ID A0A0B4BMM7_9RHOB Unreviewed; 497 AA.
AC A0A0B4BMM7;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=RA20_11595 {ECO:0000313|EMBL:KIC19936.1};
OS Leisingera sp. ANG-Vp.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Leisingera.
OX NCBI_TaxID=1577896 {ECO:0000313|EMBL:KIC19936.1, ECO:0000313|Proteomes:UP000031177};
RN [1] {ECO:0000313|Proteomes:UP000031177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-Vp {ECO:0000313|Proteomes:UP000031177};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(2015).
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:KIC19936.1}.
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DR EMBL; JWLD01000032; KIC19936.1; -; Genomic_DNA.
DR RefSeq; WP_039128508.1; NZ_JWLD01000032.1.
DR AlphaFoldDB; A0A0B4BMM7; -.
DR STRING; 1577896.RA20_11595; -.
DR OrthoDB; 9815202at2; -.
DR Proteomes; UP000031177; 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 Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
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 PANTHER; PTHR44936:SF9; SENSOR HISTIDINE KINASE GLNK; 1.
DR PANTHER; PTHR44936; SENSOR PROTEIN CREC; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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 PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..497
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002101568"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 246..300
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 308..497
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 497 AA; 53349 MW; 4E10C4B750F04B19 CRC64;
MALVVAMVCC ALVSIPLAAM LTVRLTSSQF VRETEQALLQ QGAIYAEIYR NRFEAAEGLS
IGSIPEKEVL EFWASDLRPA RASINLRRDP VLPPMPAGAA AGPLSDPRHR ALLPALIEMA
REAGKSTLAG VIFLDHEGNG TGEEGLRSHA GLPEVKKALA GKLGTTLRAR EDAYGRHPLA
SLSRDTGYRV FVAYPVLSHG RVIGVILLSR TPLNLSKFLF RERDALIIMA LFTLTGAALT
GYLLLRLMSR PVRGLRDEAR AIAEGGKPPA QPLQHYGVRE LAELGQSMLS MAGTLHSRSR
EIATYTDHVT HELKSPVTSI TGAAELLSEP ALSAEDRDRL LGNIRSEAAR MNTLLTRLRE
MTQLRQASKS GPGHLKDMLP AVEGLSVRIL SPGGALVPLS QEHGQVILTH MAQNARAHGA
TTLDLHFESG LLRISDDGDG LSESDIPRLA DPFFTTRRET GGTGMGLAIV TAVLDGYGAA
LTATAAPEGA VFEIRFP
//