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Database: UniProt
Entry: A0A0X3Y794_9GAMM
LinkDB: A0A0X3Y794_9GAMM
Original site: A0A0X3Y794_9GAMM 
ID   A0A0X3Y794_9GAMM        Unreviewed;       885 AA.
AC   A0A0X3Y794;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AR688_10475 {ECO:0000313|EMBL:KUM52694.1};
OS   Rheinheimera sp. EpRS3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Rheinheimera.
OX   NCBI_TaxID=1712383 {ECO:0000313|EMBL:KUM52694.1, ECO:0000313|Proteomes:UP000054239};
RN   [1] {ECO:0000313|Proteomes:UP000054239}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS3 {ECO:0000313|Proteomes:UP000054239};
RA   Presta L., Bosi E., Fondi M., Maida I., Maggini V., Bogani P.,
RA   Firenzuoli F., Chiellini C., De Pascale D., Palma F., Di Pilato V.,
RA   Rossolini G., Mengoni A., Fani R.;
RL   Submitted (NOV-2015) 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:KUM52694.1}.
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DR   EMBL; LNQS01000009; KUM52694.1; -; Genomic_DNA.
DR   RefSeq; WP_068235415.1; NZ_LNQS01000009.1.
DR   AlphaFoldDB; A0A0X3Y794; -.
DR   OrthoDB; 9806130at2; -.
DR   Proteomes; UP000054239; 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; cd01987; USP_OKCHK; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; IPR038318; KdpD_sf.
DR   InterPro; IPR025201; KdpD_TM.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR   PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR   PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR   Pfam; PF13493; DUF4118; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF02702; KdpD; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
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   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KUM52694.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        396..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        423..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        446..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        472..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          663..880
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   885 AA;  98496 MW;  F848FDA8C9DA8A6E CRC64;
     MAQDVRSQKA DALLKSLQQQ QGGQLKIFLG AAPGVGKTCA MLNAAKECMQ QGVKVTVGLI
     ETHGRADTEA MLQGFSFLPR RELNYHGQQL TEFDLDAALA AKPELILVDE LAHTNVPGSR
     HKRRYQDIAE LLSAGINVYT TLNVQHIASL NDLVLQISGV RVSETVPDQF IDQAQQLVFV
     DLAPNHLLDR LAQGKVYLAD YAQQAVQQFF QLETLTALRE MAMKLVMGHV DSQLKTEQDA
     KARSSDYLIK DKLLVLISNR RDHEYLIRIG RRMAEKRQTP WLVVWVDTGQ LQYQAAQKRL
     QSAFALAREL GAQTEILRGP STLQTILPYL AEHRINTVLV GAGTKRRFQP WRKPLYQQLI
     NSGLPLEVSV WRAAERSSLP ASAAQASTTF GQKAGYVYGL LYTAIASLVV LGLSSWLQSG
     NLVLVYVLSV VVCGLKYGAR PAIFTAVLSF LSFNFFLTEP YYTFFVNKNA DIATLLFMLV
     IGVVCGPAAS RIRRQFLLLK EANRYSELQR DFAQQLTVIN QPDELWATLA TQLSQALHCP
     VHIVATTEQQ QIIPALKQPL QALDQAMIDW CQRHQQRAGR FSETLNASDW TAFALTAQEK
     TVAVLLVQFS PAQQLLRPDD TDLLTSLSQQ AFNVWQRMQL NTELESSKLK AEMEQLRSAL
     LSSVSHDLRS PLSAMMGSAE SLQMLDNQLS AEDRKELLDT IVQESGRLDR YIQNLLDMTR
     LGHGTLKLER DWVSVADIIG SARQRLKRFF PEVELTYQSE PDMPLLYVHA ALLEQGIFNI
     LENAAKYSPP GEPVLVFVSH KANICRIEIE DSGPGIAESL REKVFDMFYV VADGDSKRHN
     TGMGLAICRG MIGAHGGTVK ADAARVGSGS RFIIDLPLPE AQAGD
//
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