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Database: UniProt
Entry: A0A1I7GYM1_9BURK
LinkDB: A0A1I7GYM1_9BURK
Original site: A0A1I7GYM1_9BURK 
ID   A0A1I7GYM1_9BURK        Unreviewed;       644 AA.
AC   A0A1I7GYM1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05216350_102420 {ECO:0000313|EMBL:SFU53480.1};
OS   Polaromonas sp. YR568.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=1855301 {ECO:0000313|EMBL:SFU53480.1, ECO:0000313|Proteomes:UP000217451};
RN   [1] {ECO:0000313|EMBL:SFU53480.1, ECO:0000313|Proteomes:UP000217451}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR568 {ECO:0000313|EMBL:SFU53480.1,
RC   ECO:0000313|Proteomes:UP000217451};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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};
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DR   EMBL; FPBM01000002; SFU53480.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I7GYM1; -.
DR   STRING; 1855301.SAMN05216350_102420; -.
DR   Proteomes; UP000217451; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   CDD; cd17580; REC_2_DhkD-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; 2.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
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   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13426; PAS_9; 2.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
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); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:SFU53480.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:SFU53480.1}.
FT   DOMAIN          25..80
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          100..152
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          153..226
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          228..280
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          290..508
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          525..641
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         574
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   644 AA;  71085 MW;  1692BAC2EDED9D57 CRC64;
     MAPAGHAGYY VLMPLTPNPP AEQPVTDRFR LLVDAVQDYG IFMLDTVGNV VSWNTGAQRL
     KQYRPEEIIG RNFSTFYPPE AVAAGWPAEE LRRAEKDGRF EEEGWRIRKD GSRFWANVVI
     TALRGPDGKL EGFGKVTRDL TERRAHEEAL RESEQRFRLM IEGVQDYAIF MLSPDGVIES
     WNSGAQRIKG YSPAEVIGKH FSLFYLPEDL AAGKPQAELK LALAQGRAEE EGWRVRRDGS
     VFWANVAIAP VYDAGRVLRG FVKVTRDMTE RRRLYELEKS SKRMSEFLAM LAHELRNPLA
     PIRNAVTILQ LEPSPSPLVR SSRDMIDRQL SHMTRLVDDL LDVGRLTTGK IRFKTEQVSY
     NQVVARSIEA VRPLMDARRH RLTVDVPTAP MLVQGDATRL AQVLQNLLIN AAKFTPEAGQ
     IELKVWQDGT QLYTTVSDNG AGLSPEALSH IFELFAQGDA QTAARESGLG IGLTLARSLV
     EMHGGTLSAE SEGPGRGSRF SFFLPNAQLA AGSANDQPGK EAGATIMVVD DNKDAANSLA
     EVLRLMDCQV KVAYDGPAAL ELFRKQPSQA ILLDLGMPGM NGYEVLSALR ALHGGERVTV
     AALTGFGTDE DKQRALEAGF DEHLTKPLDF AVLQTFLQTA GLVV
//
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