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Database: UniProt
Entry: A0A0D5YVA9_9FLAO
LinkDB: A0A0D5YVA9_9FLAO
Original site: A0A0D5YVA9_9FLAO 
ID   A0A0D5YVA9_9FLAO        Unreviewed;       696 AA.
AC   A0A0D5YVA9;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=VC82_2603 {ECO:0000313|EMBL:AKA36165.1};
OS   Allomuricauda lutaonensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Allomuricauda.
OX   NCBI_TaxID=516051 {ECO:0000313|EMBL:AKA36165.1, ECO:0000313|Proteomes:UP000032726};
RN   [1] {ECO:0000313|EMBL:AKA36165.1, ECO:0000313|Proteomes:UP000032726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-HSB-11 {ECO:0000313|EMBL:AKA36165.1,
RC   ECO:0000313|Proteomes:UP000032726};
RA   Kim K.M.;
RT   "Complete genome sequence of Muricauda lutaonensis CC-HSB-11T, isolated
RT   from a coastal hot spring.";
RL   Submitted (MAR-2015) 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};
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DR   EMBL; CP011071; AKA36165.1; -; Genomic_DNA.
DR   RefSeq; WP_045802738.1; NZ_CP011071.1.
DR   AlphaFoldDB; A0A0D5YVA9; -.
DR   STRING; 516051.VC82_2603; -.
DR   KEGG; mlt:VC82_2603; -.
DR   PATRIC; fig|516051.4.peg.2670; -.
DR   HOGENOM; CLU_000445_114_67_10; -.
DR   OrthoDB; 9810447at2; -.
DR   Proteomes; UP000032726; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
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   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
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   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
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; PF13424; TPR_12; 1.
DR   Pfam; PF13176; TPR_7; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00028; TPR; 6.
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   SUPFAM; SSF48452; TPR-like; 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50005; TPR; 2.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AKA36165.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032726};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transferase {ECO:0000313|EMBL:AKA36165.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        414..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REPEAT          102..135
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          182..215
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          473..689
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   696 AA;  79326 MW;  2AB1966C20CC5D0C CRC64;
     MTSNLFIKRL SFNIGGLTLL LFLIAGSPFN KVHAQKSVRD SLLHEVESLN ISKQSSKKDT
     TYINLVNSLA SRYRYYKSDS LLLLSKKALK LSEEKNYVKG KIIALLSMGA YYSDQGNCKK
     AIAHIKNALE VAKSNKNNEL TIKAQNNLAG EYAYMGDNAK ALNLYLLTIE LAEKEEDLAM
     LSILNENIAN LYAAQNDYDS ALEFYEKVKD LNEQVGKPIP SAETMSNVAS VYADIEKFDY
     AMFNINQSIS IFEKHEILDW LAYAYEVKGK IYLKQKKYKW ALYWYDHSQL LHQNLDDERA
     KIDLYNGIAQ AHLGMDNDDV AKEYAVQAFD IATNIKSLEG QKDCAKTLYE IHKKLGDYDE
     ALGYHEIYQQ LSNDLSRRDN KKSLAMLKVK LDYEKQKQSL IDENKRSLAR QRNYTILAII
     IFLILLSITF LVYRNQEIQK KLNIELYNKT ASLEERESEL KAINATKDKL FSIIGHDLRG
     PIGALQSLLD LFANGDLTKD EFLTQMPKLK SDVDSISFTL NNLLSWGQTQ MNGAVTKPKR
     ISLNSIVEEN INLLSKLAVK KSIRLINELP ENVYAWADKN QIDIVVRNLI SNALKFTPEN
     GLINIKAVER KNNWEITVRD TGVGMDPETQ DKIFCDNTNF TTYGTNNEKG TGLGLSLCKE
     MVQKNKGEIW VESYLRKGSC FYFTVPKADK KYRKAS
//
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