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Database: UniProt
Entry: A0A0N0V3V3_9RHOB
LinkDB: A0A0N0V3V3_9RHOB
Original site: A0A0N0V3V3_9RHOB 
ID   A0A0N0V3V3_9RHOB        Unreviewed;       818 AA.
AC   A0A0N0V3V3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=luxQ_3 {ECO:0000313|EMBL:KPA21994.1};
GN   ORFNames=shim_18800 {ECO:0000313|EMBL:KPA21994.1};
OS   Shimia sp. SK013.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae.
OX   NCBI_TaxID=1389006 {ECO:0000313|EMBL:KPA21994.1, ECO:0000313|Proteomes:UP000037951};
RN   [1] {ECO:0000313|EMBL:KPA21994.1, ECO:0000313|Proteomes:UP000037951}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK013 {ECO:0000313|EMBL:KPA21994.1,
RC   ECO:0000313|Proteomes:UP000037951};
RA   Voget S., Kanukollu S., Daniel R., Engelen B.;
RT   "Genome Sequence of Shimia sp. SK013.";
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};
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:KPA21994.1}.
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DR   EMBL; LAJH01000011; KPA21994.1; -; Genomic_DNA.
DR   RefSeq; WP_054002365.1; NZ_LAJH01000011.1.
DR   AlphaFoldDB; A0A0N0V3V3; -.
DR   STRING; 1389006.shim_18800; -.
DR   PATRIC; fig|1389006.3.peg.1929; -.
DR   OrthoDB; 9801651at2; -.
DR   Proteomes; UP000037951; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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; cd00130; PAS; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.450.350; CHASE domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR006189; CHASE_dom.
DR   InterPro; IPR042240; CHASE_sf.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF03924; CHASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM01079; CHASE; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50839; CHASE; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:KPA21994.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000037951};
KW   Transferase {ECO:0000313|EMBL:KPA21994.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        18..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        273..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          113..253
FT                   /note="CHASE"
FT                   /evidence="ECO:0000259|PROSITE:PS50839"
FT   DOMAIN          308..379
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          380..434
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          452..671
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          694..809
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          418..445
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         743
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   818 AA;  89452 MW;  2A0A63BDD8889825 CRC64;
     MISKTVFLST SLVGRSKAYL PVLFATLLLL AFAIYAERQE TFIAKQEQRN SVHSETSILR
     AQVEGQTNGD IFLLRGFVAA IRANPDMSQA EYEFLADQVM GGHSEFINIA AAPDLVINRV
     YPYEPNKAAL GLDYHKNEAQ REAVYRVRDS GKMVLAGPVN LVQGGVGFIA QFPIWSDMGH
     EAQFWGIISA VIDAEKLYAL SGLTDPDLNV DLVLVGRDGT GAQGEVFFGD PAVLDDNPVI
     MDIQLHTSTW QLAARPKDGW ITKAANYWRT RGFFLLIAVF ILGPILAASR LSQTRQKMID
     QLEQRDAEVE RLSLVAKHAT DSILVYDPKG NITWVNDGFS RLTGYSFEEA VGRHPGMLLN
     APETSQDVVD AIREHQENGL PFQSELLNRT KSGDQFWVHI NTFPILDEDG NLVMSIGIER
     EITEIKRHEE ELALAKLNAE EAARAKSEFL ANMSHEIRTP MNAIIGMAEL LSDEDLGEEN
     NQSLETIRSS GQALLTIIND ILDLSRLESG KLEISKVDFN LRNGVNGVVH LLKQKADQKG
     IALEVSYADD LPETLHADDG RVRQILVNLI GNAVKFTSSG GVYVHVRCDF DDPYTICFEV
     KDTGIGVSDA QAEQIFERFS QADTATTRAF GGTGLGLTIS SMLANRMGGA IALCSDYKDG
     ACFDVSIRGF APTGEVSAEP PAVEASQTAL DGITILLAED NKTNRLLIRK FLAAHPVTLL
     EAQNGKEAVD LCKENEPDII LMDMAMPEVD GLQAARLIRQ LPIPQPPIIA LTANAFASDK
     QACLDAGMDL FLSKPVSKSA LLAAMAAKLS PPAQRKQA
//
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