ID A0A2U2PIM2_9SPHI Unreviewed; 1350 AA.
AC A0A2U2PIM2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, 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=DDR33_07720 {ECO:0000313|EMBL:PWG81256.1};
OS Pararcticibacter amylolyticus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pararcticibacter.
OX NCBI_TaxID=2173175 {ECO:0000313|EMBL:PWG81256.1, ECO:0000313|Proteomes:UP000245647};
RN [1] {ECO:0000313|EMBL:PWG81256.1, ECO:0000313|Proteomes:UP000245647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJ4-8 {ECO:0000313|EMBL:PWG81256.1,
RC ECO:0000313|Proteomes:UP000245647};
RA Cai Y.;
RT "Pedobacter chongqingensis sp. nov., isolated from a rottenly hemp rope.";
RL Submitted (APR-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:PWG81256.1}.
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DR EMBL; QEAS01000005; PWG81256.1; -; Genomic_DNA.
DR Proteomes; UP000245647; 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; 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; IPR011047; Quinoprotein_ADH-like_supfam.
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; 3.
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; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 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}; Reference proteome {ECO:0000313|Proteomes:UP000245647};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 792..813
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 845..1062
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1090..1205
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1244..1343
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1138
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1350 AA; 153121 MW; 00D3F26A989B8706 CRC64;
MLVHNGCMKI YMRILFLFIA LFQVLFLAGQ PPTVKYLSLQ EGLSNQQVLD LAQDESGFVW
IATELGLNRF ASNSFKQYYK SEKADGVSVN SNEINTLFYN NGQLYIGTRA NGLNVLNLQT
NRFSYYLHDP NNNKSIATND ITDIIKGEDG YLWLATYHQG IQRFDPVKKE FEHFNKKRIP
SLPENSIWSL AFDQQGLMYV GHVGKGLSVF HTRSGKVEVL NKERTNGMLP DDEVKALFCD
SKNNIWIGTR KGLAVYNPLK RSIQSISLVR QVRQPFVYSI KEIDGAIWVG AESSQLFIVK
PEYGINKDVR NVRSVIPFNL DKGTNSSVQH IAADSFGNIW LAVYGVGVGV VSHLKPFFKV
FPGEGMSAGS FGKLTAVSGI LLNNDNSMWL ATVGNGVVQM KEGEGLKYPS RANGGADDFL
LSAFCDRKNN KWFGLQSGGV AVFNSEEKRW QQKGKLENMT EVRAMIEDSH GQMWFAAQEG
LFTLVPEQQK WQKLIINNPM LGDYAPRALV EDSRGYIWAG TYGQGLYVFN RDLKLVRKIS
KDDGLKSNTI NHLFRDHRNN IWIATNEGIA VQYVSSELGR IENIVPPGSD AWLIVNAIAQ
DRSGNLWCST KSGLLRYLPE ERRFLSYDRA FGLPLGGFVN NSVAVDHKGR MFFGMPGGVC
YFDPGEIPLK IAMSSIMVSR FTVFNNGESH TQSEKYPSLA QEILLNHDEN SFRIELAVMD
YALNDLVEFS YKLQGLDEDW IFMGSEKNLD FRNIPYGKYE LRIRTRQKNE NWPDNYKRLF
IVISPPFYLS PYAFVFYGLL VATIVFVVVF FYIKKIKAEA ELRLKKHQLV HDEKLYTERL
NFFTNITHEL RTPLTLILGP LHDLLNEDKL SSRHRDLVQT VQKSANRLFA LVSQLLEFRK
VESQYKQLVL GEGFIGEMLQ EIVAKYAESN SKKAFSISCI VPRPDVKTSF DAEIVQLVMD
NLLSNACKYT SAGSIEVRLE YEQDRLSTWA VIYVKDSGCG IAPEYLDKIF DKFYQVPRSA
MQGTGVGLAL VRELVAIHHG KILVKSEPEK GSEFCVRLLT NAVATGGNEK DESLSFTDGT
HHVDGDHSPL LLLVEDDTDL REYLTSLLRH RYEIISAENG SSGFDMATNR IPDLILSDIV
MPDMDGFGML KKLKQERETS HIPIIFLTAK DGDTDRQHGY ELGVDSYLTK PVSAQLLYQR
IENLLLKRKE TYAEVLAQLS VQNEPETARS GREEELWREN AFVREFVSLV EECILDEVLD
AATLAEKMNM SQSTLYRKLK GLTGKNINQL VRKVRIQKAA ELLRSGQYNV TEVSFMVGIN
SSIYFRQCFK EEFGLLPSEY QKEALNSKQR
//
