ID A0A370KA23_9GAMM Unreviewed; 1150 AA.
AC A0A370KA23;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DVT68_11540 {ECO:0000313|EMBL:RDI99277.1};
OS Dyella solisilvae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=1920168 {ECO:0000313|EMBL:RDI99277.1, ECO:0000313|Proteomes:UP000254711};
RN [1] {ECO:0000313|EMBL:RDI99277.1, ECO:0000313|Proteomes:UP000254711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHG54 {ECO:0000313|EMBL:RDI99277.1,
RC ECO:0000313|Proteomes:UP000254711};
RA Gao Z., Qiu L.;
RT "Dyella solisilvae sp. nov., isolated from the pine and broad-leaved mixed
RT forest soil.";
RL Submitted (JUL-2018) 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:RDI99277.1}.
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DR EMBL; QQSY01000002; RDI99277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370KA23; -.
DR OrthoDB; 9764438at2; -.
DR Proteomes; UP000254711; 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 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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 35..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 400..421
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 428..450
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 794..1008
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1029..1144
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 739..773
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1078
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1150 AA; 126284 MW; 30C8EC9541630B31 CRC64;
MLLLVSLLYV GLLFVVAYAG DRRPLYPRQP RLRPLVYSLA LAVYCSSWTF YGAVGTAARE
GLAYLPIYLG PILLFVFGYG LMRRLVLVAR HRNITSIADF IGARFGKSHG LAALVAIIAV
IAVVPYLALQ FKAVSMSYAV LGGFGAPGAA QFGDSALWCA ILLATFAILF GTRTIDATEH
HHGMMLAIAV ESLIKLMVFV GLAAYALWRG PGLHATLQLP MQQATQGVSP GFLAQTLLAF
CAMFCLPRQF QIGVVECEDP RDLRSARWLF PAYMAIVCVV VLPIVAAGLH LPQVRMGNQD
AWVLTLPMAY GDRGMALLAF LGGFSAATGM VIVASVALST MISNDLVMPM LLRIHRFKLE
QRTDLSQLVL LVRRIAIIAL SAMAYVYYRV VADNTNLAAT GLLAFAAVAQ FAPGIVAALY
WRSASRRGVS VGLAAGFAVW VYTLLLPAMW RSAPWLDTGP AGLGWLRPQA LFLLSGWDPV
MHGTFWSLLF NVACLIFVSL RFRPSLEERL HAAMFIDPYA IDNRGAGDWR GRVAVADLRT
IAERIVGERT SQRAFDDYAE RRGKPLQPGE AADRALIQYT ERLLASAVGA ASARRILMGA
LSGSGLDIAE AMALMDEASQ ELRFNRELLS TTLENVSQGI SVVDAHMRLV AWNRRYLELF
DYPDGMVYVG VPVADLIRWN AEHRECGPGE VEAHVAKRIG HMRAGSPHLF QRIRPDGTVI
EMRGRALPGG GYVTTYTDVT AYKHAEQALI EANENLEQRV DQRTAELSEA LNATAHARRE
AEMANASKTR FLAAASHDLL QPLNAARLFT SALRQHPGLD AEASQLAERI DASFRAAEDL
LDALLDTSRL DAGSYRADIS NVALADLFDS LKAQFAVVAE QRGLNLRVAP TRLAVRSDPQ
LLRRVLQNFI SNALRYTRSG AVLLGARRLG HEVRIEVWDT GPGIPPEQRA RIFGEFQRLD
RPSPWGEKGL GLGLSICERI AGILDHRLEL ESREGRGSRF AVRVPRAETP APRRRTVAHT
VSHERLPLTV LCLDNDPSIL DGMRALLQRW GVDCRTALDV TQAQQELLRG RIDLILADYH
LNDDMDGLQA LQQLRGVVDE LPPVAMITAD GSSELKQRAR TLGYPLLHKP VRPAALRALL
SALVRRQTPA
//
