ID C5BMP3_TERTT Unreviewed; 650 AA.
AC C5BMP3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=TERTU_2800 {ECO:0000313|EMBL:ACR13882.1};
OS Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Teredinibacter.
OX NCBI_TaxID=377629 {ECO:0000313|EMBL:ACR13882.1, ECO:0000313|Proteomes:UP000009080};
RN [1] {ECO:0000313|EMBL:ACR13882.1, 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., Elshahawi S.,
RA Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT endosymbiont of marine wood-boring bivalves (shipworms).";
RL PLoS ONE 4:E6085-E6085(2009).
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; CP001614; ACR13882.1; -; Genomic_DNA.
DR AlphaFoldDB; C5BMP3; -.
DR STRING; 377629.TERTU_2800; -.
DR KEGG; ttu:TERTU_2800; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_019737_0_0_6; -.
DR Proteomes; UP000009080; Chromosome.
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 InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
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 PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF07695; 7TMR-DISM_7TM; 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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ACR13882.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000009080};
KW Transferase {ECO:0000313|EMBL:ACR13882.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 74..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 220..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 262..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 302..514
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 650 AA; 72668 MW; 685E02AE34B4FB39 CRC64;
MQTGEHAQEF FSDFSQGFGN ARLNVLGRGF ELSLEPNTTY NIAIELTADG IVAPPYIRLT
TAAAYTSWSN YMGYIYSLAV GVIIGLILIA LCCAAVLRDT TFLWFSLSSI FLLSFLCYRS
VVGVKLFGYS PETSWWLWLW VSALQISTLM FARAFLTEEA QYSRFQRLFD GTLIFFGLSL
ALSFVLPLKL NMVLFVFNGV LMMMLILSAG LDKLVRRGRY YLLFMLGWLP VLYALVELGF
VAARVPDAHS STLSYKVVRE PFFQIAHMLI HFIAMLIRIN ELKRQSFLAT MRNDAKSRFL
ASASHDLRQP LHSMGMFLAH LSEHIQNKSS RVLLSKVFQL HEQMNQSFGT LMELSRLEAG
AEEAHIERVN LNSLLASLRV EYEPQAQSKG LSLRFHCSVN HLASDQVLLE RILRNLLSNA
IKYTDRGGVL LGVRRRDQYL LIQVWDTGQG ITSESRNVIF DIYQRSQHAN SDHAGMGIGL
AIVRHSAELL HGAITLRSRA GRGSVFELRL PAIEAPSLPA GSRETSTADR LRIVVELSET
TLRSQVNACL HSWGYLASDQ TASDQNAAMT LVIGESPGEA DYEALVAHAQ SLEARFGNVV
QAQFGGTVER ALAAKLTSLN VHTLSSEFRP AELRSLLRYL EAQWLQGSQS
//
