ID E4T6G3_PALPW Unreviewed; 1368 AA.
AC E4T6G3;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Multi-sensor signal transduction histidine kinase {ECO:0000313|EMBL:ADQ80307.1};
GN OrderedLocusNames=Palpr_2171 {ECO:0000313|EMBL:ADQ80307.1};
OS Paludibacter propionicigenes (strain DSM 17365 / JCM 13257 / WB4).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Paludibacteraceae;
OC Paludibacter.
OX NCBI_TaxID=694427 {ECO:0000313|EMBL:ADQ80307.1, ECO:0000313|Proteomes:UP000008718};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WB4;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Ivanova N., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Paludibacter propionicigenes DSM 17365.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADQ80307.1, ECO:0000313|Proteomes:UP000008718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17365 / JCM 13257 / WB4
RC {ECO:0000313|Proteomes:UP000008718};
RX PubMed=21475585; DOI=10.4056/sigs.1503846;
RA Gronow S., Munk C., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brambilla E., Rohde M., Goker M., Detter J.C., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Paludibacter propionicigenes type strain
RT (WB4).";
RL Stand. Genomic Sci. 4:36-44(2011).
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DR EMBL; CP002345; ADQ80307.1; -; Genomic_DNA.
DR RefSeq; WP_013445676.1; NC_014734.1.
DR STRING; 694427.Palpr_2171; -.
DR GeneID; 78492561; -.
DR KEGG; ppn:Palpr_2171; -.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG3706; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR eggNOG; COG4585; Bacteria.
DR HOGENOM; CLU_267832_0_0_10; -.
DR OrthoDB; 1109395at2; -.
DR Proteomes; UP000008718; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR CDD; cd00130; PAS; 3.
DR Gene3D; 1.20.5.1930; -; 1.
DR Gene3D; 3.30.450.40; -; 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; 6.
DR InterPro; IPR011006; CheY-like_superfamily.
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; 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; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 5.
DR PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR PANTHER; PTHR24421:SF10; SENSORY TRANSDUCTION HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07730; HisKA_3; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13426; PAS_9; 4.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 5.
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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 6.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 4.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ADQ80307.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000008718};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 7..126
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 184..255
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 258..310
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 311..381
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 384..435
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 436..509
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 511..563
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 744..788
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1080..1145
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1171..1368
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 1136..1163
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 58
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1368 AA; 155838 MW; 525BFECEFEE83457 CRC64;
MESDQIKILA IDDNLDNLII IQALVLESFP YARVIKALSG NEGLLLASKE DPDVILLDIV
MPDMDGFEVC RQLKENERLR DIPVVFVTAL KGDKESRIKG LEVGGEAFLA KPIDQSELIA
QIRAMLKIKI GNIQRRDENI RLAALVEART LELKKTHSAT LNLLEDLKNE NEARKKTEEA
LRASEELYRS VINASPDNIT VADLQGNILM VSPRGLELFG YKNSEEIIGK NIEQFLVSSE
VQRARNNVES MFRGVFKGPE EYQIYRRDKT ILNTEINAEF VRDADGNPSR LVFAIRDNTE
RKLAQEALRE SEEKFRDMAN LLPQVVFEMD VNGIITYVNE QAYTIFKYEN GTLIGKDSLD
LHIPAERKRA TGIVQKALLG KRVEDNEFRL VAKDGSIFSA LIYSNAIVKD GRNVGARGII
IDITEQKKAE ERLRESEEKF REMANMLPQI VFESDVHGNL TYVNKHGFTI CGYNEEEGLE
LLGTNGLDFI KYSDREVAQG VLRDRIAGKP IDSNLYYVKK KDETTFPALI YSNPIYKDNK
SVGLRGLIVD ITEQKQVEKK LNYVTRLYAF LSQINQEIIR SKNIDELFEI ICKLAVQFGQ
FRMCWVGIYD EATGMLNPIA SSGDDDRYLE SLKIYPMGEN GNGPTGTAFR EERMIFCNNI
ASDPMMSLWK EEALKRGYQS SFAAPIFRKG KAIGTMTLYA SEVNFFDDEE QKLLLEIRED
ISYAIDVIDS EEERKQAEEA LEKSRNELKT IYDYAPVMMC VVDEKRQIQF ANKAFSSLTG
VSEVDLIGDV VGGVVGCINS FESPKGCGHG SKCSECSLRM AMESTFITGE GHQNVEYQSV
FRINNVEKDV SLLGSTAIIN YGKSKSLLLC LHDITARKQA EDALHKSEML LRTFIENTPF
EIWARDINSV GILENKKLVD HFGSIIGKTP NTDPTIDESL RELWEYNNKR AFEGEMIDEE
YTFFWNNEEH VFQQIIFPIN INSKLIGIAG FNIDITDRKR IEKELIDQKQ FFEQMFMQSS
LSTQILDKEG WCERVNPKLT QLFGVEAKYM EGKVYNIFED VEILKKGINK KLERVFTKGK
TVEWEMFREI GSTESVPDSS TNENRKAWFS NWAYPIQDRD GETTHVIIQH TDITDRKKAQ
EALTESQEQL KKFAAHLQNV REEERILLAR EIHDELGQIL IAIKIDMGML KQNVLKGIDD
QHSAEVLEKF ESLSSLVDNT IHTARKIMTD LRPEVLDLLG FIDAVKQHLK AFQNRHKVQC
KFENTDNDLQ FSSQQAVALF RIIQEALNNV AKHAKATEVK VKLKQKDDSL ILEIIDNGVG
FDENQKKNHD SYGLIGMKER VFLLDGELAI ISGKNTGTTI KITMPYNK
//
