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Database: UniProt
Entry: A0A0Q5UXM0_9SPHN
LinkDB: A0A0Q5UXM0_9SPHN
Original site: A0A0Q5UXM0_9SPHN 
ID   A0A0Q5UXM0_9SPHN        Unreviewed;       791 AA.
AC   A0A0Q5UXM0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-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=ASG20_08095 {ECO:0000313|EMBL:KQS49030.1};
OS   Sphingomonas sp. Leaf198.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736299 {ECO:0000313|EMBL:KQS49030.1, ECO:0000313|Proteomes:UP000050871};
RN   [1] {ECO:0000313|Proteomes:UP000050871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf198 {ECO:0000313|Proteomes:UP000050871};
RA   Garrido-Oter R.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000050871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf198 {ECO:0000313|Proteomes:UP000050871};
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:KQS49030.1}.
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DR   EMBL; LMPX01000002; KQS49030.1; -; Genomic_DNA.
DR   RefSeq; WP_056050907.1; NZ_LMPX01000002.1.
DR   AlphaFoldDB; A0A0Q5UXM0; -.
DR   STRING; 1736299.ASG20_08095; -.
DR   OrthoDB; 9796100at2; -.
DR   Proteomes; UP000050871; 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   CDD; cd17536; REC_YesN-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   Gene3D; 3.30.450.20; PAS 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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13188; PAS_8; 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   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KQS49030.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000050871};
KW   Transferase {ECO:0000313|EMBL:KQS49030.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          422..650
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          674..788
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         724
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   791 AA;  84204 MW;  B3744408BC811BB6 CRC64;
     MASLALPTPA RNAALVAIAS GVVAAAIVLL LVGSWIVAAG FFAAAAIVIG ALIAWRLLNP
     VAKDAPRPVD WDLTRTVAEA GTDAIAITDR AGRLVCANDA YDALFAGFPT PPGLPLDDVG
     TAALADAGRT AWRDGIARVE RLNARGICLS AHIARAGDEA DMLVWRFVTA QDHDLAETLA
     ALLPGPTGDR LGGSGIMAAL LSTDGRVRTA NRVLRARASG NDHESIDGRD FASFLITDSR
     GFVRFEREGL EGTPLRVLQV PFLEGDDAPV LVALLDDEEA APPVGASAAA HVRSLVSLMP
     FGMALVDRDG RFLQMNTSFL RAAGVNPVAP PLYPGDLVVR EDKAAVADAI RKFANGATHS
     ADMAVRLKDH PDEPVALTIA GARGLGDAAV LLSLKDNSEE SRLKREVAQA TKMQAVGQLA
     GGVAHDFNNI LTAIIGHCDL MLMRHSPGDS DYDDIQQVRT NSNRAASLTR QLLAFSRQQT
     LRPQILQLPD VVSEVSNLLK RLMGENVRLD MTHGRNLGPV RADPGQLEQV VVNLAVNARD
     AIVSANARGG GVLTITTRAV YASEVRAMAS DILPVADYTA LIVQDTGTGI PPDVLPKIFE
     PFFTTKEFGR GTGLGLSTVY GIVKQSGGYI FADSKLGQGA TFTMYLPVHS APAATRPAIV
     KPAPKPVDLW GTGTILLVED EDMVRAVAER ALSRQGYTVL TAENGEVALE VLEKHGRPDL
     LISDVVMPQM DGPTMVRHVR EKYPDLPILF MSGYAEEQLR KSIDLDNVSF LPKPFSVQEL
     AEAARDVLAT R
//
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