ID A0A3P2AC80_9BACE Unreviewed; 1345 AA.
AC A0A3P2AC80;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EII33_06860 {ECO:0000313|EMBL:RRD91790.1};
OS Bacteroides heparinolyticus.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=28113 {ECO:0000313|EMBL:RRD91790.1, ECO:0000313|Proteomes:UP000279562};
RN [1] {ECO:0000313|EMBL:RRD91790.1, ECO:0000313|Proteomes:UP000279562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH1047_COT-310 {ECO:0000313|EMBL:RRD91790.1,
RC ECO:0000313|Proteomes:UP000279562};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-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:RRD91790.1}.
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DR EMBL; RQYF01000023; RRD91790.1; -; Genomic_DNA.
DR Proteomes; UP000279562; 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; 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; 6.
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; 4.
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; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000279562};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 782..804
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 836..1048
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 1246..1345
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1147
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1345 AA; 154050 MW; 326E23E0499DA705 CRC64;
MKIFQFLSVL LGGLFPCMMY AAIMEDIRFS HIGLEDGLSH STVFAINQDK EGNLWFATYD
GVNKYDGYSF TVYRHQYTDS NSIASDISRC ITVDDSNRIW VGTREGLSLY NRHRDAFSNY
YYKKDGINVA VNSIIAIKKD WLMLGTAEGI LLFDVKKERF FNDTLSSALH GLKPTALVRQ
DDNVYIGAES GVYVYALSSA TLEKLVNIPA GVKVHAVLCQ MFNKLWLATE GDGLYLYDTK
SGELKNYRYA SGKSGLNSDY VRSLALDTEN RLWVGTYGGL NIYKEGTDSF LSIRSSEIQE
GSLSQNSVRS IFRDSQGGMW LGTYWGGLNY YHPLCNRFQR IKHVPFLNSL SNNVVSCIVE
DSKHNLWIGT SDGGLDCYDN VSRQYRNYLF NSDNLDIPFK DIKTVYVDEA QDKVYVGAHA
GGMMALHRKS GYVEYYNRQN SNLPSNNIYS IISDGHRGLW VASLEYLLHF DIEKRRFTIV
EKDEKGHKLQ QYNRLLFRDS KKRIWAGGEM GISVFNQTGA SLLANTEFRM DSMLRQAFVN
CFYESSSGYM WIGTRNGLFA LKEGESKTIQ YTTASGLPSN VIYGILEDAY GRLWISTNQG
LSCLNPESGK FRNFTILDGL QSNQFNAGSY CRKINGDMLF GGVNGITSFR PETLIDNPYA
PKPVINKLFI YNKEVLPNDE TGILKESVAY VNHITLSSSQ NSFAISFVVS NYIAGKHNTF
AYKLEGYNDV WYKQNDISPV SYSNLPAGDY TFYVKAANND GKWNDDPTIL HIRILPVWYR
TWWALSLFTL SAVLLIFGIV RFFWLRKSMQ AEIRMERLDK EKQEEINQMK IRFYVNISHE
LRTPLTLIIA PLQELLNRIS GHWEHEQLLY IQRNTSRLLH LVNQLMDFRR AELGIFELRV
VYSNAYKRVL NSFLNYESLA KRKDIDYNFY TELQDENVLF DENYLDLIVN NLLSNAFKYT
EVGESITVKL YIENDDLVLQ VADTGIGIPA EKQKKVFERF YQLENGREGS GIGLSLVHRL
VELHHGRIAL QSEVGKGSVF SIYLPQNKSV YAQEELLDGS EDIRKQRVYS TNAHDVYIGD
EEKPDEENVT DVEGGKRGTI LIVEDNKELR KYLVNSMADL FNLLEAENGQ KAVELLKEQE
VDLIITDVMM PVMDGVKLCK WVKQNLRTCH IPVYMLSAKA DVKYQLEGLH VGADDYIAKP
FSLEILRAKI LNALRTRYRI FERYSNTTEV EPEKLTNNTM DEELLRKAIA IVEKNMDNVE
FSTEQFAREM NMSRSNLHLK LKAITGKSAI DFIHKIRFNR ACQLLKEGKY SVSEISFMVG
YNTPSYFAAR FKKYIGCLPT EYGKK
//
