ID I4N3E9_9PSED Unreviewed; 1200 AA.
AC I4N3E9;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PMM47T1_13555 {ECO:0000313|EMBL:EIK95989.1};
OS Pseudomonas sp. M47T1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1179778 {ECO:0000313|EMBL:EIK95989.1, ECO:0000313|Proteomes:UP000004339};
RN [1] {ECO:0000313|EMBL:EIK95989.1, ECO:0000313|Proteomes:UP000004339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M47T1 {ECO:0000313|EMBL:EIK95989.1,
RC ECO:0000313|Proteomes:UP000004339};
RX PubMed=22887683; DOI=10.1128/JB.01116-12;
RA Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT "Draft Genome Sequence of Pseudomonas sp. Strain M47T1, Carried by
RT Bursaphelenchus xylophilus Isolated from Pinus pinaster.";
RL J. Bacteriol. 194:4789-4790(2012).
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 -!- 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:EIK95989.1}.
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DR EMBL; AJWX01000011; EIK95989.1; -; Genomic_DNA.
DR AlphaFoldDB; I4N3E9; -.
DR STRING; 1179778.PMM47T1_13555; -.
DR PATRIC; fig|1179778.3.peg.2727; -.
DR eggNOG; COG0834; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR OrthoDB; 9797243at2; -.
DR Proteomes; UP000004339; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd13705; PBP2_BvgS_D1; 1.
DR CDD; cd13707; PBP2_BvgS_D2; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4.
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; IPR036641; HPT_dom_sf.
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; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00497; SBP_bac_3; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00062; PBPb; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 2.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022519};
KW Kinase {ECO:0000313|EMBL:EIK95989.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022519};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000004339};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:EIK95989.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1200
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003695552"
FT DOMAIN 572..644
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 646..699
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 717..938
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 958..1077
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1104..1197
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 1007
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1143
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1200 AA; 131726 MW; 3A0A91695B84861B CRC64;
MRARMFCWLW LFLAPWALAE ETGPTLYGRS NLAVGLLDLE LTDDDRRWLW QCRVLRLGVS
LPEYAPFDIL GTGQEYEGIT ADYAALVAGL LHLSVRVVRY PTRAEALAAV RDGDIDLLGT
SNVFEAATAN LVLSQAYAQD ESVLATRRDD HTALLGGLRD RRLAMQEFYL PRALVEGLYP
EARLQLYPST LTALGAVAFG QADVFLGNAL GAYYQIYKGQ LGGLHLNHFE QVQSNYFGFA
VSAHNSRLLT LLNTALQAIP EHERLAILGR WSVGGVSIGQ RRELQLTEAE QRWLNQARPL
KVLMDEQFVP LSYRDDQGRY RGVSAQVLEV IGQMTGLTFE VASGLTLAQM TEQVQRGEAD
LIAALPQSRA REEQLGFTRA YLSSPRVLVT RDEPKAPYSL EQLEGKRLAL VHGSFLLDQV
LSQYPGIVHV PARSADHALS LVTDGKADAA VLTLIGARYR ISRQYAGLLR VSATLPVRAA
SLAFATSRNS PELLSILNKA LLAIPPQEIN DLAARWRGEV VLEEGFWMRH RWHIAQAVLM
GLLVWGLLVG WLTQLRRQVK RRNIAEQALT NQLEFMRVMI DGTPHPLYVR DRDGCLLTCN
TSYLDELQLT HDEVVGKPVA DTAAFTVEQA ESYQQAYLQA MEAGVKVVED RDVMFRNGES
KTICHWVLPY RGTDGEIAGL IGGWIDITDR QRLLQAYQHA KEAAEAANRA KTVFLATMSH
EIRTPMNAIT GMLELALKKS AQGRLDHLSI EVAASAATGL LALIGDILDI TRIETGQLNL
VPQPTDLMLL VEAVVRLFQV QARHKRVRLT LQVHGELDRA VMLDPLRFKQ VISNLVSNAV
KFTQEGTVVV AVYLTPTADG VGARLDIIDT GVGIPPDELA KLGDAFAQAS NNQQSPREGC
GLGLNISRTL CAMMGGQMRL HSVLGKGTRV TVELALRWAE GNAPAPVRDV TPASRVLNIL
VVDDYRANRI LLQQQLAYLG HRVTLADDGQ AGLVCWLRGG FDLVMSDCNM PGLDGYQLAH
AIRVHERRSQ SPPCRVLGFT ANAVPEERAR CLAAGMDGCL FKPLSLTDLA VALQPAGSEP
AVKAAGAMGE GIDLGALEEL TAGDSTALKA LLDDLAECCR EDLHSLSTLD RERDRKALSD
LAHRIKGGAR IIQATQLLDA CEQLEQACAK GQQPPSSTVI EHLHGALSDL TARLERHCRG
//
