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Database: UniProt
Entry: A0A0Q4FZJ5_9SPHN
LinkDB: A0A0Q4FZJ5_9SPHN
Original site: A0A0Q4FZJ5_9SPHN 
ID   A0A0Q4FZJ5_9SPHN        Unreviewed;       785 AA.
AC   A0A0Q4FZJ5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ASE72_14305 {ECO:0000313|EMBL:KQM70575.1};
OS   Sphingomonas sp. Leaf20.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1735685 {ECO:0000313|EMBL:KQM70575.1, ECO:0000313|Proteomes:UP000051642};
RN   [1] {ECO:0000313|Proteomes:UP000051642}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf20 {ECO:0000313|Proteomes:UP000051642};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000051642}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf20 {ECO:0000313|Proteomes:UP000051642};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQM70575.1}.
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DR   EMBL; LMKN01000009; KQM70575.1; -; Genomic_DNA.
DR   RefSeq; WP_056022996.1; NZ_LMKN01000009.1.
DR   AlphaFoldDB; A0A0Q4FZJ5; -.
DR   STRING; 1735685.ASE72_14305; -.
DR   OrthoDB; 9797304at2; -.
DR   Proteomes; UP000051642; 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; 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; IPR035965; PAS-like_dom_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; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF12860; PAS_7; 2.
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   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KQM70575.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051642};
KW   Transferase {ECO:0000313|EMBL:KQM70575.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          570..785
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   785 AA;  84410 MW;  B6E7D05D2037253D CRC64;
     MVLGTWETVL AGVAVLLLVG VGAVLVYLGL RARADAASTI ADNENMRGLL DGSPAVATIV
     RSDGRVEMPR RMADWLGIPA PRYLADLSGD GSGLSTEDAA ALTADVTAAQ RAGRPFVRAV
     RPVGSTRAIT LRGGRAPGGM GATGSVLIWA FDATDSESEI NRLGAETARL GAAFDALTGL
     IEAAPMPMWY RARDLKLSMV NTAYVAAVEG QDAKDVIARG VELVEGSGRG GPLAGAAAAR
     EQGRPHEQIL PATIDGARRS LQIYDVPLPT GGVAGFAIDI EDLEQARSGA KRFAEAQRAM
     LDRVSAGVAQ FGGDRGLVFC NQPFRRMFAM RAEWLADRPE FDRVLERMRE ANRLPEVRDF
     PAWKAERREW FMQTGTMPNG GASEEIWHLR GGTHLRVVAQ PLPDGGLLLI FEDRTEHVQL
     ASARDTLLRV RTATFDNLFE ALGVFAADGR LQLWNNRFRV LWGLEEEFLA GHPRVDVFAE
     AAASKLATPS RSVLIPDLVR SATVERQQRA GRVAFADGRH FEFAGVPLPD GNALFTMLDI
     TDSKRAEQAL RDRANALEAA DKVKTAFVAN MSYELKTPLT SISGFAEMLH GGYAGKLGSQ
     AEGYLEAILE SVERLGLLVD DVLDLTRTDA DGMEIMRADV DLAAVTRAAG EAIHAVAKRR
     NLDFAVEIGR STGRVCGDAK RLREIVEHLL RHAVAGTGEG GRILLHTDGN ATHARIIVSD
     DGMGMSTEAV AHAFDRFAES KTIGDRALGL GLPLAKQFVE AHNGTIELVS EPGSGTLVTV
     ELPRR
//
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