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Database: UniProt
Entry: A0A1I2PT03_9BACT
LinkDB: A0A1I2PT03_9BACT
Original site: A0A1I2PT03_9BACT 
ID   A0A1I2PT03_9BACT        Unreviewed;       944 AA.
AC   A0A1I2PT03;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05216383_10691 {ECO:0000313|EMBL:SFG17137.1};
OS   Prevotella sp. KH2C16.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1855325 {ECO:0000313|EMBL:SFG17137.1, ECO:0000313|Proteomes:UP000198560};
RN   [1] {ECO:0000313|Proteomes:UP000198560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH2C16 {ECO:0000313|Proteomes:UP000198560};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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};
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DR   EMBL; FOOW01000006; SFG17137.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2PT03; -.
DR   STRING; 1855325.SAMN05216383_10691; -.
DR   OrthoDB; 1116352at2; -.
DR   Proteomes; UP000198560; 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   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; 2.
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   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; PF17874; TPR_MalT; 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; 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.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Kinase {ECO:0000313|EMBL:SFG17137.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000198560};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:SFG17137.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..944
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011778836"
FT   TRANSMEM        393..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          439..655
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          695..810
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          843..943
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   REGION          658..689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         743
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   944 AA;  106872 MW;  64AFACCCC245D3DB CRC64;
     MEIRMRHPKL LCSLLCVFLA LYAAGCADKK DAPGPSESER LEADSIVMAC NDTVRLQEML
     RGYQREGNIL YQEATLRQLG KLYREASNFS RSIRYHNQEL QLAEKARDTV EAILALNGIG
     TSFRRMGILD EASAYHIKAL NLSMEYSDQA SQIMHKYRVV SLNGLGNVYL TAGNLESADS
     VFRLSLEGER LLGSSLGQAI NYANIGAIKE TRGQTDSAWY YYRKSLEYNT LAGSKLGVSL
     NHNAFGQLYE KDWELEKAIR EYRQAYAIME NDPDKWHWLE SCIALGRVYL SKGDLATAGR
     YLDRADSVAE QIHSNEHLHA VHELYGKLYD SQGNYKRAFE EQRLAHLYKD SVVNVANLNR
     IQNLRISFER SKKQQEIKLA TASIKARSKV KDIVLAAFIV ILVLLVAVIL QLWYLLRVRR
     QKTRVVHQMS EVRERFFTNI THEFRTPLTV ILGEGEQLAV GQTTDLGAIH KAGEMIVRQG
     RSLLTLVNQL LDISKVKSEV GEADWHTGNA VPYLHMIIEE NLQLARAKNI SMLFLPNEND
     VKMDIVPDYL EKIMRNLISN AVKFTSPRGS IIVSCKKQGP DFQIEVADDG IGMSEEVKGR
     VFEPFFEADT ESTHIGTGVG LSLVYQLVKA MKGTIRVESE PGKGSTFTVL LPRRHGTGSW
     KPLEEQPSVR PPLTVGTEEP DYPEDREKGG DRPIQILVVE DNADVAHYIG ELIPGEYSVA
     YAANGEEGLR KAADLLPDLI LTDLMMPGVD GLELCRRIRA NESTNTIPII IITAKTTQGD
     LEEGLKAGAN AYIFKPFSAN ELLLRIDAIF NERRMLQEKF LLASHELSEV KPDISREDID
     FISRFTNIIY DQMRTCVIDL EELAQKLFMS QRTLRRKIVD LTGETLNDYV MKIRIDYARQ
     QLKRRPEFSI NEVAMCCGFT DQAYFSRIFK QVVGITPNQY RKNV
//
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