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Database: UniProt
Entry: A0A0D0F072_9SPHI
LinkDB: A0A0D0F072_9SPHI
Original site: A0A0D0F072_9SPHI 
ID   A0A0D0F072_9SPHI        Unreviewed;       359 AA.
AC   A0A0D0F072;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=TH53_23180 {ECO:0000313|EMBL:KIO75023.1};
OS   Pedobacter lusitanus.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1503925 {ECO:0000313|EMBL:KIO75023.1, ECO:0000313|Proteomes:UP000032049};
RN   [1] {ECO:0000313|EMBL:KIO75023.1, ECO:0000313|Proteomes:UP000032049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NL19 {ECO:0000313|EMBL:KIO75023.1,
RC   ECO:0000313|Proteomes:UP000032049};
RA   Santos T., Caetano T., Covas C., Cruz A., Mendo S.;
RT   "Draft genome sequence of Pedobacter sp. NL19 isolated from sludge of an
RT   effluent treatment pond in an abandoned uranium mine.";
RL   Submitted (JAN-2015) 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:KIO75023.1}.
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DR   EMBL; JXRA01000119; KIO75023.1; -; Genomic_DNA.
DR   RefSeq; WP_041886159.1; NZ_JXRA01000119.1.
DR   AlphaFoldDB; A0A0D0F072; -.
DR   STRING; 1503925.TH53_23180; -.
DR   OrthoDB; 9781208at2; -.
DR   Proteomes; UP000032049; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17569; REC_HupR-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
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   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:KIO75023.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:KIO75023.1}.
FT   DOMAIN          7..121
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          150..359
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          120..147
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         55
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   359 AA;  40730 MW;  F5AB4929C95E1F33 CRC64;
     MTRSPVKVLY IDDEENNLLA FKASFRRQYE IYTAISAAEG LKVLENLPVE VIIADQKMPE
     TTGVEFFKSI ATTYPDPVRI LLTGYTDIAA LADAINHGDI YRYITKPWND LELHNSIKNA
     HDAYRSKIDL RNKIKELEKT NDELNRFIYS ISHELRAPLV SVIGIVNLVK MEGLYNSSGE
     YWELIESCSN KLDYYIQKTL QYYKNNKNIS ENSPIDFKTL VDEMIDLYAY SDRDTQFNLN
     INQSHPFMGD SFRIEVILGN LISNAIKYQK ESGHHKVVDI AIEANLLSAE ISITDNGLGI
     LNEHLEKIFT QFFKAKNNKG SGLGLFIVKE ALNKIDGTIA VSSSLNHGTT FKITIPNAK
//
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