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Database: UniProt
Entry: A0A1V2GXK8_9PROT
LinkDB: A0A1V2GXK8_9PROT
Original site: A0A1V2GXK8_9PROT 
ID   A0A1V2GXK8_9PROT        Unreviewed;       868 AA.
AC   A0A1V2GXK8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-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=BKE38_21865 {ECO:0000313|EMBL:ONG48458.1};
OS   Pseudoroseomonas deserti.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Pseudoroseomonas.
OX   NCBI_TaxID=1817963 {ECO:0000313|EMBL:ONG48458.1, ECO:0000313|Proteomes:UP000188879};
RN   [1] {ECO:0000313|EMBL:ONG48458.1, ECO:0000313|Proteomes:UP000188879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M3 {ECO:0000313|EMBL:ONG48458.1,
RC   ECO:0000313|Proteomes:UP000188879};
RA   Subhash Y., Lee S.;
RT   "Draft Genome sequence of Roseomonas sp. strain M3.";
RL   Submitted (OCT-2016) 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:ONG48458.1}.
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DR   EMBL; MLCO01000245; ONG48458.1; -; Genomic_DNA.
DR   RefSeq; WP_076959416.1; NZ_MLCO01000245.1.
DR   AlphaFoldDB; A0A1V2GXK8; -.
DR   OrthoDB; 9796100at2; -.
DR   Proteomes; UP000188879; 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; cd19410; HK9-like_sensor; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
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; IPR007891; CHASE3.
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; IPR035965; PAS-like_dom_sf.
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; PF05227; CHASE3; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF12860; PAS_7; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
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; 2.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000188879};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        182..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          352..575
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          595..711
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          749..864
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         645
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         799
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   868 AA;  92428 MW;  B0854A8B9539AB42 CRC64;
     MRRGKPWPIL AVALALLAVS LGLLVASHVS SQLQANRQAV WHSFRVADVT RALLSAVQDA
     ETGQRGYILT ERDSYLGPYE AAQRQVPLLQ RQLGQLLAGN AAQRARAERL QGLVEDKMVE
     LAESLTLSRN QGFAAGRALV QTDRGRELML AIRGAVEAIL SEQQAALGQQ VEAADRSQDA
     SLLAALSGIV LSLAAIAAGT LLLLRNNTRL KRAEAALAEK GAVLQATLDH IQDGVAAFDA
     AGALVACNRQ FFTLLDFPHA LAKLGTPFSA FLAIDRRREP SVLAAPDRVR GPAGSGQQVS
     LSQAGRELEV YRNAMPEGGF VVSCIDVTRR AQAEAILRQT QKMEAIGQLT GGVAHDFNNM
     LQVVSANLEM LGRELGPEHG GRRHLGHAIS GVARGARLTA QLLAFARRQP LDPRVIHPGR
     LVQEMTDLLR RTLGERIAVE AVVAGGLWNT QVDPGQLENA LLNLALNARD AMPEGGKLTI
     EVANAALDED YAAVHLEVEP GQYVMLAVSD TGLGMPPGVM ARVFEPFFTT KEEGHGTGLG
     LSQVYGFVKQ SGGHVKLYSE PGQGTAVKLY LPRSRRAEDL LGGGSLGPVV GGHETILVVE
     DDAELREAVV EMLQGLGYRV LRAEQAEAAL TVLSSGVQVD LLFTDVVMPG PIRTRDLARR
     AQEMMPGLKV VYTSGYTANA IIHDGRLDED VQLLSKPYRR EDLARHLRRA LGAAAPEPGL
     LAAAALGGGS GEAAGEGGET PIGWPEGAVA LVVEDDPLIR MNLVQMVEIM GLTPAEAGKA
     ETALAWLGKN PRPALLITDL TLPGMDGIAL AVEARKLHPG LPVMLATGHA EGSLSIPPEL
     ADGLGFLGKP FAMLQLERAL KALWLKTR
//
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