ID C6W2D6_DYAFD Unreviewed; 1871 AA.
AC C6W2D6;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Dfer_0854 {ECO:0000313|EMBL:ACT92109.1};
OS Dyadobacter fermentans (strain ATCC 700827 / DSM 18053 / CIP 107007 / KCTC
OS 52180 / NS114).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=471854 {ECO:0000313|EMBL:ACT92109.1, ECO:0000313|Proteomes:UP000002011};
RN [1] {ECO:0000313|EMBL:ACT92109.1, ECO:0000313|Proteomes:UP000002011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700827 / DSM 18053 / CIP 107007 / KCTC 52180 / NS114
RC {ECO:0000313|Proteomes:UP000002011};
RX PubMed=21304649; DOI=10.4056/sigs.19262;
RA Lang E., Lapidus A., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H.,
RA Cheng J.F., Land M., Hauser L., Chang Y.J., Jeffries C.D., Kopitz M.,
RA Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA Mavrommatis K., Chen A., Palaniappan K., Chain P., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Goker M., Rohde M., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Dyadobacter fermentans type strain (NS114).";
RL Stand. Genomic Sci. 1:133-140(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; CP001619; ACT92109.1; -; Genomic_DNA.
DR RefSeq; WP_015810366.1; NC_013037.1.
DR STRING; 471854.Dfer_0854; -.
DR KEGG; dfe:Dfer_0854; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3899; Bacteria.
DR HOGENOM; CLU_000445_34_2_10; -.
DR OrthoDB; 9806704at2; -.
DR Proteomes; UP000002011; Chromosome.
DR GO; GO:0005524; F:ATP binding; 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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43642; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR PANTHER; PTHR43642:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:ACT92109.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002011};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..259
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1494..1715
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1735..1853
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 1453..1484
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1786
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1871 AA; 207737 MW; DB2B4FEB1FB81EB6 CRC64;
MGLETIQIPD YQLTQQIYKE GDTLLCRAVK ESTGREVILK VSPQAAGSDA DTGMVLPWND
VFGRVLNHVR FIRTESHQIT ELENFTGIHL PQYLDNHAID LPAAAAIASG LVRTVEELHY
LGITHPDLRP AHFLINPGTL EVRLADLACA YRGTSGESAH GRGAIGLHYI SPEQSGLTDV
PVDYRSEYYH LGVMLYRLFT GKLPFNSTDP NELVHAHIAR APLWPADAPE LPGIITLKLL
AKKPGDRYQT TRGLLEDLAY CANVAGSGAE GFVSGRYDQP GVLRLPGQLY GRENELAALL
AAYGRIGERN ELALISGQSG IGKSSLVAAL ENQLERAGAL FVSGKFDQYV QNIPFEGVIK
SLKQLVGKIS GMDAGHWKTA ILDAVGTLGQ IVIDVIPEMQ QIIGRQPAVE RLPPLEAQNR
FVNVFTRFIN VFTKKEHPLV IFLDDLHWAD LSSLRFLSRI THSVEGSNLL IIGTYRDNEV
SASHPLRAAI HDLDGRQSAL TQITIAPLQR EDIAALVADT FSCPGQAALP VAEIILAGTL
GNPYFVRETI ADFCQQGLIH YDPGRRRWEW DIAALNGNAR SGSSQQLLAA KINHLTAHAR
HAVMTASCIG TEFDLTVLSA LLDKTPQETG EDLQEALAEN LLRITASRQP QEHYLIQSKY
IFVHDQVQQA AYDLLSEAQQ VEIHLHIGYF LLERLSSAER DAQLFEIVNH FNYCRAFTGE
AERCSVARLN LEAGQKAKAS SAYSVAFAYF TKGREMLVPE DWHRDHPLAF SLHVQCAEAA
YLAGHPEASL GIAGLALARV EKWEDKVEIR DVQIRGLILS RQHERAVALS LDVLRELKIT
FPREPGNRHI IAAYLKSKWL LRGRNIASLA ELPAMTDART LAAMRVLQNI TAIVFARQPA
LYPLMVIKMM ELSLRYGVAA ESAITFTTYG AIVNAIEGNP GACYGFGNLA LSLAEHTGGV
ARERTLLVYN IVNRPWGEHI NNSLEPLRRS YEKGIEMGDL EYCTYASSSY AFHLLLSGKN
LRWCKHEMLR FNEPPRALSR EPMTHFNEPL IQTVANLLGE NDDPVRLTGA YFDEKPDFSA
ILGQNDRSRM FASFVYKMIL AYLSGDMLRA TEHAVHAVPF IDAARASLFE PLHSFFLGLA
NVALYRGTSR RTGQMRVADV HRRKLRRLAR LVPVNFEHRY LLLDAEILAV RGKSMEAIAR
YDQSILAALE NGHPHEAALA NELCGRYWTD KGQAKTGLIY LQSALEGYRE WGCVLKERQL
TAAFPVLSQA PPAQPGTPVH AGESIASTLD LSTLMKASAT ISSEVVFSQL MEKLMQFAIE
NAGAQAGYFV LDWGGELVIE ATRSVVNESS DLRKIPLAES AEVPVSMIGH VFREKTDIIL
HDARMSAFKN DPVVKARQVL SALCIPALNQ GKVVGALYLE NNLATAVFTL ERTQLIKLLS
GQIAVAIENA ILYEKLEQKV AVRTAEIQVQ KEEIERQKQL VEQKSRFKEQ FFANMSHEIR
TPMTAILGMS ELIFDTPLNE KQLEYARGIR YSSENLLAII NDVLDYSKIE AGKFSFINKP
FQVGDRMERL GYILRVIAEE KGLELRITVD SDVSPQVIGD PIRLHQILLN LAGNAVKFTE
NGSVSIHVAV LSRDAGQEQL QFSVADTGIG IAEDKLEYIF ETFTRIDDDS NSRQSGTGLG
LFIARKLVEE QGGRMQVTSR VGHGTEFRFD LTFEICSTLE DHDDPRADVL LTGLSVLLVE
DNLFNQVVAE ETLKKMIRDV RVTVADNGAI ALQKLDETHF DIILMDVKMP VMDGYTATRA
IRARENGARV PILAFTSNAN PTEAEKCRDA GMDDYITKPI EAKKLKYKIR KLVQSRETAA
STPTIIRPEM Q
//
