ID A0A3R8UNW2_9GAMM Unreviewed; 1146 AA.
AC A0A3R8UNW2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, 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=EGJ34_19200 {ECO:0000313|EMBL:RRU03782.1};
OS Stenotrophomonas sp. 278.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=2479851 {ECO:0000313|EMBL:RRU03782.1, ECO:0000313|Proteomes:UP000274083};
RN [1] {ECO:0000313|EMBL:RRU03782.1, ECO:0000313|Proteomes:UP000274083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=278 {ECO:0000313|EMBL:RRU03782.1,
RC ECO:0000313|Proteomes:UP000274083};
RA D'Souza A.W., Potter R.F., Wallace M., Shupe A., Patel S., Sun S., Gul D.,
RA Kwon J.H., Andleeb S., Burnham C.-A.D., Dantas G.;
RT "Transmission dynamics of multidrug resistant bacteria on intensive care
RT unit surfaces.";
RL Submitted (OCT-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:RRU03782.1}.
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DR EMBL; RHPP01000165; RRU03782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R8UNW2; -.
DR OrthoDB; 9764438at2; -.
DR Proteomes; UP000274083; 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; 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; 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; 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 Kinase {ECO:0000313|EMBL:RRU03782.1};
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:RRU03782.1};
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 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 188..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 234..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 405..426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 438..459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 634..671
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 789..1003
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 MOD_RES 1076
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1146 AA; 126264 MW; 12DD9684A338BBF8 CRC64;
MVSSWILLLV SVAYAALLFG VAWWGDRRPM YPDRPWLRPV VYSLALAVYC SSWTFYGAVG
TAVRNGIGYL PIYLGPLLML LFGWRIIERL ALIARSQNVV SIADFISSRF GRSRRLAALV
AGIALIGIVP YLALQYKAVA MSLEVLTGHH GPTGYFGDPA LYVALLMALF ATLFGTRQID
ATEHHHGMML AIAFESMVKL LAMVAVGLFA YLWLNDRGEA VMRSAHTLFT GLPPVGFISQ
TLLGFLAIIC LPRQFHVAVV ECADVGDVRR ARWMFGGYLI VISAMVIPIA TAGVTLFGSG
GTVADDSMVL ALPLAEGRRL LALVAYVGGF SAATGMVIVT SIALATMVSN DLVMPVLLRR
SGDHREAAEV ASKVLWIRRL AILALAFAAY SYYRGSSNDS TLASYGLMAF AAVAQFAPGL
IGGLYWRGAS RRGVEAGIVL GFCTWIYTLL LPALTHAGWM DPVWLSAGPL GIEWLQPQRL
FGMSGWDPLT HGTFWSLLVN VAVMVLGSVR WRPGVDERLR AAPFLDPYAE RPSVAGAWPG
HVHVADLLAL ASRVVGERHA RRAFFEQAQS MERDLQASAP ADRAWVQFTE RLLAASIGAA
SARLLLTSLL RGSGMDLGEV VAVLDEAGQE LRFNREILST TLENISAGVS VVDPEMRLTA
WNRRYQQMFG YPDGMLYVGR PVADLIRYNA ERGELGEGDI ELQINRRIGY MRAGSPHIFE
RTRSDGKVIE MRGQALPGGG YVTSYNDITD YKHAEKALLE ANETLEQRVA ERSHEAEVAQ
QSKTRFLAAI SHDVLQPLNA ARLFASALRD SHQNNEEQRH LAERVDASLR AAEELLDGLL
DVSRLEAGGL HPVVGEFDVS LLMRELAAQY SPVAAGRGLR LDLFARPAWV RSDRRLLRRV
LQNFLANALR YTRQGRIVMA VRHRGDSIEL QVWDTGPGIP EHHMQQIFDE FHRYQQPFDW
GEQGLGLGLS ICQRISRLLD HQLNARSRVG RGSMFSILLP RAPTPQLPAP APVSAERPVR
TDSLAGMRVL CVDNDQEILD GMRALLGRWQ VQVITASTVD QALDEVQAQP DVMLVDYHLH
DRLDGLDALV ALREKAGRDI PGALLTADGR DELKRMARER GYRLLTKPIK PASLRAFLTA
HSRLSG
//
