIYRIIQE
     GITNSIRHGQ AEEIYIDMIR RDKQLNITIR DNGKGCANVE EGFGLRHIEE RVKLLNGTVE
     YDGSDSFLIT VNIPIRWGDG S
//
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