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Database: UniProt
Entry: R8ARW3_PLESH
LinkDB: R8ARW3_PLESH
Original site: R8ARW3_PLESH 
ID   R8ARW3_PLESH            Unreviewed;       867 AA.
AC   R8ARW3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=PLESHI_07935 {ECO:0000313|EMBL:EON89061.1};
OS   Plesiomonas shigelloides 302-73.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Plesiomonas.
OX   NCBI_TaxID=1315976 {ECO:0000313|EMBL:EON89061.1, ECO:0000313|Proteomes:UP000014012};
RN   [1] {ECO:0000313|EMBL:EON89061.1, ECO:0000313|Proteomes:UP000014012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=302-73 {ECO:0000313|EMBL:EON89061.1,
RC   ECO:0000313|Proteomes:UP000014012};
RX   PubMed=23814109;
RA   Pique N., Aquilini E., Alioto T., Minana-Galbis D., Tomas J.M.;
RT   "Genome Sequence of Plesiomonas shigelloides Strain 302-73 (Serotype O1).";
RL   Genome Announc. 1:e00404-13(2013).
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:EON89061.1}.
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DR   EMBL; AQQO01000047; EON89061.1; -; Genomic_DNA.
DR   RefSeq; WP_010863210.1; NZ_KB944508.1.
DR   AlphaFoldDB; R8ARW3; -.
DR   PATRIC; fig|1315976.3.peg.1567; -.
DR   HOGENOM; CLU_000445_113_1_6; -.
DR   OrthoDB; 9806130at2; -.
DR   Proteomes; UP000014012; 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; cd00075; HATPase; 1.
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   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EON89061.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014012};
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        386..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        414..442
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        462..480
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          645..862
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   867 AA;  94974 MW;  F02B898C16214709 CRC64;
     MRDDVRADAL LASLENEQKG KLKVFLGAAP GVGKTYAMLQ AVREQFNEGT SILIGVVETH
     GRRETLALLD KLPMQARKTV YHRNQRIEEM DLDALLEQKP ALAVVDELAH SNAPGSRHEK
     RWQDVQELLA AGIDVYTTLN VQHLESLNDL VWQLTGVRVK ETLPDQVLLD ADSLVLIDLP
     PKELLERLRE GKVYVPHQAK TALQSFFSLN NLTALRELAM QTAASHVEGD LQLQWQAAGK
     ATQPLRGKLM VCLGTQQGMA LVRYGHRFAQ RRQLPWLVLH VDTNGQTSAE TEQALALASQ
     LGAKVLTLSS PSVADAIRLT SEQQQVSQLL LGKPHKIPWR PSLVQYLIRA TQGLEITLVD
     VAQTADAVSN PKRKDKLNAA GKWRDYAISA VIMGSTTVLA WFLSSWLPDS SIPLIFVLGV
     MTTALSTSLL PATLASIFGF IAHNLLFVDP LYSLKVSRHS DLLTLLVLLI VGMTAGRLAS
     RQRKQLISLR ESQHLGNALL ALNQALSKAN SSEEVVRLGS EAIAGALHIA VVVLDQDYLE
     HSGNSLAIPG QTDKAAIDWC LAKKQSAGAF TATLNAAESQ YHPLTDHLVL GIRLLSPLSA
     GAERQLQALL SDMRAALARI DLDERLADSQ LQAETDRMRA ALLSSVSHDL KTPLATIMGA
     SGTLLAYDEK IPPEEKNELL QSIQEEAARL RSYVQNLLDM TRIGSPDFQL KREWVAIEDL
     VDAAYHRLQA AWRQHKLLIH IDQNIPLLYV HGALIEQVLV NVFDNAVRYS PAGTPIEFKV
     VLALPDIIID IIDMGAGIAD ADRSKIFNLF YTQPVGDCGS RGTGLGLAIS RAMIEAHGGK
     IWAFPGVNKV GTCMRISLPV GLNSPEK
//
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