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Database: UniProt
Entry: A0A0N0D9J2_9RHOB
LinkDB: A0A0N0D9J2_9RHOB
Original site: A0A0N0D9J2_9RHOB 
ID   A0A0N0D9J2_9RHOB        Unreviewed;       343 AA.
AC   A0A0N0D9J2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=phoR_1 {ECO:0000313|EMBL:KPA22562.1};
GN   ORFNames=shim_08480 {ECO:0000313|EMBL:KPA22562.1};
OS   Shimia sp. SK013.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae.
OX   NCBI_TaxID=1389006 {ECO:0000313|EMBL:KPA22562.1, ECO:0000313|Proteomes:UP000037951};
RN   [1] {ECO:0000313|EMBL:KPA22562.1, ECO:0000313|Proteomes:UP000037951}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK013 {ECO:0000313|EMBL:KPA22562.1,
RC   ECO:0000313|Proteomes:UP000037951};
RA   Voget S., Kanukollu S., Daniel R., Engelen B.;
RT   "Genome Sequence of Shimia sp. SK013.";
RL   Submitted (MAR-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:KPA22562.1}.
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DR   EMBL; LAJH01000009; KPA22562.1; -; Genomic_DNA.
DR   RefSeq; WP_054001342.1; NZ_LAJH01000009.1.
DR   AlphaFoldDB; A0A0N0D9J2; -.
DR   STRING; 1389006.shim_08480; -.
DR   PATRIC; fig|1389006.3.peg.865; -.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000037951; Unassembled WGS sequence.
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   Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
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; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 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   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037951};
KW   Transferase {ECO:0000313|EMBL:KPA22562.1}.
FT   DOMAIN          119..343
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   343 AA;  38178 MW;  4C7D0CC4195F5BCC CRC64;
     MTENFNASVL EAVPLPAFFV DADGRVTAAN ARAVELQPQA SENRPLILVF RQPALNDAVE
     KCLRTRQQQR SLYLHNDGRQ EHRYEVLCSP VEGGGGIVCF RDVTEERQLD QMRRDFVANV
     SHELRTPLTA ILGFIETLQG PAKNDPVAQE RFLTTMSNEA SRMNRLVGDL LSLSKVEEVS
     RMRPTDPVDL CRIVNASVQN LSPLAEENRS ALTFENENSD QTVLGDSDQL LQVVTNLIEN
     AIKYGGQGTN VTLSLSELPR VLGVRGPAVR LTIRDNGPGI DEIHLPRLTE RFYRIDSHRS
     REKGGTGLGL AIVKHIIHRH RGRLEIESVL GEGTEISVFL PVH
//
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