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Database: UniProt
Entry: A0A1I4VAW4_9GAMM
LinkDB: A0A1I4VAW4_9GAMM
Original site: A0A1I4VAW4_9GAMM 
ID   A0A1I4VAW4_9GAMM        Unreviewed;      1117 AA.
AC   A0A1I4VAW4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05216289_101264 {ECO:0000313|EMBL:SFM98130.1};
OS   Dokdonella immobilis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dokdonella.
OX   NCBI_TaxID=578942 {ECO:0000313|EMBL:SFM98130.1, ECO:0000313|Proteomes:UP000198575};
RN   [1] {ECO:0000313|EMBL:SFM98130.1, ECO:0000313|Proteomes:UP000198575}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.7659 {ECO:0000313|EMBL:SFM98130.1,
RC   ECO:0000313|Proteomes:UP000198575};
RA   de Groot N.N.;
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC       family. {ECO:0000256|ARBA:ARBA00006434}.
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DR   EMBL; FOVF01000001; SFM98130.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4VAW4; -.
DR   STRING; 578942.SAMN05216289_101264; -.
DR   OrthoDB; 9764438at2; -.
DR   Proteomes; UP000198575; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd00156; REC; 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; 3.30.450.20; PAS domain; 1.
DR   Gene3D; 1.20.1730.10; Sodium/glucose cotransporter; 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; IPR038377; Na/Glc_symporter_sf.
DR   InterPro; IPR001734; Na/solute_symporter.
DR   InterPro; IPR000014; PAS.
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   NCBIfam; NF041832; near_NosP_CTERM; 1.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43047:SF9; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF12860; PAS_7; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 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; 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; PS50283; NA_SOLUT_SYMP_3; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000198575};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        36..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        66..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        113..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        154..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        196..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        229..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        268..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        315..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        374..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        399..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        431..456
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          599..639
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          764..973
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          993..1107
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          730..757
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         1042
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1117 AA;  120129 MW;  5815EB4A68F7D473 CRC64;
     MLPDLKILGA GLLWLGLLFG AAVLGDRRPK FFARHWALIY SLSLAVYCTS WTFYGTVTQA
     SRSGWWLPPT FVGTILIYLF GFGLLMRLVS IARAHNSSSL ADLVAIRLGR SPAIAALVTA
     VAVIGIVPYI ALQLKSVAMS YGMLARRQDL MAPAWQDSAL WVALAMALFA MLFGARRASA
     TAHNRGLVLA MAFESLFKLI AMLALGVLVW FGISLPADAS PSLPPPGGSA GFTTLIMLGA
     FAVFTLPHQF HAGVVECRDP EHVRTARWLF PLYMLLIALP ILPLARAGDA LLAPLGVPSD
     LYVLALPLAN GHGTLALIAF LGGLSAATSM VVVATLALSL MIGNHWIAPL RVRAGWGRAA
     VGDLRGEVLL QRRLIILVVV LLAWAYSRVL VASDALADIG AVSFSALSAI APGVLVAVYR
     PQLGARAVGA GLVAGSLVWL YALMLPVLAG GSLAWVEQGP FGIEWLAPDR LLGFDDWSRL
     ARAVVLSLAA NVAVIGLVAS SRFAHGAKSG HRGLVDVGDL RALASRFLAD EQVEALFGAN
     EGDSPASETL VAAIEHELAA VIGASSARLL LTVARRERSV ELEAVAAIVG ETSQDLRFNQ
     RVLEAALENM SQGISVVDRD LGLVAWNQPY ARLFGYPPEL LRVGVPIADL LRWNLTHRLS
     VAHSADEEVH KRIRHMRAGT PYVAERTFET DDGERVVEIR GNPMPGGGFV ATFTDVTEFR
     RNEAELMQVA ETLELRVEER TAELDMARRE AEKANRAKSR FLAAVSHDLA QPLNAAHLFT
     HALAQRLGHA EYREAVDNIS GALTSAEDLL SGLLDISRLD GGQTRARAEA FPLREWLGGL
     AAEFSVLADE RGLRLDAVPC SAWIRSDPQL LRRIVQNFLA NAVRHTRSGR ILLGCRRRRS
     HVSIEVWDTG PGIALADQEL IFEEFRRLGH SGEGLGLGLA IADRIARLLG HRISLRSRPG
     RGTVFSIEVP TTATLQPPLT VAPPQAQALP RRRLLVVDND PAVLKAMQAL LAGWQSEVSA
     AQTPAQARLL FAEHGADVLL LDYHLDDHVS GLQLRESLGP AAQGIPCVII TADHGKTVSD
     AVLAAGCQLL HKPLKPLALR SLLAQLIARD TGGENSR
//
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