ID A0A165U5H6_9GAMM Unreviewed; 1175 AA.
AC A0A165U5H6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A3709_15640 {ECO:0000313|EMBL:KZX58989.1};
OS Halioglobus sp. HI00S01.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Halioglobus.
OX NCBI_TaxID=1822214 {ECO:0000313|EMBL:KZX58989.1, ECO:0000313|Proteomes:UP000077184};
RN [1] {ECO:0000313|EMBL:KZX58989.1, ECO:0000313|Proteomes:UP000077184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI00S01 {ECO:0000313|EMBL:KZX58989.1,
RC ECO:0000313|Proteomes:UP000077184};
RA Sosa O.A.;
RT "Microbial cycling of marine high molecular weight dissolved organic
RT matter.";
RL Submitted (MAR-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}.
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:KZX58989.1}.
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DR EMBL; LWEE01000025; KZX58989.1; -; Genomic_DNA.
DR RefSeq; WP_066051167.1; NZ_LWEE01000025.1.
DR AlphaFoldDB; A0A165U5H6; -.
DR OrthoDB; 9764438at2; -.
DR Proteomes; UP000077184; 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; 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 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}; Kinase {ECO:0000313|EMBL:KZX58989.1};
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:UP000077184};
KW Transferase {ECO:0000313|EMBL:KZX58989.1};
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..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 327..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 390..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 413..435
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 442..465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 821..1037
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1058..1174
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 759..807
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1108
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1175 AA; 129187 MW; DAEE7DB267183DD0 CRC64;
MVTASNLLSL ALLYICVLFA VAWWADRQVD EGAQDSWLAR PDVRGLIYAL SLAVYCSSWT
FYGAVGSATA TAWGHAPIYL GPIALFVLGW PIIQRLLAVG ERHRVTSIAD YIGARYGKRQ
ALAVLVTLVA TTAVLPYIAL QFKALAQAWS IVGGNLEGMG EYDGDTALLV AIVLAVFTIL
FGTRRLDGRE RHQGMMAAVA IESIVKLVAF VAVAILALAY LGRLPADIRV TQGSQALGEF
SITADFLART LISALAILCL PRQFHVMVVE AGQGTRTGVA RWLFPAYLAL FMLLVVPISL
AGAHVYAMSD TISPDTYVQL LPISLEARWV TVAAFIGGIS AATGMVIVAT VSLAIMITNE
IVAPMIMRAN AASAAAVLNL GDSLRRSRQL TIAGILLAAW LVTRQIMNIP WLTQIGFISF
LAAAQLAPGL LAGLYWRRAH GIGVIVGLLC GLGLWFYCCV LPVVLNVDAT LLTQGLFGQN
WLRPMNLFGI SGENRLAYAT GWSLTVNLVA LVVLSLAFKP SQADIRQARL FTEDQQASPS
ESDRDFELSL IRVSQLQALL PPFLDEAESR AMWLRFEDSY EQRLLPGDRA PIFVVTQVEA
VLARIIGSTS AHQAMEQLER SQQLEYTDLA GMVTDASRLN TFNRELLQTT VESLIQGVSV
VDKELRLVAW NKRYEEMFHY PQRFLYVGCP IERVYRFNAE RGILDTGGRL VEEEIDKRLA
WLREGNPHRL ERTLPDGTVI DIRGTPLPHG GFVTTYIDIT DYRDVVAQLE DAKLELEQKV
ASGSQTLSET NAKLRQENRL RAQVESRLRD AHQSRTRFMS ATSHDLLQPI NAARLFTAVL
KPRLSGDGEG ETRRVVDQID SSLQRAEELI AELREISRLD SGKQMPRRSH FPISAIFDSL
SREFIPVAQS RGLELSVVDS SAWLYTDQAL LTRILQNLIS NAVKYTDSGR IVVGLRRRRD
GAELQVLDTG PGIAEQDQLL VFQEFQRLER HRHQGEEGLG LGLAIVARYA ELLGHHLKLR
SAPGRGSCFA IGVTFGQPQQ QDTREQQSSL GADLQGLKIV CVDNDPLILD GMQELLSTMG
AVVSTAAGRE ALLRRIGERP TPDIVLADYH LDEGDTGLNA VIEARKLLGK ALPCIIISAD
DSDVIRDRAK AAGFRFLPKP VNAARLRALV LALTR
//