ID A0A3B7MRF9_9BACT Unreviewed; 711 AA.
AC A0A3B7MRF9;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-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=D3H65_18780 {ECO:0000313|EMBL:AXY75899.1};
OS Paraflavitalea soli.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Paraflavitalea.
OX NCBI_TaxID=2315862 {ECO:0000313|EMBL:AXY75899.1, ECO:0000313|Proteomes:UP000263900};
RN [1] {ECO:0000313|EMBL:AXY75899.1, ECO:0000313|Proteomes:UP000263900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5GH32-13 {ECO:0000313|EMBL:AXY75899.1,
RC ECO:0000313|Proteomes:UP000263900};
RA Weon H.-Y., Heo J., Kwon S.-W.;
RT "Genome sequencing of strain 6GH32-13.";
RL Submitted (SEP-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};
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DR EMBL; CP032157; AXY75899.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B7MRF9; -.
DR KEGG; pseg:D3H65_18780; -.
DR OrthoDB; 9811889at2; -.
DR Proteomes; UP000263900; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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; 3.30.450.20; PAS domain; 1.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 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:UP000263900};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 348..569
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 592..706
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 641
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 711 AA; 81171 MW; AB22831844A0DD94 CRC64;
MKQKLLYLGW SIYRDIVFSG LQEGITKDQR KKIIGFNQFI LLALLVNFFS VVSYFYHKLY
ISALINITSA YFFLLAFYFG SRRKLETGRI IAVVNLNLYL IVISYIEGLK AGEYLFYFPY
FLVLTFVVSI RRNSRELFIV YTITVIASLI CLKLSPYTNT VQVINDALYT RLYSSNLVIS
LCMTIIFSYS ILRVNKDNEV AIMQEKKFGD TIFNTSLDGV FIIFSQSGII ASCNHRALEL
FDVQEKREIE GSHVENWFDE DHVRRFNSIE RTVSDGTQSW QGELAFTTQK GRTFHGYVSL
APFSYKDIRY TKISILDVSH VKMTEFELMK AKEKAEVAAK AKSRFLSNMS HELRTPLNGI
IGASNLLVQE EHLPSQKAHL DILKFSSEHM MMLINDILDY NKIEAGKLEL AEAPVNIKEF
IQQVSTQFAS QVKARGLEFK TDIDDRLNAE FITDETRLNQ VLSNLLSNAI KFTHAGKITL
AVRKLFASST KATIQFIVMD TGIGIPRNKH REIFETFTQA DVNTTRKYGG TGLGLAITKK
IVNKFNSDLL LESEEGKGSA FHFTVELKIN ESRPRYIHEE NISQLTQLPG VRVLIAEDNP
VNLAIARRFL AKWGIEVSEA ANGREAVDKF RKQEFDLLLI DLEMPEMDGA TALREIRKLN
NNIPVVAFTA AVYDNMQEDL LQKGFTDFIH KPFRPVELHA KINYLVAALR A
//
