ID A1ATC9_PELPD Unreviewed; 763 AA.
AC A1ATC9;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Ppro_3002 {ECO:0000313|EMBL:ABL00600.1};
OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC Desulfuromonadaceae; Pelobacter.
OX NCBI_TaxID=338966 {ECO:0000313|EMBL:ABL00600.1, ECO:0000313|Proteomes:UP000006732};
RN [1] {ECO:0000313|EMBL:ABL00600.1, 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; ABL00600.1; -; Genomic_DNA.
DR AlphaFoldDB; A1ATC9; -.
DR STRING; 338966.Ppro_3002; -.
DR KEGG; ppd:Ppro_3002; -.
DR eggNOG; COG3221; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_011260_2_0_7; -.
DR Proteomes; UP000006732; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
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; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF12974; Phosphonate-bd; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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; SSF53850; Periplasmic binding protein-like II; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ABL00600.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006732};
KW Transferase {ECO:0000313|EMBL:ABL00600.1}.
FT DOMAIN 524..749
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 362..403
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 763 AA; 84141 MW; 4D964BBE4628C6BB CRC64;
MAALCAGLPP RPGERPFLLL LLSPLLLGLT LSPLQAHEIY PAPTATSVAL PIRIGALANR
GREECIRRWK PTATYLEHHL GGSRFEIVPL DFGQVAQKVA SEEVQFIITN PVQYAQLEFS
GKAYRIAGFQ LPSLNGPQGV YGGVIFTRAD RKDIRTLSDL KGKKFSAVDS ESLGGWLCAR
RELHGARLKP ERDFANLRFA GTHDAVVRDV VSGTSDAGTI RSSQLETMAA QGKMDLRSIR
VIPPARPVRG YPFLLSTRLY PEWPFAVVSG TNDELSRRVA IALMTMRPDD PTALASGGSG
WTIPADYSAV HELLRELRLG PYRDMGRITL GQVITHYRTH LLAITVAASL IALFAFRSLL
LNRRLRASLA ELSQRTSELN ESRENLRNER DNLVAIFEAM QDDIYISDSN HTILYGNDAL
ARDFGDWRGR ICHDYLDDRT SPCLDCRLRE VQAGATVRRE QFFPKSGKTY DIIETPLRQS
GRTVKLTIFR DVTELRAMEA ERLAMERRLL HSQKLESLGI LAGGIAHDFN NLLTVIIGNL
DLVRRRLLPD SPTRGNIESA QAACQQAAKL IGQILDYTGK MPVIADSIDL NDLLRHNEAL
LRGSLPENVT LTISISDGIP RIRGDRSRIE QVVMNLLANG VEAVGDAPGS IAITTGVREC
DDSYLAQSRI EDKPPAGRFV YLEVADSGCG MTRETEVRLF EPFFTTKFMG RGLGLSAVQG
IVKMHGGAIL LENRQGRGSV FRVLFPANGP ADSPHPSSLR SGL
//
