ID A0A1J8PWY9_9GAMM Unreviewed; 1313 AA.
AC A0A1J8PWY9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=QHL1GM_08830 {ECO:0000313|EMBL:OJA05488.1};
OS Halomonas sp. QHL1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1123773 {ECO:0000313|EMBL:OJA05488.1, ECO:0000313|Proteomes:UP000183854};
RN [1] {ECO:0000313|EMBL:OJA05488.1, ECO:0000313|Proteomes:UP000183854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QHL1 {ECO:0000313|EMBL:OJA05488.1,
RC ECO:0000313|Proteomes:UP000183854};
RA Seilhamer J.J.;
RL Submitted (AUG-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:OJA05488.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MINL01000001; OJA05488.1; -; Genomic_DNA.
DR RefSeq; WP_071694161.1; NZ_MINL01000001.1.
DR STRING; 1123773.QHL1GM_08830; -.
DR OrthoDB; 9764438at2; -.
DR Proteomes; UP000183854; 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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
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; 2.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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; PF08448; PAS_4; 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; 2.
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); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:OJA05488.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:OJA05488.1};
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..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 40..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 65..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 387..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 410..433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 440..463
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 840..893
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 950..1165
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1189..1306
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 884..943
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1240
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1313 AA; 145279 MW; 5A06978D5AF5ED97 CRC64;
MFHGGLLVAV SLLYIAVLFG IAWYGDRRAR THGATRRRPI IYSLALAIYC TSWTFYGAVG
QAATAGWSFA SIFVGPILTF LLFWPVLAKM IRVAKHQNVT SIADFIASRY GKTQSLAAFA
SLVALVGTLP YIALQLKAVS TTFSVLTDAT DVTHTPLFGD TAFYVAIVMA IFAILFGTRH
TDATEHHEGL IHAVAFESLV KLLAFVVLGA FVTWGMFDGL GELMGHAESQ LELQRQLANQ
DFGQSFWAQT LLAMLAILCL PRQFHVAVVE NIHPDDATKA RWLFPLYLLA IAFFVVPLAA
AGLLLFSESG VEPDTYVLAL SMASGHQWLT LLTFIGGFSA ATGMVIVAAV AVSIMISNEI
VIPALFRLRW FDTKARDYGR LVLRARRLTI VAVLAMAYGF YQLIAEFTSL ASIGMLSFAA
AAQFAPALIG GLYWKRGNRL GVIVGMNAGF AIWAYSLLMP AMINAGVLPT AWLDGGPLGL
NWLSPTALFG LNLGDSFTHG VMLSLGVNLF CYIFVSQVTS QRVVERIQAS LFVDSVETRQ
TSVNRPWTGA TTVGDLKVLC ERFLGAGQVD RAFEDYARRV GKPLDDGTRA SIDIIQFTER
FLASVLGASS ARIVVNSALQ GRGIGISDVI SIVDEASQVL EFNRALLQAT IENINQGISV
VDQNLRLVVW NQRYLELFRF PDHLIRVGAP IDRIFRYNAH NGEYGPGDPE EHVQLLLDNI
REGQPHRYVR YRQDGSVLEV QGNPMPGGGF VYTYQDITQQ KRIEEALIRS ENNIRIYTDN
VPALIAYFDK ECRYLFTNRA YEQAFNIDRN AVIGRRFEDV LQIKQAEERA PWVARALKGE
RVSFEVSLRV NEAMRYMLVT YTPHFGDSQA ILGFFALYQD ITERRQAEIA LKETNETLEE
RVRERTQALS EANAALRQEN RVRAEAELAL RQAKQLAEDA NASKTRFLAA ASHDLLQPLN
AARLFTSALM QNVTTTDTQR IVGHIDNSLQ AAEELLSTLL DISKLDAGAL TPRRSHFALA
DIFRPLRAEF EVMADDRGLD LEVVPTRLWV DSDPQMLRRI VQNFLSNAIR YTQEGRVLLG
CRRQNGWLSI EVWDSGPGIP ESKLSEIFQE FRRLDQVSRH KESEKGLGLG LSIADRMSRV
LDHPIKVRST VGKGAVFSVS VPIVTAHEAS SNELEPQARR GSHKLSGTRI VCIDNETLIL
EGMTAMLSGW GCEVFTATSI GGAKSILRNM DGDPDAILAD YHLDNEVTGL MALEALSERF
EGAVPGIVIT ADRTEAVAEE IKRAGYQLLL KPVKPAALRA LLTRTLQANR AAR
//
