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Database: UniProt
Entry: U5N8G3_9BURK
LinkDB: U5N8G3_9BURK
Original site: U5N8G3_9BURK 
ID   U5N8G3_9BURK            Unreviewed;       868 AA.
AC   U5N8G3;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=Cenrod_0440 {ECO:0000313|EMBL:AGX86558.1};
OS   Candidatus Symbiobacter mobilis CR.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae.
OX   NCBI_TaxID=946483 {ECO:0000313|EMBL:AGX86558.1, ECO:0000313|Proteomes:UP000017184};
RN   [1] {ECO:0000313|EMBL:AGX86558.1, ECO:0000313|Proteomes:UP000017184}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CR {ECO:0000313|EMBL:AGX86558.1};
RX   PubMed=24267588; DOI=10.1186/gb-2013-14-11-r127;
RA   Liu Z., Muller J., Li T., Alvey R.M., Vogl K., Frigaard N.U.,
RA   Rockwell N.C., Boyd E.S., Tomsho L.P., Schuster S.C., Henke P., Rohde M.,
RA   Overmann J., Bryant D.A.;
RT   "Genomic analysis reveals key aspects of prokaryotic symbiosis in the
RT   phototrophic consortium "Chlorochromatium aggregatum".";
RL   Genome Biol. 14:R127-R127(2013).
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};
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DR   EMBL; CP004885; AGX86558.1; -; Genomic_DNA.
DR   AlphaFoldDB; U5N8G3; -.
DR   STRING; 946483.Cenrod_0440; -.
DR   KEGG; cbx:Cenrod_0440; -.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_330300_0_0_4; -.
DR   Proteomes; UP000017184; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43065:SF50; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF13185; GAF_2; 2.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF08448; PAS_4; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 2.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 2.
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.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AGX86558.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017184};
KW   Transferase {ECO:0000313|EMBL:AGX86558.1}.
FT   DOMAIN          299..369
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          614..861
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   868 AA;  95994 MW;  220B88B39B9BC253 CRC64;
     MVECGQTIIR SRSRGVLFGD VCRHLVDAGG MRAAWVGIWN PLEHRIWPTA RYGKGLGYLQ
     ALSLGGKVGV HLGGSLAEQA IARNELVWSD DVTTDPGMES LRELASPLQW RSALVVPLQL
     GGAAWGVLNV YAEQGKAFDA GVRSLFEQLS ANISHALDIF ENDAQRREAE FALQESEVRY
     NALFASSCMP LIVLDPKSGR IVDANIRALD FYGWNHAGFT SMCVAQIYVC DPETAMRELH
     EAAECTFVSL EHRHRLHSGE VRDVEIFSSP IHIDGGKFLI WAVHDVSERK RLHAKMRSAQ
     ALTQRFIDHL PGAAFVKDKD LRLIVVNRHL GTMLGAEPHT LVGKTAYDLF PPEFAHNATH
     FDQEVLADGK SRTMDEFFEG RHAETTLFVM EDDTGERFLG GLSIDVTDPG RIRERTRGLL
     QLNEFASKMD EPAFLLQGLE SAQSLTSSQI GFLHFVSADQ QHYEMAVWTA STRNFCSADY
     PTHGSLHTAG VWADCLRQAC PVIYNDYSTV PHKHGLPEGH PALNRFITVP IMEDGLARIL
     IGVGNKRNAY DQIDTDTLLL VGNGMWRIIG RMRAERALQQ RLQEMSALYR DLAEAQSQLL
     QSEKLASIGQ LAAGVAHEIN NPIGFIKSNL GSLADYVAKL LDIAKAYAHT EDELEAQGIH
     SPAFEELRRR KAEADFDFLL TDLPELIEES REGVERVGKI VMDLKNFARV GDSDFGWADI
     HAGLESTINV VWNELKYKAD VVREYGELPL VFCVASQINQ VFMNLLINAA QAMTTRGTIT
     VRTGAVGDEV WIEVQDTGCG IDLAKQARIF DPFFTTKPVG QGTGLGLSIA MNIAKQHQGS
     LTVQSQPGEG TVFRMTLPVC PVTGNPPQ
//
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