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Database: UniProt
Entry: A0A255T189_9BACT
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ID   A0A255T189_9BACT        Unreviewed;       933 AA.
AC   A0A255T189;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=CIL02_13025 {ECO:0000313|EMBL:OYP58880.1};
OS   Prevotella sp. P3-122.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=2024223 {ECO:0000313|EMBL:OYP58880.1, ECO:0000313|Proteomes:UP000215645};
RN   [1] {ECO:0000313|EMBL:OYP58880.1, ECO:0000313|Proteomes:UP000215645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P3-122 {ECO:0000313|EMBL:OYP58880.1,
RC   ECO:0000313|Proteomes:UP000215645};
RA   Accetto T., Nograsek B., Avgustin G.;
RT   "Comparative genomics of non-oral Prevotella species.";
RL   Submitted (AUG-2017) 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:OYP58880.1}.
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DR   EMBL; NPJH01000080; OYP58880.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A255T189; -.
DR   OrthoDB; 1116352at2; -.
DR   Proteomes; UP000215645; 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; 1.25.40.10; Tetratricopeptide repeat domain; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
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; PF00072; Response_reg; 1.
DR   Pfam; PF13424; TPR_12; 2.
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   SMART; SM00028; TPR; 5.
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; SSF48452; TPR-like; 2.
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.
DR   PROSITE; PS50005; TPR; 1.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000215645};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        361..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REPEAT          167..200
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          407..618
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          670..785
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          829..930
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   COILED          774..801
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         718
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   933 AA;  104805 MW;  40D6ABA7E567FAB8 CRC64;
     MTRMAATKIL QAGLICLTMT NMSCGEEKNS NAAKTHEFTD SLVSLRNRGK DLRDEGRYDE
     ALMLHNDGLT LAKSTGDTCE WVQALNNIGT DYRRMGMLDI AQEYHYEAWR MCEESADTCR
     TMRKNRVVSL NGLGNIYLTI KDYVRADSAF RQALAGEREL GSATGQAINY ANIGAIYNAQ
     GNYKEARRYY EMSLKMNEKD SNTLGLSLCH TYLGNLHEQA KEYDMARQEY MTAYELIKDS
     KDKWHTLEPM MALVQLGLDT GNMAEAEAWL KEVDKEMKGL NSREHESEIY TLHYRMDNSK
     GLYREALRWY EKAKAMEDSI MDQDKNNRIH NIGISIERRR QEMILARTKS ELKAEKSRST
     FWLWGGVILL TVSVLTVGLM TYVQRIKAAS MKALQEASGM REDFFTNITH EFRTPLTVIL
     GLSGEMKEKS DNEEWRSKCE AIYRHGNSLL RLVTQLLDIA KIKSRVGEPD WRHGNIVAQV
     KMIAETFNDY AASRGIELAV EAQGDIDIDF VPDYINNVVS NLLSNSLKFT PTGGQITIKT
     ASDGKLLTLA VTDTGKGMSE EEKNNIFKPF YSSATGNKGT GVGLALVKQI ADSLEGKITV
     ESTEGEGSTF TLTIPVRKAV KGVRKLNPAN YDMAQAKTEA MAGLDNGNST EADMQEDLQE
     GMQGNQQRKV VLVIEDNRDV AKYIGSQLSA DYDVAYAVNG NDGLKKAISM IPDMIVSDLM
     MPEMDGLEMC SKIRSNEEVN HIPVIMLTAK ITEADKLKGL EAGVDAYLPK PFNADELRLR
     VAKLLEQRQV LRHKYSQAKA AGKDIKDITV VADDRQAMAT MEMADAFLNK ATDYIYAMLE
     RYEVVSVSTL AEKLNMNARQ LHRKLTAVAD ITPNTFIMNL RIRKAMKMIE DNKSIPLKNV
     AFDCGFSEYS HFTKSFKSIV GVSPSEYGKE KKI
//
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