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
//