ID A0A3N0C124_9SPHI Unreviewed; 1370 AA.
AC A0A3N0C124;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=D7004_03850 {ECO:0000313|EMBL:RNL55897.1};
OS Pedobacter jejuensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1268550 {ECO:0000313|EMBL:RNL55897.1, ECO:0000313|Proteomes:UP000274046};
RN [1] {ECO:0000313|EMBL:RNL55897.1, ECO:0000313|Proteomes:UP000274046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TNB23 {ECO:0000313|EMBL:RNL55897.1,
RC ECO:0000313|Proteomes:UP000274046};
RA Cho Y.-J., Cho A., Kim O.-S.;
RT "Genome sequencing of Pedobacter jejuensis TNB23.";
RL Submitted (OCT-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 -!- 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:RNL55897.1}.
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DR EMBL; RBEE01000004; RNL55897.1; -; Genomic_DNA.
DR OrthoDB; 9809670at2; -.
DR Proteomes; UP000274046; Unassembled WGS sequence.
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; cd00082; HisKA; 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; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
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; PF07494; Reg_prop; 6.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF07495; Y_Y_Y; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00342; HTH_ARAC; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 2.
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; SSF101898; NHL repeat; 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 Kinase {ECO:0000313|EMBL:RNL55897.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:RNL55897.1}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1370
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018137210"
FT DOMAIN 845..1068
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1117..1232
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1264..1363
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1165
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1370 AA; 156710 MW; 982E629D0A077DB7 CRC64;
MNRFIQSLIL LLFFVQNAHA QVLEFRHISI DNGLSQNTVN SIAQDKNGII WVGTLGGLNK
FNGYDFTVFT HNERDSKSIS HNRVNVVFID KDGNVWIGTD DGLNFYNPSD DSFNHIPDAA
NQRYFVYCVT QDRAGNIWLG TAQGLKRLNR KKNRVEDVDL NITNINKRVQ SIYEDDKGLL
WIGLAKGFKI YDVSKQKAVQ GPRNLQARLS SSWIQSIKQT KNNDFWFATE NDGVFSYHQK
ENTILSYNKS NGILSNTVRD IFIKDDQHIW MATKMGLNIL NLASGKITGH SYAPKLSLEN
SLSHPSVKCI FRDRSGNIWL GTYSGGINLI YNFSKIFSNK GIAQGDQEPF SNKEVNAILG
DGNKKFWIAT DGGGLNCWNK AVDNVEVYKY DNDNVLYHFI KDVAVDLLDS NKLWIGSSAG
ILVFDKNSKK FKEFKDIQKG LNVEFNHDYK FLNSKYGLWV ATNYNGLHLI KNNIVVKSYT
LANKKLVSNN ISCLLLQGNN LWAGYLLSGL SRIELTTGRI SSYAFDKKDL HSLSNNSVSC
LFNDSKNRLW IGTNGGGINF FDEKTKRFYP INSQNGLANN TIHAIEEDSQ GALWVSTNKG
IFKILLKNNK FPLADKDIEV TNYTVLDGLQ SNQFISGSSF KNKNGEIFFG GINGLSSFMP
EKIAYNREIP NIIFTDFKIL NREKVDLNDS VNQKMVDFQK EIVLQYDESY FTIKYAALNY
IFPERNSYAY KLDGLSMDNW HYVKNQREVT YTGLEPGEYT FLVKAANNSG IWNNLPRQLK
ITVLPPWWKT NWAYLMYTLL GLVLLYLFNH YTKYTERLKN TIRYETELYQ KEQELSQKKL
SFIINISHEI KTPITIIMGP LQKLLKMHEG NTKTSNYLDL MNRSGQRLLN LVDQLLDLRK
LDGHAVPLKA AKGNLVRFTK EIVIVFGGLA KSKNLELTFN AKKDKLELWF DRDKLEKILY
NIISNAVKYT PDYGKIEVLV REDEIGKNAA IEIIDNGVGI SQDRLPDLFQ PFKPMDVSNN
HIKGTGVGLA FAKELIELHH GRIEVESKEA SIENRGYTKF SVKIPLGATY LGADELDNEY
LVSEDISNYK SIAIKQQSSF RERKKAIKMA NHNERFTMLL VEDNPDVIDF LADSFEDDFD
IIKGFDGSTG LKEALERMPD IIISDVMMPV MDGIELCNKL KSNIITSHIP VVLLTARSPM
IFKLEGLENG ADEYVTKPFN FDLLEAKVWN LLENRQKMKL RYQKEITLQP TNTTISTFDD
KFLASVMKYI EDNIAEESLN VEDLSSYIGM SRGNLYRKLK VLTSKSPVEF IRYIRLKRAA
QLLKQHKMYI NEVSYMVGFQ NVTYFRKCFK EEFGYTPTGF AKTEEETEED
//
