ID A0A1J5MWB4_9GAMM Unreviewed; 985 AA.
AC A0A1J5MWB4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BM565_09900 {ECO:0000313|EMBL:OIQ46792.1};
OS Gammaproteobacteria bacterium MedPE.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1860093 {ECO:0000313|EMBL:OIQ46792.1, ECO:0000313|Proteomes:UP000182920};
RN [1] {ECO:0000313|EMBL:OIQ46792.1, ECO:0000313|Proteomes:UP000182920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MedPE {ECO:0000313|EMBL:OIQ46792.1};
RX PubMed=27446036; DOI=10.3389/fmicb.2016.00996;
RA Lopez-Perez M., Kimes N.E., Haro-Moreno J.M., Rodriguez-Valera F.;
RT "Not All Particles Are Equal: The Selective Enrichment of Particle-
RT Associated Bacteria from the Mediterranean Sea.";
RL Front. Microbiol. 7:996-996(2016).
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:OIQ46792.1}.
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DR EMBL; MPDF01000069; OIQ46792.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5MWB4; -.
DR STRING; 1860093.BM565_09900; -.
DR Proteomes; UP000182920; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17574; REC_OmpR; 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; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR InterPro; IPR000014; PAS.
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; 1.
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; PF12833; HTH_18; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00342; HTH_ARAC; 1.
DR SMART; SM00091; PAS; 1.
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; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 31..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 280..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 471..682
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 720..835
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 884..982
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 768
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 985 AA; 111788 MW; 9B1AD35D17F2C92E CRC64;
MHHMVKPVLF LGIFCIVMMP VLFQFNDVSL YSFLALNLVT LIFVGGRFIK ANGRSERVFW
QFLLLAMTIS FIQDVIVGFS ITEHVLLINS IQLITYLLLI IAIESSPHLT HLAIKKLATP
IVSLLIFSVL LFCYFVLIPL ELDTSDSVIQ TSTLLFHFVI FCVLGGRLLS ILLSGVGDYF
KIVYSMLICA IVTILLQYYV AFKEAALSDF FQSFLIQVPY LMVIGTTLVN PSRYVAKKTK
ADSYTDVSAN FVILMTIIIL SFSHLYGVMN SKDFIVDLRF QTIVVGIWLV LGCCFLVFNI
YSLVQRNRRL KHSLIQEQIL LNDAKNFSDY LNHQIVNSED TAIVNASSNA ILTVDMTGIC
LSANPAAVQM FQYLSTKLVG CHIKKLFDDN DEMHYFFDFK SNVYSLERNR SGISRESVAC
RADKVQFPVQ VALQWAERRD EPLIVITFIN LTDRKRREEK SLELKDKFIA NISHEFRTPL
TIINGILDRY LVDEKSNNEL VIAKRNGLRL VTMVEQLLEL SRLRDNPTMT FHHYRLASLM
AMPIESFSRL AEQNTLTFSS TVPPGLWVEC DAQGFEKILF NLLSNAIKYT PSGGDVTVVT
YVENDSIVLD VIDNGIGIST EYQHKIFERF QRAENQQTNN TFGVGIGLSL VNELVAAHGW
HISLTSELDK GSKFSLSMPI AQPQIEDSPL IDSTLSQDIS PLFDSPKNVN VLQKSHSQKV
VLIIEDNLDM QNHIKQVIEN HHHCLLAGSG EIGLELAKEY LPDLIVCDLM LTGIDGFTVL
NTLKTDEMTS HIPVILLTAR SDQESKLKGL NLSADDYLGK PFQHEELLTR IQNLIDNRML
LQQSFQRKID SKQQESRLES VQESLEKLVV DTDVEQSPEA IFVQKLEKVV AKFYAEPLLD
VNFIAKEMAM SERQLQRKIK VILGTTTNNF IKELRLKKAK ALLQNGLQIG RVALDVGFSS
QTYFGRCFKE QYDCTPKQFQ QRLKD
//
