ID A4Y0E2_PSEMY Unreviewed; 1291 AA.
AC A4Y0E2;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Pmen_4311 {ECO:0000313|EMBL:ABP87058.1};
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739 {ECO:0000313|EMBL:ABP87058.1};
RN [1] {ECO:0000313|EMBL:ABP87058.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ymp {ECO:0000313|EMBL:ABP87058.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; CP000680; ABP87058.1; -; Genomic_DNA.
DR STRING; 399739.Pmen_4311; -.
DR KEGG; pmy:Pmen_4311; -.
DR PATRIC; fig|399739.8.peg.4363; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_263411_0_0_6; -.
DR OrthoDB; 8573350at2; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 4.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
DR InterPro; IPR029150; dCache_3.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR43771:SF2; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
DR Pfam; PF14827; dCache_3; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF08447; PAS_3; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 4.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 4.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ABP87058.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:ABP87058.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 541..588
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 630..682
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 683..743
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 760..812
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 813..883
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 887..939
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 940..1010
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1017..1067
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1071..1289
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1291 AA; 144794 MW; EB5DD01FC1D8ECAC CRC64;
MTPRLSHRWF GQWLFSRWDA GRRDAGRWIV IGGSLCLALF FAFLGRQALN EREALWQLQM
GKQADIQRMA LNSTQHGLQE RTQLLAETIA ADAWVTELVR QAHALPASDL EGLASIRSQL
YTRLAPRWRN LQAHQPFRLY VHLAPDIKVL LRVHEPEHFG DLQIGWRPMV QEALRSASSQ
AGLGLTRGSI GMRAIAPLLA EGKHGAEQVG AIEVAMGVLE NLAQLDREFN SGVALLLRED
LLLGSGSGEE LRGLASDAQR WQLMDYSRQQ VLAWQEQRRL PAPEEGDSVR LLDHGERHYL
VNQVALSSYR QAHQRSDEPL AVALIWHDIS DQYNVHRRDK RWLVIKWLLA WCGAEALLLG
LLRSTQRSTQ RLMQRQQAAL RALNEIAALP SLSRTEQLRQ ALRLGAEHFG MPLGIISRIE
GERYQVVVQV SPDGALSDGQ QFELGDTYCS LALQQDEALA ITHMADSPHR RHPCYRQFAL
ESYIGTAVRV AGKPFGTLAF ANPEPRRRPF DAADRDFLGL FARWVGAILE RQQQERAVRA
ARAYLQAVLD SATGVSIIAT DTSGTISLFN SGAERLLGYG AAEMIGRQTP AIIHLEEEVQ
ARAAELSEAS GHAVEGFEVF VHNARGGEPE TRQWTYRHKD GGLRQVNLTV SAIFDENGQI
TGFLGIASDI SELLQTTRAL QKSESRFRGL VANLPGVVYR CANDSQWSMR YVSDEIRNLC
GYPASDFIDN RVRSFSSIVH PDDLAITFRA GEAIERQESF ELTYRLRHAD GHNVWVREKG
RGEYDGQGHL LWVDGFIWDI SERQAMEDEL RLSQQRFLNA FNTAPQGMAL VGPDGRWLEA
NDELCRMLGY SREELLACTY QQVTHPDDLD ADRQNMEDLL AGRINAYQME KRYLDKQGRI
LWVLLSVSLV RDSEGRPVHF VSQIQDFSDR VAAERAVRER EHYLSTLLDN VLDAIVTIDE
QGRIETFNHA AEAIFGYRQS EVAGHNVRLL MPEPYRSAHD GYIQRYLRTG EAWVIGQARE
LEGMRQNGER FAMELAVSQI SHQGQRRFIA VIRDIAERKR IELMKNEFVS TVSHELRTPL
TAIAGSLGLI NGGALGAVPD NMRQMLAIAH SNSQRLSALI NDLLDMDKLV AGKMHFDLQA
RTLQPLLEQA LLHNQPYAEQ HQVELRLQVE DDAQVRVDAQ RLAQVMANLL SNAAKFSPPG
TCVDVRLQHG GEVLRVSVTD SGPGIPEAFK PRIFSKFSQA DSGDTRQQGG TGLGLAICKE
IIERMGGHIG FDSSPGQGAT FWFELPITGS A
//
