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Database: UniProt
Entry: A0A1P8R686_9GAMM
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ID   A0A1P8R686_9GAMM        Unreviewed;       726 AA.
AC   A0A1P8R686;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BWR19_14645 {ECO:0000313|EMBL:APX94072.1};
OS   Halomonas sp. 1513.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1883416 {ECO:0000313|EMBL:APX94072.1, ECO:0000313|Proteomes:UP000187327};
RN   [1] {ECO:0000313|Proteomes:UP000187327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1513 {ECO:0000313|Proteomes:UP000187327};
RA   Shuang W.;
RT   "Complete genome sequence of Haloterrigena daqingensis type strain
RT   (JX313T).";
RL   Submitted (JAN-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   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP019326; APX94072.1; -; Genomic_DNA.
DR   RefSeq; WP_076748936.1; NZ_CP019326.1.
DR   AlphaFoldDB; A0A1P8R686; -.
DR   STRING; 1883416.BWR19_14645; -.
DR   KEGG; halo:BWR19_14645; -.
DR   OrthoDB; 9797243at2; -.
DR   Proteomes; UP000187327; Chromosome.
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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.20.120.160; HPT 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; IPR036641; HPT_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF01627; Hpt; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000187327};
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..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          235..452
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          476..593
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          628..723
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   MOD_RES         525
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         667
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   726 AA;  78355 MW;  9D12ACEF6DE76A04 CRC64;
     MLRYPGRLKL GAIAALLFFI AAITVAGLVL WRQDSLAQSV GGDAAWSAYK LDREAIQLRS
     QLARPADQGT LSDLRLRFEL MYSRVNLLRR GELAELLDSI PRASSLMASI GDQVDAIDER
     LYREDFSLEQ DGRDALDARL DTLSRYSEEL IVAINAHLAD TTTHEREQLQ GLYRLLLGLI
     MAMSAAAALV VVFLFREARE SAAARRATEA LSGELEITAR RAEAASQAKS EFLATVSHEI
     RTPLNGVIGM SELLRERPLD ATSRHYAATI HESGGLLLGL INDILDFSKI EAGRLELEHT
     DYDLRELMAQ AVALFAPRAS AKSLTLRSEC DPRLPARLSG DPGRVNQIIL NLLSNAIKFS
     TRGEVVLAAQ RGEDEGLEIS VSDQGCGIDE GQRDLLFEPF RQGDPSTARR FGGSGLGLAI
     CKQLASAMDG EIDFTSAPGQ GSRFWLRLPL QPAMAADTVV PASRPHVATA VNFGASLLLV
     EDNPINQQVA VAMLERLGCR VTVAASGSEA LACCEAQRFA LIFMDVQMPD LDGLAVTRAL
     RQRDGWTRQV PIVAMTAGAL DGDQARCREA GMDGYLAKPL FRETLLAMLE RHLPDAPHPA
     PAASPDTPDE ASTWLDGAAL EELEASLALA DRQALLALFQ SNMPARLDQL EAARAADDLA
     RTAQLAHLIK GEAGSLGLGR LAAAAQRLEQ AAAQQAPCQA ALEALRDCLA PSLAALARRW
     PASETS
//
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