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Database: UniProt
Entry: T0PAA4_AERSA
LinkDB: T0PAA4_AERSA
Original site: T0PAA4_AERSA 
ID   T0PAA4_AERSA            Unreviewed;       862 AA.
AC   T0PAA4;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=kdpD {ECO:0000313|EMBL:ATP07284.1};
GN   ORFNames=Asalp_00170 {ECO:0000313|EMBL:ATP07284.1};
OS   Aeromonas salmonicida subsp. pectinolytica 34mel.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=1324960 {ECO:0000313|EMBL:ATP07284.1, ECO:0000313|Proteomes:UP000222916};
RN   [1] {ECO:0000313|Proteomes:UP000222916}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=34mel {ECO:0000313|Proteomes:UP000222916};
RX   PubMed=29304740; DOI=10.1186/s12864-017-4301-6;
RA   Pfeiffer F., Zamora-Lagos M.A., Blettinger M., Yeroslaviz A., Dahl A.,
RA   Gruber S., Habermann B.H.;
RT   "The complete and fully assembled genome sequence of Aeromonas salmonicida
RT   subsp. pectinolytica and its comparative analysis with other Aeromonas
RT   species: investigation of the mobilome in environmental and pathogenic
RT   strains.";
RL   BMC Genomics 19:20-20(2018).
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};
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DR   EMBL; CP022426; ATP07284.1; -; Genomic_DNA.
DR   RefSeq; WP_021139876.1; NZ_CP022426.1.
DR   AlphaFoldDB; T0PAA4; -.
DR   OrthoDB; 9806130at2; -.
DR   Proteomes; UP000222916; Chromosome.
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   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:ATP07284.1};
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, ECO:0000313|EMBL:ATP07284.1};
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        382..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        409..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        457..475
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          640..857
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   862 AA;  94213 MW;  B02F854FA15EAC68 CRC64;
     MRDEARADAL LASLEQEHKG KLKVFLGAAP GVGKTYAMLQ AVREQAREGV DILIGVVETH
     GRQETLALLD KLAIQPRKLH LHRQQRLEEM DLDALLARKP AIVVVDELAH SNAPGSRHEK
     RWQDVEELLG AGIDVYSTLN VQHLESLNDL VWQLTGVRVK ETLPDQVLLE ADSIVLIDLP
     PKELLGRLKE GKVYVPHQAK AALQSFFSLN NLTALRELAM QTAASHVEGD LQLQWQAAGK
     TTLPLRGKLM VCLGDQHGSA LVRYGHRFAQ RRQLPWLVVH IDSKGQRSAE LEQALALASH
     LGAKVLTLSS PAVASTLLET AEQQQVSQLL LGKPHKAPWR RSLVQHLLKQ AQGLEITLVD
     TEKRKPGIGL QPLHPKDIRQ SLLAVTIMGL TSAAAWGLSH WLPPASLPLL FVLGVLATAL
     TTSLVPAILA AVLGFVGHNL LFTAPYFSLS VASHSDLLTL FVLLIVGMTA GRLASRQRQQ
     LVGLRETQQL GNALLSLSQG LATASSPEEV LRQGTQAISL ALAQPVFALD QDYQYRAGSA
     QHNPGQTDKA AIDWCLAQKQ SAGAHTATLN AAEAQYHHLT DELILGIRLS NPLASSAEHQ
     LQALLTDIRA ALARIDLNER LADSQLQAET DRMRAALLSS VSHDLKTPLA TIMGAGSTLL
     EYGDRISPED RSELLHSVQD EARRLHSYVQ NLLDMTRIGS PDFQLKRDWV DLADLVESAR
     KRLESSWRQH KLLVHFDQQI PQLYVHGALI EQVLVNILDN ASRYSPAGTP IEFKVMLADP
     DLILDIIDIG VGIAESDRDK IFNLFYTQPV GDCGSRGTGL GLAISRAMIE AHGGRIWAFS
     GPNGNGTCMR ISLPLALNAP EV
//
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