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Entry: A0A0J0YB67_9SPHI
LinkDB: A0A0J0YB67_9SPHI
Original site: A0A0J0YB67_9SPHI 
ID   A0A0J0YB67_9SPHI        Unreviewed;      1352 AA.
AC   A0A0J0YB67;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AB669_01725 {ECO:0000313|EMBL:KLT67439.1};
OS   Pedobacter sp. BMA.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1663685 {ECO:0000313|EMBL:KLT67439.1, ECO:0000313|Proteomes:UP000036014};
RN   [1] {ECO:0000313|EMBL:KLT67439.1, ECO:0000313|Proteomes:UP000036014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BMA {ECO:0000313|EMBL:KLT67439.1,
RC   ECO:0000313|Proteomes:UP000036014};
RA   Anderson B.M., Pipes S.E., Miller J.R., Newman J.D.;
RT   "Pedobacter sp. BMA.";
RL   Submitted (JUN-2015) 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:KLT67439.1}.
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DR   EMBL; LECU01000001; KLT67439.1; -; Genomic_DNA.
DR   STRING; 1663685.AB669_01725; -.
DR   PATRIC; fig|1663685.3.peg.367; -.
DR   OrthoDB; 9809670at2; -.
DR   Proteomes; UP000036014; 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; 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; 9.
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:UP000036014};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1352
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005246278"
FT   TRANSMEM        793..815
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          836..1055
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1103..1218
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1250..1348
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   MOD_RES         1151
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1352 AA;  153744 MW;  9B0CBBC7363D1343 CRC64;
     MNCRLLTCLL SSFLMFCLNS AAQQTISFDH LGVEKGLSQS SVISIAQDQQ GFMWLGTRLG
     LNRYDGYRFK VYQHDEKDPE SISNNYITAL YTDSRKTLWI GTISGLNIYH PENDHFEQVL
     NDSKKANTLK GISINCITED RKGNIWIGTQ QGVFLFKDGN PLHLTRYFNP SQPKPAINAK
     AIKEDHLGNI WVGTASGLFC LVPHDQKFSM VSYLANGKAG SISDNNITSI LEDHTNRLWV
     GTQRNGLNLW NSSTATFSIF NHSAADSHSL VNNTIRSLEL DDQGRLWVGT LDGISILNQQ
     GSFTNLQYEP DNKSSLNQNS IYKLYKDKNG SMWVGTYFGG VNINYPYHTS FKIYQRSNGK
     SSINNNVISG FAEDNQKNLW IGTEGGGLNF YNHISQQYVA FLSTGASGAL RSNLIKKIFY
     DRNGTLWVGT HSGGLSCYDP KSASFRHFDL GSETETNLLD EIVSIDEDQH GRLWVATQRN
     GIKISNTAKT SFLNYALPAA FPKAAKVKYM IINDRVYFGT TYGLFILNPL RNEFYSINDP
     QTKERINFFV NCLLETKKGE IYIGTNHMGM IKYDQLHNRI IRYTKKSGLP NDDVFGLMED
     EKGNIWIGTA NGLSMLDQQS QSFKNYTISD GLPGNEFNSN AFFRKSDGEM LFGGYNGFVG
     FYPDKIQTNT QASEMTFTDL ILDNQPVKIN GEDLLLEKNI VQTKKLVLGN DQNTFTLDFA
     LLNFIKPEKN QYLYKLEGFE KKWNRGNIPS VTYTNLPTGN YRFLVKGINN DGIYSSNMLN
     MDIRIKPPFY STWWAYLFYV LVAALIVALL LRYIFLKAIL FKEKEISAHK LEFFTNISHE
     IRTPLTLILG PLDKLIEETR DQWQWNKELQ PIKNNADRLM RLVTELLDFR KAESGKMQLE
     VSPGNIVQFT KEIYLAFRDL AAEKKIDYKF ECAESDIKLY FDQKQLEKVL YNLLSNAIKF
     GHENGKVLVS LKPENGTVAI NVSNEGKGIP LDQQSNLFDT FYQVNPGLNI GTGIGLSFSK
     TIVELHHGEI SFESTPETIE KTGFTRFTVL LKTGKDFFKA EDLVEDDREY EALSGYSFSP
     VPVSEESFDQ ESEPDTDFKE RFTILLVEDN QDIRFFIKSY LSQDYDVVVC ENGRQGWEYA
     IEQIPDIIIS DVMMPEMDGL TLCSKLKTDE RTSHIPIVLL TARSAYVHQI SGLETGADVY
     MTKPFNIRLL KVHLQNLLAT REKIKSKFSN VMVLEPTHVV IRKADEDFLN KLIATIEDNI
     VEQFDVPFLA KKMGMSQPVL YKKLRALTGI SVNDFIKSIR LKRAAQLLDL KSGSITDIAY
     SVGFNDRKYF SVEFKKFFGV SPREYQSGMR QQ
//
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