ID A0A1E5TBP9_9FLAO Unreviewed; 1371 AA.
AC A0A1E5TBP9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A8C32_00580 {ECO:0000313|EMBL:OEK08804.1};
OS Flavivirga aquatica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavivirga.
OX NCBI_TaxID=1849968 {ECO:0000313|EMBL:OEK08804.1, ECO:0000313|Proteomes:UP000095713};
RN [1] {ECO:0000313|EMBL:OEK08804.1, ECO:0000313|Proteomes:UP000095713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-16 {ECO:0000313|EMBL:OEK08804.1,
RC ECO:0000313|Proteomes:UP000095713};
RA Wong S.-K., Yoshizawa S., Nakajima Y., Ogura Y., Tetsuya H., Hamasaki K.;
RT "Draft Genome Sequence of Algibacter sp. Strain SK-16 Isolated from the
RT Surface Water of Aburatsubo Inlet.";
RL Submitted (MAY-2016) 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};
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:OEK08804.1}.
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DR EMBL; MDJD01000028; OEK08804.1; -; Genomic_DNA.
DR RefSeq; WP_069829486.1; NZ_MDJD01000028.1.
DR STRING; 1849968.A8C32_00580; -.
DR OrthoDB; 358279at2; -.
DR Proteomes; UP000095713; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17574; REC_OmpR; 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; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
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; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12833; HTH_18; 1.
DR Pfam; PF07494; Reg_prop; 6.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF07495; Y_Y_Y; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00342; HTH_ARAC; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000095713};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1371
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009186327"
FT TRANSMEM 795..812
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 849..1067
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1116..1231
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1263..1362
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1164
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1371 AA; 157890 MW; 8D1F342A1793BFA7 CRC64;
MTFKKVVISL LIIFNTVLAY TQNINNTYNN LKFKNYSTKD GLSQRSVLSI LQDNHGFMWF
GTRYGLNKFD GNTFKNYNYN SEDLNSISNN WITELVKDKY NTVWIGTKKG LNKYVPENNN
FVRVKKSNLT KQFYNGEIWD IKVQDSTFLW IATNQGLDKF NIKTNNVLTF KHNKNNPNSI
SSNEIRRVLI TSNKNLWIST NESIDIYNPT KNSFKHISYP NNATPTLTKN NTTALFEDSN
GKIWLGYNNG LAFFNPKTIA FEDFKLNSKT IITSSVRTIC EDKEGHLWIG SYNGLCKLDQ
KNKFFYKYEH DITNPKSLTQ NSIYKVIEDS RGDLWIGTWA GGISYYDKSS NDFTTFSVGY
STKNLNYRIV SSIVEDEKEN LWIGTEGGGI NFYDKKNGTY TYYKHNPKNT NSLSANNVKA
IIEDYKGNFW VGTHGGGLNQ IIINKNSKTF KIYKNKPNDS TSISDNKITT LTEDHNFNIW
IGTNEGGLNY YNRNTNSFSR IKDPENFLGN FIYKILKSQT KNLLFIGSEN GLTQIDIKTK
KTSTINFRDN TKNAFTLNPV ISIYQESQNS LWIGTEGDGL YNYNTTTKES TRYSLQNGLS
NEVIYAILPD DNNNIWLSTN KGLSRLNLDT KQFKNFEETD GLQGNEFNYG AYLKTKNNDL
IFGGTNGFTV FNPNEIKKDA FIPPIAITSF HVRNKPFKIV TDSLKSIKLK HNENDFSFNF
VALSYSQPNK NQYAYKLDGF DLDWNFIGNN NTAIYTNLNP GSYTFKIKAS NSDGIWNEDG
RSIHLTILPP YWKTWWAFLI YVILSLTLFW FIRRYTLLRI QDRNELKQER LDKEHMEEVN
RLKLQLFTNI SHDFRTPLTL IIGPLKKMIN DKAGNTYVQN QLTDMYRNAS ILLQLINQLL
DFRKSEAGKL HLHTSKYDIV TFIKNIKLSF NELAQDRNIQ YTLESSETVI DTWFDKIEMK
KVILNILSNA FKFTPKNGEI IIKISTNTST KNVKIEIKDS GKGISKDDLE FVFDRYFQLG
QQNEVRSGTG VGLALAKDIV ELHHGKIYAE SQLGKGSSFT LLLPLGNSHL SPEEIILEDY
TESDLLNYDE VADIKSGWIR EEINTKQIRF DDSLPSILLV EDNIEVRKFI KSIFDKHFNV
FEAENGETGI QSAQYNPIDV IISDVMMPKM NGIEMCTKIK SDIRTSHIPV LLLTARTSSK
VQKIGYETGA DVYLTKPFDG ETLKLQVNNI LKSRKSLIDK YKKDILLEPK EITVVSTDEV
FLKKAMKIVE ENLSNTEFNV NSFIEKMYMS QSVLYRKIKV LTGQSISEFI RSIRLKKASQ
LLSQTNMTIS DIAYDIGFND LKYFRKCFKN TFNQTPSLYR KQNQKQRTKS D
//
