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Database: UniProt
Entry: A0A2T7QD65_9BACT
LinkDB: A0A2T7QD65_9BACT
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ID   A0A2T7QD65_9BACT        Unreviewed;       722 AA.
AC   A0A2T7QD65;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=PAS domain S-box protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DC498_05175 {ECO:0000313|EMBL:PVD53269.1};
OS   Terrimonas sp.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Terrimonas.
OX   NCBI_TaxID=1914338 {ECO:0000313|EMBL:PVD53269.1, ECO:0000313|Proteomes:UP000244333};
RN   [1] {ECO:0000313|EMBL:PVD53269.1, ECO:0000313|Proteomes:UP000244333}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NS-102 {ECO:0000313|EMBL:PVD53269.1,
RC   ECO:0000313|Proteomes:UP000244333};
RA   Zhang L., Jiang J.;
RT   "The draft genome of strain NS-102.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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:PVD53269.1}.
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DR   EMBL; QCZJ01000003; PVD53269.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7QD65; -.
DR   OrthoDB; 5401121at2; -.
DR   Proteomes; UP000244333; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.20.5.1930; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR007891; CHASE3.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR   PANTHER; PTHR24421:SF10; SENSORY TRANSDUCTION HISTIDINE KINASE; 1.
DR   Pfam; PF05227; CHASE3; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244333};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        182..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          224..287
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          290..342
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          620..709
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   722 AA;  82133 MW;  C02D0648786F72B9 CRC64;
     MKISTGKILL ITLLLTAITV ATALYISVNQ SKKVNTTFQS VSNTQNILFF AEKLLAEVTQ
     SEMLAREYFL TGHEEHLLSF NKMKGLIQDN FDKLKRSTAD NKVQQKRLDT LSEYMSASLR
     ASDNLTSSER SVQPEEIIAL VSKATNSYNM VAIKNLINNI ANEEQRLLSV RKNESTIANS
     SLRALLFLTF ALLFILMMIL VQKLRVEVIS DRETYRIMQY NTLLMDNIHD AVISTDKDLC
     IVSWNDKAEK IFGWKEEEVR GKPILSVVKP GYKDEGRAAI EKRVKSTGTW DGEINLEKKD
     GQKITASLSW SAIWAPNGKV RGSITIARDV TPRKQLEEQL KRFNAKLGKQ VEERKAEIKH
     VVERLVSSEK KYKQLFENNP LPMMMLSYPE LNIIDVNEAA ILQYGFTKEM FLKKNIKDIQ
     VKEELLDFKD YIKEDVAGYQ EAGVWKHHKI DETIIFVEIF VHSMIIDGLK AKLVLAHDIT
     QKVETEKKQT EYLEQIRMLT GYLQEVRETE RKNIAREIHD ELGQQLTVLK MEIAWMIKKL
     EVNEKNVEVK LTELLDTIDG TMTAVRRICA ELRPTVLDDI GLEAAMEWHI KQFQQATGIA
     VKLLSTTQDF HISADIKTAL FRIFQESLTN IARHANASAV QVDLSKKDGF ITLMIADNGR
     GFDMAIADQK RTLGILGMKE RSLALGGEYK INSKPGKGTA IRVSIPLMPS EEKLDILNKK
     TG
//
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