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Database: UniProt
Entry: A0A1V1V304_9CAUL
LinkDB: A0A1V1V304_9CAUL
Original site: A0A1V1V304_9CAUL 
ID   A0A1V1V304_9CAUL        Unreviewed;       348 AA.
AC   A0A1V1V304;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=baeS_2 {ECO:0000313|EMBL:GAW42272.1};
GN   ORFNames=SH203_02688 {ECO:0000313|EMBL:GAW42272.1};
OS   Brevundimonas sp. SH203.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=345167 {ECO:0000313|EMBL:GAW42272.1, ECO:0000313|Proteomes:UP000195546};
RN   [1] {ECO:0000313|EMBL:GAW42272.1, ECO:0000313|Proteomes:UP000195546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH203 {ECO:0000313|EMBL:GAW42272.1,
RC   ECO:0000313|Proteomes:UP000195546};
RA   Suzuki T., Kikuchi M., Habu N., Konno N.;
RT   "Draft Genome Sequence of Brevundimonas sp. SH203, producing Cellouronate
RT   (beta-1,4-linked polyglucuronate) lyase.";
RL   Submitted (MAR-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   -!- 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:GAW42272.1}.
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DR   EMBL; BDMM01000006; GAW42272.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V1V304; -.
DR   OrthoDB; 9804645at2; -.
DR   Proteomes; UP000195546; 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; cd06225; HAMP; 1.
DR   CDD; cd00075; HATPase; 1.
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; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 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; SSF158472; HAMP domain-like; 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, ECO:0000313|EMBL:GAW42272.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195546};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        12..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        49..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          78..132
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          140..348
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   348 AA;  38227 MW;  9C41F70CFA624E83 CRC64;
     MIQHSPSLRR KFSFYMATVA ISGLLSSFVV WGGFYFVFVD PRNEYLESYL NFIDLAALLL
     SVMLGLIVSL VAARILSKRI AAPLSEVALV ARHLTAGDLS ARVAYKDGSL GEISQLISDF
     NTLAAHLQQS TNESIQWNAA IAHELRTPLT IMNGMMEGVA DQVFDLDDEW MALMKFQLEG
     LTRIVEDLRV ISLYESGRMS LKTERLALDQ VIQPLRSLYE PLLSKLGFTI EWESRPVRVF
     GDSTRIRQAL NALLENVRVH AAPGVVRVSI EENAGFAVIS VADSGPGIPH DIAPQMFDPF
     RSARSDAKGS GLGLTVVKYI AEAHGGYALL GRSESGGLRA EFELPLAD
//
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