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Database: UniProt
Entry: A0A1H1V5N8_9PSED
LinkDB: A0A1H1V5N8_9PSED
Original site: A0A1H1V5N8_9PSED 
ID   A0A1H1V5N8_9PSED        Unreviewed;      1160 AA.
AC   A0A1H1V5N8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05216221_2667 {ECO:0000313|EMBL:SDS80022.1};
OS   Pseudomonas oryzae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1392877 {ECO:0000313|EMBL:SDS80022.1, ECO:0000313|Proteomes:UP000243359};
RN   [1] {ECO:0000313|Proteomes:UP000243359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 32247 {ECO:0000313|Proteomes:UP000243359};
RA   Varghese N., Submissions S.;
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; LT629751; SDS80022.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1V5N8; -.
DR   STRING; 1392877.SAMN05216221_2667; -.
DR   OrthoDB; 9764438at2; -.
DR   Proteomes; UP000243359; Chromosome i.
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; cd00156; REC; 1.
DR   CDD; cd10322; SLC5sbd; 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; 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   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; 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; 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:UP000243359};
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..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        39..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        158..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        192..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        245..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        284..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        328..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        378..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        414..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        442..464
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          805..1018
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1041..1157
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          750..798
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         1091
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1160 AA;  127398 MW;  CE1A5BB900F3D403 CRC64;
     MSLSSGLITA VALLYMAALF AIAFYGDRRQ NRGISRPRLR AWIYSLSLAV YCTSWTFFGS
     VGQAAENLWS FVPIYLGPVL LMLFLPQMLA KMILISKQEN ITSIADFIAA RYGKSQPLAI
     VVTLVCLVGV LPYIALQLKG IVLGVNLLTG AKADANGVGA QDTALVVSLI LALFTILFGT
     RNLDATEHHR GMVMAVAFES IIKLLAFLAV GAYVTWGLFD GFADLLDRAQ NTPRLDDYWR
     QPLDWASLLV QTGVAMMAIV CLPRQFHVTV VENIEPRDLN LARWVFPLYL LLAALFVVPI
     ALAGQMLLPA GVVPDSFVIS LPLAEAHPAL ALLAFIGGAS AATGMVIVAS VALSTMISND
     MLLPWLLRRH SAERPFEVFR HWLLSVRRIS IIALLLLAYV IYRLIGPNIS LASIGQIAFA
     AITQLGPAMF GALYWKQANS RGVFAGLAVG ALLWFYTLLL PLVASGMKWS LAQLPGQQWL
     ATNPLSLPLD GVTQGTLLSL CGNFLTFALV SWLSRTRVSE HWQASRFVGQ EASVRPSPRM
     LLAVQVQDLL MLAARFVGEE RARQSFIRFA YRQGKGFSPN QTASGEWIAH TERLLAGVLG
     ASSARAVVKA AIEGREMQVE DVVRIVDEAS EVLQFNRALL QGAIENISQG ISVVDQSLRL
     VAWNRRYLEL FEYPEGLISI GRPIADIIRY NAERGLCGKG DPDIHVAKRL YWMRQGTAHT
     SERVFPNGRV IELVGNPMPG GGFVMSFTDI TAHRQAEDAL KEANESLEQR VAERTRELSA
     LNEQLSEAKA RAESANQSKT RFLAAVSHDL MQPLNAARLF SAALAHQEAL PGEVRDLVQH
     LDSSLRSAED LIADLLDISR LESGRFTPER SAFALDTLYD ALGVEFRALA QEQGIDLRIR
     ASKQRVDSDP KLLRRVLQNF LTNAFRYAKG KVLLGVRRDG RHLRLEVWDR GPGIPPDKLK
     VIFEEFKRLD SHQTRAEKGL GLGLAIADGL CQVLQHKIEV RSWVGRGSVF SVRVPLARGR
     AVPLARTQTA GATPQPLNGA QVWCIDNEDS ILTGMRSLLS RWGCQVQTAR TRTECEQLLA
     QGGLPELVLA DFHLDHGETG LALMGWLRAH LGQPVPGVVI SADGRAELIA EVHAAGLDYL
     SKPVKPAALR ALLSRHLKLR
//
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