GenomeNet

Database: UniProt
Entry: A0A1X7IBR1_9RHOB
LinkDB: A0A1X7IBR1_9RHOB
Original site: A0A1X7IBR1_9RHOB 
ID   A0A1X7IBR1_9RHOB        Unreviewed;       682 AA.
AC   A0A1X7IBR1;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN02746000_00553 {ECO:0000313|EMBL:SMG12075.1};
OS   Paracoccus sp. J56.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=935850 {ECO:0000313|EMBL:SMG12075.1, ECO:0000313|Proteomes:UP000193912};
RN   [1] {ECO:0000313|Proteomes:UP000193912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J56 {ECO:0000313|Proteomes:UP000193912};
RA   Varghese N., Submissions S.;
RL   Submitted (APR-2017) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FXAQ01000003; SMG12075.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7IBR1; -.
DR   STRING; 935850.SAMN02746000_00553; -.
DR   Proteomes; UP000193912; 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; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 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; 3.30.450.20; PAS domain; 1.
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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 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; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:SMG12075.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000193912};
KW   Transferase {ECO:0000313|EMBL:SMG12075.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        39..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          312..535
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          559..675
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         610
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   682 AA;  74830 MW;  6B6D61BBAC1CE246 CRC64;
     MSSERTESLR SARIVLPFLT LPMVIGALWL AIYPHWREGG LVLISAGAVI MAWYLLAGIL
     SARHIGRALI TKRDLDDVLP AIHQHEQPAM ATDAAGLILA QNQEALDRFG DLVGHRIHEV
     LGRSHADPER MWSDLTIRLS RRGRIRADLG NGCEYTVTRR TRSEIRLWQA VACERSVTPP
     PAVLGSDHGD FDSLPVALIV LDPTGNIIRA NAAARNLLGG QILGQKLSIL LDGLGREIGD
     WVSDVCAGRT VGGSEVLHVK ADGPDRFVQL TLTRARGDYV TAVLSDASAL KTLEAQFVQS
     QKMQAIGQLA GGIAHDFNNL LTAITGHCDL LMLRHDKADP DYADLDQISQ NANRAAALVR
     QLLAFSRKQT LKPQIMDLRD TLSDLTHLLN RLVGERVVLT FDHDPALRMI RADRRQLEQV
     IMNLVVNARD AMPDGGDINI STDNVRLETK AEFGRAILPA GDYVRVQVRD QGCGIAPDDL
     VKIFEPFFTT KRVGESTGLG LSTAYGIVKQ TGGYIFCDSM LGEGSSFSLF FPAHDRHELE
     KTSPPVVVPI RPLRELEATV LLVEDEAPVR SFASRALKLQ GFKVLEAACA EDALSLLADE
     RLIVDVFVTD VVMPGMDGPA WVRTALRDRP DTKVIFMSGY TEDIFSEGRP PVPDAAFLAK
     PFSLSDLTAL VTRQLGDQRR DE
//
DBGET integrated database retrieval system