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Database: UniProt
Entry: A0A258P0G0_9BURK
LinkDB: A0A258P0G0_9BURK
Original site: A0A258P0G0_9BURK 
ID   A0A258P0G0_9BURK        Unreviewed;       517 AA.
AC   A0A258P0G0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=B7Y60_11205 {ECO:0000313|EMBL:OYY36052.1};
OS   Polaromonas sp. 35-63-35.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=1970418 {ECO:0000313|EMBL:OYY36052.1, ECO:0000313|Proteomes:UP000216365};
RN   [1] {ECO:0000313|EMBL:OYY36052.1, ECO:0000313|Proteomes:UP000216365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35-63-35 {ECO:0000313|EMBL:OYY36052.1};
RA   Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA   Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT   "Lifting the veil on microbial sulfur biogeochemistry in mining
RT   wastewaters.";
RL   Submitted (MAR-2017) 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:OYY36052.1}.
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DR   EMBL; NCFQ01000008; OYY36052.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A258P0G0; -.
DR   Proteomes; UP000216365; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 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; 2.
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; PTHR42878:SF7; BACTERIOPHYTOCHROME; 1.
DR   PANTHER; PTHR42878; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 2.
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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          291..507
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   517 AA;  56207 MW;  1251934FB7BD1621 CRC64;
     MKSLRGSRRA LLPGARTGQA RANAEALQAG LDLSSDGIVL LDNAGRVVAF NSCAQALMHS
     ALGNLRGVDF WDAVQEEIAD EYRGATEQAL LETGSHSFVV WHAFENQWVD YCLRQHDNGL
     LVTLRDVSAV HQASRSLRNS ESCNQTLFAA HPQAMWLLDT GSRHLLAVNN AAAALYGLAP
     EALRGAFVES LFPEGEGASL LDSLPPSDFQ QEMRLCTQKR ADGELMLVEL ACSSVQWDLR
     PAVLVSVTDV GARHLADAHL SRLNEELEIR IEQCTGELQR GRGEFDAFTS AMLHDLKAPL
     HVIDGFATTL AERHGTALDA QGQHYLARIQ ASSLQLARLI DDLRTLTYLP RMVMAPDRVD
     LAPVCLRIVA ELRKREPARH LVLEMEPSLP LVCDKDQLSI ALACLLDNAW KFTSRKEQSW
     IRVGLMPGEN SADIVLSVSD NGAGFDTAYT DKLFTAFERL HSSVDFPGTG LGLAIVKRVA
     QLHGGEVWAV AADKGGASFF MSLPQESGSV SGSPPAA
//
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