ID A0A415ZUS7_9BACT Unreviewed; 672 AA.
AC A0A415ZUS7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DW083_17040 {ECO:0000313|EMBL:RHO67800.1};
OS Parabacteroides sp. AF48-14.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=2292052 {ECO:0000313|EMBL:RHO67800.1, ECO:0000313|Proteomes:UP000283361};
RN [1] {ECO:0000313|EMBL:RHO67800.1, ECO:0000313|Proteomes:UP000283361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF48-14 {ECO:0000313|EMBL:RHO67800.1,
RC ECO:0000313|Proteomes:UP000283361};
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:RHO67800.1}.
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DR EMBL; QUDI01000040; RHO67800.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A415ZUS7; -.
DR Proteomes; UP000283361; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR018704; TPR_21.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF09976; TPR_21; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:RHO67800.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:RHO67800.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 461..672
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 672 AA; 77232 MW; 157AC09CE65506E1 CRC64;
MKERHIYVKG VLIVFCLFLS DLYGSCRTDG RTDDAGERLK ALYELSRQNW ETPMEVPYLK
SLVELAGEVD SMGYYYSALS SLGRYYCNIN RLDSLTYWGN MVDSVTKARR ETPLAKFDFL
NYYCRYYLIN GEYELAMNEA VMLQMLSKEK NNMTGLISSN EYLGLVYLLI GRDSDAVTAF
EEALDLLKTK SKPDYELQII PYLLIAYLHL DELDHVKSTL ARFEESLQKI ESYKSDIREN
YPIKAKKCLL YANYLNLYVA EKNLPKARET VSLLPSYMDE SMGPDVTSVY DLAMARYYFF
IKDYPQALRE IDKVLAVDYS SEPLKLKVDI LKAAGRTDEA LKQYAELLSL VEQTNVTAFT
RQLNQLRMLH DLNDKKMQEQ KLLYQKRQLS EKQLQLTASI LVSCMLLVLL YVLFRYSNRT
RKLKNDLQVE RETLIETTES LRVAKEQAEE SNRLKTSFVA NISHEIRTPL NAIVGFADLL
QDADEAERNE YLKIIKNNTD MLLGLVNDVL DLSRLESDSF SVILEDCDLS ECCQNAQERI
RHRVQPGVKL GFTASDDHFI LKTDDLRLQQ LLNNLLSNAV KFTVQGEINL DYRVDRENRQ
VVFTVTDTGC GIPLDKQEVI FDRFAKVNEF IPGAGLGLPI ARTIAIRLGG TLTVDPDYDK
GARFIFVHPF GE
//
