ID A0A432VI39_9SPHN Unreviewed; 1298 AA.
AC A0A432VI39;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EJC47_11805 {ECO:0000313|EMBL:RUN76412.1};
OS Sphingomonas sp. TF3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=2495580 {ECO:0000313|EMBL:RUN76412.1, ECO:0000313|Proteomes:UP000275325};
RN [1] {ECO:0000313|EMBL:RUN76412.1, ECO:0000313|Proteomes:UP000275325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF3 {ECO:0000313|EMBL:RUN76412.1,
RC ECO:0000313|Proteomes:UP000275325};
RA Afonin A., Vasilieva E., Akhtemova G., Zhukov V.;
RT "The Draft Genome Sequence of a Sphingomonas sp strain TF3.";
RL Submitted (DEC-2018) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:RUN76412.1}.
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DR EMBL; RWKS01000011; RUN76412.1; -; Genomic_DNA.
DR Proteomes; UP000275325; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 4.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-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; 4.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR007895; MASE1.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF05231; MASE1; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 3.
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; 4.
DR SMART; SM00091; PAS; 4.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 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; 4.
DR PROSITE; PS50112; PAS; 4.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000275325};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 35..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 300..370
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 374..426
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 427..481
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 494..551
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 552..622
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 623..676
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 677..747
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 753..806
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 824..1040
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1063..1185
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1117
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1298 AA; 140462 MW; 617CCEC280251053 CRC64;
MVPVRRPHSA ALALFGGLIL LLAWGGVAIS RGNGYVAPLW LANAALAATI LQAGWRSAWY
WIATAFIALC LAASLNGDPP LFSPVLAAVN CAEAIGGSWL LMRWQKHTPD MADFRDLLRF
ALCCCGVAPA VSGVAATLWL APHDLWHGLS IWRYWFLADS LGMLIGGPIA LIAIDSWSNR
RKVTPPRAFE IAAILTANAL VAAIVFLQPA YPMFFVALPL IILASFRLGV RGAAAAIAVV
GIIGTVGTLS GLGPAYMIGG TLATRVHLLQ LFLAACFGIS LPFAAAIAGR ERIREELKRS
RDFSETLVSS MQEIVFRTDA ERRWIFLNPA WETITGYSVA ESLGRSTTEY LLPEDRAQGD
ARFNKIISGE VTEATLRQRF FNAAGECRHI ETMLRRLAEP DGSFAGTIGT IRDITETVAT
QHALTESEAR FRRLAETAPV GIFRAGATGG LTYVNRAWAD KVGLSMEDAL GNGWMRALVD
PTPFLEQPAW EDFKPGDVRV RDNAFRGSDG RELWFQTVNS PEFDENGVLT GFIGAIIDIT
EQRQSRIALA ASKRLFETLA DLSPAGIFRT DTEGRVTYVN RAWMEFAGLS YEQSMGYGWS
KAIHPDDLAR VSKTWNEAVG GAQKVRMDFR FLRDGVERWV EVLAVNEYDS EGKRIGFLGV
DIDITERKAA EAALAASEEQ LRLLAENATD AVFRLSLDGV CLYASPSFQH MLGIDPQRLI
GQNILVRFHA EDSDAVMATH RALAAGEMER SVTTFRWESI EHKGKWFWLE ANSGLVRDPE
THQPLEIISS IRDITVRKQL EFDLDSARRH AEVAAQAKSS FLANMSHEIR TPMNGVLGFT
DLLLAEDPRP DQQQKLQMIA ESGTAMMRLL NDILDLSKIE AGHVTLAHDR VDLRHLARSC
AKLILPIAMR SGLELQTEIA DDVPNMVIGD GLRLRQIILN LLGNAAKFTE HGAITLSVAM
VDGDVAISVG DTGIGIAPDR QAAIFGEFVQ EDSSTERRYG GTGLGLSISS KLAKLMQGSL
SLFSAVGIGT TITLRVPLPV APPNAPAIKP TPAATLPPVP GARVLVAEDH EVNQLLIKAM
LTRLGYDPVI ARGGIEAIAM VQDAATHGNP FGLVLMDMQM PDIDGLVATQ RIRQGGIAPT
TLPIIALTAN AYASDIEACR AAGMQDHLAK PVRLSALDHA VRRWAIPPTG VPTEAPLPAS
ADPELIAQFE ARVQRTFTAL DIALGENGGP TTDPKRAIDD VQEALHLLAG TAAFFGKADL
GTIAADLDEQ LGAGHHIGTA AFLQAARAQL RAAAAESV
//
