ID A1ASK1_PELPD Unreviewed; 683 AA.
AC A1ASK1;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-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=Ppro_2719 {ECO:0000313|EMBL:ABL00322.1};
OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC Desulfuromonadaceae; Pelobacter.
OX NCBI_TaxID=338966 {ECO:0000313|EMBL:ABL00322.1, ECO:0000313|Proteomes:UP000006732};
RN [1] {ECO:0000313|EMBL:ABL00322.1, ECO:0000313|Proteomes:UP000006732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1
RC {ECO:0000313|Proteomes:UP000006732};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL Submitted (OCT-2006) 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};
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DR EMBL; CP000482; ABL00322.1; -; Genomic_DNA.
DR RefSeq; WP_011736572.1; NC_008609.1.
DR AlphaFoldDB; A1ASK1; -.
DR STRING; 338966.Ppro_2719; -.
DR KEGG; ppd:Ppro_2719; -.
DR eggNOG; COG3829; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_39_7; -.
DR OrthoDB; 9779002at2; -.
DR Proteomes; UP000006732; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
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; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43065:SF50; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ABL00322.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006732};
KW Transferase {ECO:0000313|EMBL:ABL00322.1}.
FT DOMAIN 27..91
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 114..166
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 167..237
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 240..292
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 434..678
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 395..425
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 683 AA; 76219 MW; 4D9EA05A9DA1BC3C CRC64;
MTTTDEQSAP IIVPDRAGQS DARSAVTARF LGRIIQSIAA PLYVIDRSHA ILFWNSALAQ
LTGKSSFQMT GTKLHWSVFH TRQKQLLADL IIDGACPASD RAYPQVVRHA DGTLQTEGWY
DDVGGKRRYL LFEARPITDD GNTVVAAVET IQDITERKQA QEVMDGQRRF FQGILESIPN
PVSYKDLSHA YLGCNRAFSE FFGRSEEEII GKMISDVVAP EYAVGSTEAD RRVLESGSSY
KYETTLPRGD GQLRSVLVTK APFSLLNGEL GGTVGTFVDI TEQRFLDEQV KEAKREWEET
LDCLKDFVIL TDELHRVRRC NRLLCDMTGK GFDEVLNEDW RDLLPDAGFE ALSFNGVSGE
LVHAASKRYY GLNIYSMTET ENERVTGYVI SLNDMTELRA MNEELKRTAQ ELNEAQRAVY
QQEKLASIGQ LAAGVAHEIN NPMGFISSNL TTLGKYLDKL RAFETAMIGL MERDGNSETL
GELKELRRNM KIDYILGDIQ GLLEESHEGA ERVRRIVQDL KSFSRVDEAE CKPTCINDCL
TSTLNMVRNE IKYVAEVELD VAPDLPLLHC YPQQLNQVFM NLLVNAAHAI TERGVIGIRT
FRDGDDVVIQ VRDTGKGIAP EHLTRVFEPF FTTKEVGKGT GLGLSISYDI VKKHGGRIEV
ESAVGVGSTF TIHLPLGYLA ETV
//
