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Database: UniProt
Entry: C5BS23_TERTT
LinkDB: C5BS23_TERTT
Original site: C5BS23_TERTT 
ID   C5BS23_TERTT            Unreviewed;       493 AA.
AC   C5BS23;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   SubName: Full=CHASE3 domain, sensory box histidine kinase {ECO:0000313|EMBL:ACR12957.1};
DE            EC=2.7.3.- {ECO:0000313|EMBL:ACR12957.1};
GN   OrderedLocusNames=TERTU_3626 {ECO:0000313|EMBL:ACR12957.1};
OS   Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Teredinibacter.
OX   NCBI_TaxID=377629 {ECO:0000313|EMBL:ACR12957.1, ECO:0000313|Proteomes:UP000009080};
RN   [1] {ECO:0000313|EMBL:ACR12957.1, ECO:0000313|Proteomes:UP000009080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39867 / T7901 {ECO:0000313|Proteomes:UP000009080};
RX   PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA   Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA   Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA   Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G.,
RA   Elshahawi S., Hanora A., Schmidt E.W., Haygood M.G., Posfai J.,
RA   Benner J., Madinger C., Nove J., Anton B., Chaudhary K., Foster J.,
RA   Holman A., Kumar S., Lessard P.A., Luyten Y.A., Slatko B., Wood N.,
RA   Wu B., Teplitski M., Mougous J.D., Ward N., Eisen J.A., Badger J.H.,
RA   Distel D.L.;
RT   "The complete genome of Teredinibacter turnerae T7901: an
RT   intracellular endosymbiont of marine wood-boring bivalves
RT   (shipworms).";
RL   PLoS ONE 4:E6085-E6085(2009).
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DR   EMBL; CP001614; ACR12957.1; -; Genomic_DNA.
DR   RefSeq; WP_015819070.1; NC_012997.1.
DR   STRING; 377629.TERTU_3626; -.
DR   EnsemblBacteria; ACR12957; ACR12957; TERTU_3626.
DR   GeneID; 29649853; -.
DR   KEGG; ttu:TERTU_3626; -.
DR   eggNOG; ENOG4105BZU; Bacteria.
DR   eggNOG; COG0642; LUCA.
DR   eggNOG; COG5278; LUCA.
DR   HOGENOM; HOG000048503; -.
DR   OMA; HVDQGIQ; -.
DR   OrthoDB; 1755994at2; -.
DR   BioCyc; TTUR377629:G1GVH-3268-MONOMER; -.
DR   Proteomes; UP000009080; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase_c; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR007891; CHASE3.
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   Pfam; PF05227; CHASE3; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|SAAS:SAAS00925949};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000009080};
KW   Kinase {ECO:0000256|SAAS:SAAS01003914, ECO:0000313|EMBL:ACR12957.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00925310};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009080};
KW   Transferase {ECO:0000256|SAAS:SAAS01003669,
KW   ECO:0000313|EMBL:ACR12957.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     12     32       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    190    208       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      260    478       Histidine kinase. {ECO:0000259|PROSITE:
FT                                PS50109}.
FT   COILED       98    118       {ECO:0000256|SAM:Coils}.
FT   COILED      226    246       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   493 AA;  56174 MW;  988877AEB61CDF66 CRC64;
     MPFSKPSKTN RVWLIAGFFM LVFIATNTVI AYNSIKTLAQ THQSIANTLH VITVIKDLYA
     QLVSAESSQR GYIITSDKQY LEPYAKSTGE LGSILNSLDQ LTTEIPEQKN NFRELSELAK
     KKISNMRLGL TLKESKRDAE LQELFYSDRG HDLMAAISVQ IKHMEEIEYN LLDARSLAAK
     KGRTSAFRTL LFSNSFGLIL ILIIYLSVNK HIRQRLLYSE LIHKANEELE QKVKVRTESL
     EHYSEELQRS NRELQNFAFV ASHDLQEPLR KIRAFGARLN TTCADQLDDR GKDYINRMFA
     ASERMSVLID DLLTFSRVFT QQNPFEKIDL GELLSVVLDD ISMAIDDSDA DIKVAALPVV
     ECDSSQMRRL FQNLITNAIK FRKPDAQPSV QIDCDTFTED DEEWCRITII DDGIGFDQQF
     AEKIFTLFQR LHARDEYSGT GLGLAICRRI VERHGGVIKA FGELGKGSRF VIELPLTQSN
     RPIQDFLPEE ANP
//
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