ID E6WWY8_PSEUU Unreviewed; 1148 AA.
AC E6WWY8;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Psesu_2862 {ECO:0000313|EMBL:ADV28687.1};
OS Pseudoxanthomonas suwonensis (strain 11-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=743721 {ECO:0000313|EMBL:ADV28687.1, ECO:0000313|Proteomes:UP000008632};
RN [1] {ECO:0000313|EMBL:ADV28687.1, ECO:0000313|Proteomes:UP000008632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11-1 {ECO:0000313|Proteomes:UP000008632};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Ovchinnikova G., Siebers A.K., Allgaier M., Thelen M.P.,
RA Hugenholtz P., Gladden J., Woyke T.;
RT "Complete sequence of Pseudoxanthomonas suwonensis 11-1.";
RL Submitted (JAN-2011) 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; CP002446; ADV28687.1; -; Genomic_DNA.
DR RefSeq; WP_013536512.1; NC_014924.1.
DR AlphaFoldDB; E6WWY8; -.
DR STRING; 743721.Psesu_2862; -.
DR KEGG; psu:Psesu_2862; -.
DR eggNOG; COG0591; Bacteria.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_22_0_6; -.
DR OrthoDB; 9764438at2; -.
DR Proteomes; UP000008632; Chromosome.
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 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; 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; 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:UP000008632};
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..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..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 154..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 368..395
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 407..428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 435..456
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 637..674
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 792..1006
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1028..1142
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 751..785
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1077
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1148 AA; 125955 MW; 11A83A19C7499AF7 CRC64;
MVSSWILLLV SVGYAALLFT VAWWGDRRPM YPNRPWLRPV VYSLALAVYC SSWTFYGAVG
SAVRNGIGYL PIYLGPILLM LFGWRIIERL ALIARSQNVV SIADFMSARY GRSRRLAALV
AVIALVGIIP YVALQYKAVA MSLAVLSGQH VEQAAVATDP ALYVALLMAL FAALFGTRQV
DATEHHHGMM LAISLESLVK LVALIAVGVF AWAWLRGNEM RVTGAAREMF LHAPPMGFVA
QTLLSFLAIV CLPRQFQVAV VECGDVGDIR RSRWMFGGYL MIVTLMVIPI ATAGLSLFGG
DPRVASDTFV LALPLAEGNS ALALAAYVGG FSAATGMVIV ASIALATMVS NDLVMPVLLR
GGWGERHAAA DVASLVLWVR RLAILMLSLC AYAYYRWIGG DTALAAYGVM AFAAVAQFAP
GLIGGLYWRG ASRRGVEFGL VVGFATWIYT LLLPALSRSG LFDGGWMETG PFDLYWLRPQ
QLFGLSGWDA LTHGTFWSLL LNAGVMMVVS ARWRPSVDER LRIAPFLDPY AERQTLSRSE
WSGNVSVGDL LSLAKRIVGE RHARRAFAEQ AHDLGGELQP TSAADRAWIQ FTERLLAASI
GAASARLVLT SVLRGSGMHL DEVMALLDEA GQELRFNREI LSTTLENISA GVSVVDPEMR
LVAWNRRYQQ MFGYPAGMLY VGRPVADLIR YNAERGELGE GSIEQHVRKR IEHMRAGTPH
VFERVRADGT VVEMRGQALP GGGYVTSYND ITAYKHAEQA LREANENLEQ RVAERTREAE
EAQQSRTRFL AAISHDVLQP LNAARLFASA LREGGQDAAE QRHLAERVDA SLRAAEELLD
GLLDVSRLDT GALQAEISTF DAGELLRELA AQYAPVAAGR SLDLRVHARH CPVRSDRRLL
RRVLQNFLAN ALRYTRQGRI VLGMRVHDQT VYLQVWDTGP GIPPQHMRQI YEEFQRYQQP
FDWGERGLGL GLSICQRISR LLDHGLDARS KVGRGSMFSI AVPRSAQPAT TPAPAIMLPG
DNTLAGLRVL CLDNDREILD GMRLLLARWQ AVAIPAATVD EALERMADSA PQAMLVDYHL
HDRLDGLDAL DALRAAGGAI PGALLTADGR DELKRQARMR GYRLLTKPVK PASLRAWLAA
QVPAPARV
//
