ID A0A415DRT8_9BACT Unreviewed; 1348 AA.
AC A0A415DRT8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DW103_10075 {ECO:0000313|EMBL:RHJ82335.1};
OS Parabacteroides sp. AM08-6.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=2292053 {ECO:0000313|EMBL:RHJ82335.1, ECO:0000313|Proteomes:UP000285678};
RN [1] {ECO:0000313|EMBL:RHJ82335.1, ECO:0000313|Proteomes:UP000285678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM08-6 {ECO:0000313|EMBL:RHJ82335.1,
RC ECO:0000313|Proteomes:UP000285678};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-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:RHJ82335.1}.
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DR EMBL; QRMP01000013; RHJ82335.1; -; Genomic_DNA.
DR OrthoDB; 717811at2; -.
DR Proteomes; UP000285678; 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; 2.
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; 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; 2.
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; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF101898; NHL repeat; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:RHJ82335.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000285678};
KW Transferase {ECO:0000313|EMBL:RHJ82335.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 781..806
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 839..1063
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1099..1214
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1248..1347
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT REGION 1067..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1147
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1348 AA; 155153 MW; 479F92B088F6DED3 CRC64;
MADKLISRKI IRLYARLLFC ILLVLIVREA NASFSLNKAD IPDLSNNAIL CMHQDPDGYM
WFGTYDGLNM YNGKDTYVFR FEPGNKSSLS SNIIHRITDA EPGYLWVSTF LGLDKFSIKE
KKVTESYLQY ADGRLMAADK DGNTLVIGQK DFISCYSPQT KLMQDIHTPG INTKHVKTLF
TDRNNKFRLF TDDGKLKTIE PDFSTMPATL NIQEKALHTP DILYACTEDY ILYFVDKDKQ
LYEYNTIDDK KKFLSDLSDL IEQYGPISQI TFYHSEIYIG FSGSYLLPIS HPEKAINLNI
GIFCLLKDKN QDILWIGTDG QGIEKYYEKH NIFESLLTKD LPIMLRKPIR AIYTDSLKNL
WIGTKGDGIA RIKEYDQYGE DPIPASQITH FSEEDGLSDD KVYCFLRSKF NPIIWIGTDG
PELSYYSYKE DKIKTLTNET STKIAMVHSI CEINDTTLWV ATAGDGLKEV NLSKKEEQLA
VKYIETYVFE RNRRVCKEFH SMCLADDSTL YLGSRGGYGL IRFNIYNKKC DYISMDNLES
SPIGDILCVH PSQNSTYYFG ASSGLTRMTF TPNGVDTKQF SRKDGLANDM IHGILEDEEG
CVWLSTNKGL AKYNPHNNFF HNYDYADLKV VEFSDDAYWK CPETNRMFFG GINGLVWIDP
QTSNKDFYRP DLRFFELNMG DETFDLLDYT ENKSDYVKIP PSVSSFTISF VATDYINGEN
YEYSYLLQNY NTTWTDLQKE NKVTFTKLPY GDYILKVNYK NDVFESDTKN YLLHIRVLPP
WYLSSWAILV YVALALLAAL CAFYSFRRKF IRKQQQVAKK IQEEQKEKLY EAKLNFFANI
THELCTPLTL INGVSNNIRE YAKTETDEKL IKNVDVLSEN VNGLNELIQE ILDFRKIEES
GINKCHIRKV SISELMKRQA NSFAPIAEHN QIRFECSVPG NLDWNTDPAF FKKIVVNLIS
NAFKYTEEKG LIQVSVFTDS DRTLTIKVYN TGQGIEASKL KGIFDRYRIL DNMEENAYTQ
TTSRNGLGLF ICHSMVQSLQ GEIEVKSEFG KYAEFIVTLP YLETEETEVP QTTSATTKQE
VTPATKTDDT DKISSFRPYI LVIDDNKDIV WLIASSLSAD YSVKEAYSAM EALKMMEQQT
PALIITDIMM PDMNGLELVK TVKANKFTKQ IPIVIVSAKI TDSEQAEGLN LGADAYLTKP
FSPLVLHSIV NRLMSSKQEM KNYYHSPESA YEYTDGQLIH QEDKEFMDMV NAIIKENIDN
ENLRPEFVAE KMGMNSRSFY RKFKKISSLA PSDFIKDYRF IYAAQLLITT NLNVQEIIYK
VGITNKSYFY REFARKYNMT PKEYRSQQ
//
