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Database: UniProt
Entry: A0A2T3HKB8_9SPHI
LinkDB: A0A2T3HKB8_9SPHI
Original site: A0A2T3HKB8_9SPHI 
ID   A0A2T3HKB8_9SPHI        Unreviewed;      1332 AA.
AC   A0A2T3HKB8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=C7T94_09550 {ECO:0000313|EMBL:PST82870.1};
OS   Pedobacter yulinensis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=2126353 {ECO:0000313|EMBL:PST82870.1, ECO:0000313|Proteomes:UP000240912};
RN   [1] {ECO:0000313|EMBL:PST82870.1, ECO:0000313|Proteomes:UP000240912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YL28-9 {ECO:0000313|EMBL:PST82870.1,
RC   ECO:0000313|Proteomes:UP000240912};
RA   Keele B.F.;
RL   Submitted (MAR-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:PST82870.1}.
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DR   EMBL; PYLS01000005; PST82870.1; -; Genomic_DNA.
DR   OrthoDB; 9809670at2; -.
DR   Proteomes; UP000240912; 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; 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; 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; 8.
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; 3.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 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:UP000240912};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1332
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015748162"
FT   TRANSMEM        776..797
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          834..1056
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1079..1195
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1227..1326
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   MOD_RES         1128
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1332 AA;  150870 MW;  C6D9AE76F10DAFE2 CRC64;
     MSLRNILIFL FFLSFMPAQA QQPLFRSYAV TDGLVSNTVW CVGQDNKGYM WFGTKNGLSR
     FDGYQFKSYR FDKNNPQSLG NNFITAIAAA DERHLWIGTQ MGVYVLDLEK ERFSPLALLK
     NQSVYDIVRD KSGSMWVATR SNGVYRFGKK PLHFHENSKA GRLSSNHVRK LTFDHSGRIW
     IGTFGKGIDV YDPATRQVQN LNRRNSALSS DQVLSLYTDL SGDVWVGTFA GGLNVYRQST
     RNFSVFRAGT RGGINDDIVR SIYQPAPGKL YVGTEKGLNI LDLSTGQSRS YTKRTNDPYS
     ISDNAIYAIY PDREGGIWVG TYFGGISYFT EKGLGFELYY QRDGMPSLSG NAVSSFLEDT
     PGKFWIGTED GGLNLFDERT RSFKKYPWHS GQQALSYHNI HCLYKDARGR IWIGTFAGGL
     NIYDPASGSV RNYRHEASDP RSLSNDNIYV IYEDRDKQVW IGTTKGLNRY DPASDSFFRV
     GGMDMDKNVI YDIYEDNTKT VWFATYDAGL VAFNKRSQTW SAYRAGRKNA LSSDKIISLL
     DDHAGNLWIG TDGGGLNRLN MQDKTVQVFD ESQGLDANVI YGMLQDDSRN LWLSTNNGLY
     TYLPGKKVFR HYTNWDHLQS LQFNYGASYK SSSGKLYFGG IKGFNAFFPD SVRQLSGRQE
     VVITNFQLFN RPVSAGVAGS PLQKPIDYTQ KLTLSHSQSV ISFEYAALSY LAPNKVQYAY
     RMQGFDKGWN YVGSERKATY TNLPAGNYVF QVKAMGNDGN WNSHVTTLQI RVNPPFYLSV
     WAYIFYALAL AGAFWLFRHY TIKETRRKNQ IRLERLKSRK EKEFYTQKLE FFTAMAHEIR
     TPLSLIIAPL EKLLQSRNKN TDEQAQLAIM EENSNRLLNL VNQLLDFRRI ESDVYAIHQE
     EIELVSFIHT IYSRFSSIPY QKGIRFTMST KISSLQVQID PEAFTKIMNN LLINAFKFTR
     SKVKISIDEP ETRDGRAYFS VSVEDDGIGI PPSQINNIFS KFFKVSSGAH QYSNLGGTGI
     GLSLARSLVE KHEGVLEVRS QEQVNTVFKL LVPYEPAGAA VAGKAVAAVK EPEGEGLLTI
     LVAEDDESLN DFIGNGLAEA GYRVIKAFNG FEAQELLAQY QVDLIISDIM MPVTDGMEFL
     KAVKENIDHS HIPFILLTAR ANSESEIEGI TLGADAYLIK PFKWKHVLAV VKNLVESRNK
     LREKFARQPF APANSLTTNS RDKKFIDKVT GIIEERMMDP QLSVEELSKD LAMSRSSLHK
     KLKSLSGYVP NEFIRLIRLK KAAELILSED YNISEISYLV GFNSHSYFSK CFVSQFKVPP
     SEFLEKHREK IT
//
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