ID A0A086P687_SPHHM Unreviewed; 1118 AA.
AC A0A086P687;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BV98_003305 {ECO:0000313|EMBL:KFG88905.1};
OS Sphingobium herbicidovorans (strain ATCC 700291 / DSM 11019 / NBRC 16415 /
OS MH) (Sphingomonas herbicidovorans).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1219045 {ECO:0000313|EMBL:KFG88905.1, ECO:0000313|Proteomes:UP000024284};
RN [1] {ECO:0000313|EMBL:KFG88905.1, ECO:0000313|Proteomes:UP000024284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 16415 {ECO:0000313|EMBL:KFG88905.1,
RC ECO:0000313|Proteomes:UP000024284};
RA Gan H.M., Gan H.Y., Savka M.A.;
RT "Draft genome sequences of Sphingobium herbicidovorans.";
RL Submitted (AUG-2014) 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:KFG88905.1}.
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DR EMBL; JFZA02000045; KFG88905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A086P687; -.
DR STRING; 76947.GCA_002080435_03279; -.
DR PATRIC; fig|1219045.3.peg.3357; -.
DR eggNOG; COG4191; Bacteria.
DR OrthoDB; 9796100at2; -.
DR Proteomes; UP000024284; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; -; 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; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 3.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFG88905.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000024284};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 248..303
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 699..752
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 765..985
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1006..1116
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1056
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1118 AA; 122022 MW; EB71B8CA355C115B CRC64;
MASDGRESAD YPDFLIGGGE MGARIRAYDW ARTPLRSPQQ WPQSLRSALS ICLHSSVPTA
IYWGPELRLL YNDAWAPVPA ERHPEVLGQP AHAVWGDIWG VVGEHFAQVL RTGEGYSTYD
QMLPMVRQGA ARETYWNYSL TPIRGEDGSI AGIFNQGYET TARVMAERKS LAEREQLRRM
FDQAPGFMTM LKGEDHIFDL ANRAYLELVG RRDVIGKPIR DALPELEGQG YYELLDKVYE
SGEPFVGTAV PVDLKRGDGQ GIERRFVDMV YQPITDAKRR ITGIFIEGSD VTDRVRAEAD
LRASESRLRF LSELDDRLRA SRDASEVMRA AAEHLTLRLG ASRTAYADVD ADNDRFIVRD
DYAAPGIESS AGVYSLNLFG SRVAADLRAG RTVVIRDMKS ELAVGEGREM FLSIGIGAII
CCPLIKDGKL VAMMAVHQST ARDWQEDEIT LAESAVERCW AYVARVGAEA RLRDMNETLE
QRVTEALAER KIFADLFETT NSFVQIIDPD YRFLAINTAS VDEYQRMFGF RPAAGDNLLE
LILANCPWHH DPIKALWAPA LKGETFGEVS EFGAAERRWY DMKLAPVLSA DGAIIGASLF
GYDVTARIHE QQQLARAEAA RREADALYRA YFENTAEALF IINVLEDGGF SIEELNPAHE
LLTGLRTDEI KGKPLDEQLP ADVVAEATGN YRRAVAAGQP ISYREVLRLP AGARHWDTVL
VPVANAAGRI NKIIGSARDV TAHVQAEEQL RQSQKLEAMG SLTGGVSHDF NNLLSPIIGA
LDLLQRRGVG GERERRLIDG ALQSAERARV LVQRLLAFAR RQPLQTISVD VGELVNGMAD
LIRSTAGPQI KVVVDVEDAL PGAVADPNQL EMALLNLSVN ARDAMPDGGT LRISAVGDEV
ALGHATNLTP GSYVRLSVAD TGVGMDSETL KRAIEPFYST KGIGKGTGLG LSMVHGLAAQ
LGGALTIASE PGVGTNIELW LPVGGTPGQL QGQSAEATVP RDRRGTVLLI DDEEIVRAST
ADMLVELGFD VIEADSAEEG LNRMAAGLTP DLIVTDHLMP GRSGGDLAME VRGRWPDLPV
LLVSGYAEAE GVAPDQVRLV KPFRQADLAA HIAELTGA
//
