ID A1ALX0_PELPD Unreviewed; 738 AA.
AC A1ALX0;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 112.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Ppro_0709 {ECO:0000313|EMBL:ABK98340.1};
OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC Desulfuromonadaceae; Pelobacter.
OX NCBI_TaxID=338966 {ECO:0000313|EMBL:ABK98340.1, ECO:0000313|Proteomes:UP000006732};
RN [1] {ECO:0000313|EMBL:ABK98340.1, 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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP000482; ABK98340.1; -; Genomic_DNA.
DR RefSeq; WP_011734652.1; NC_008609.1.
DR AlphaFoldDB; A1ALX0; -.
DR STRING; 338966.Ppro_0709; -.
DR KEGG; ppd:Ppro_0709; -.
DR eggNOG; COG5000; Bacteria.
DR HOGENOM; CLU_019564_0_1_7; -.
DR OMA; IAWGEVA; -.
DR OrthoDB; 9773941at2; -.
DR Proteomes; UP000006732; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 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 InterPro; IPR003660; HAMP_dom.
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; IPR017232; NtrY.
DR InterPro; IPR045671; NtrY-like_N.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF42; TWO-COMPONENT SENSOR PPRA; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF19312; NtrY_N; 1.
DR Pfam; PF00989; PAS; 1.
DR PIRSF; PIRSF037532; STHK_NtrY; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABK98340.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006732};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABK98340.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 49..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 301..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 325..377
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 396..466
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 527..738
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 738 AA; 83162 MW; 04624F1A21053937 CRC64;
MGYKLSINER KKRAREAIVI VVALLLILFL TSAEIRLTQL SADTSMGSNI MIFGIINVVV
LLVILLVYLV SRNVVKLLLE NRSNPVATRL RTKLVVSFVG LSLVPTLLLF FAAAGFINNT
VHNWFNTQVE TSLSESLEVA QTYYKNSASN TIYYGRQISA IIRSSKLLNQ ENLPKLEALI
RQKQKEYNLG VVEVYSAQQE ELVRATNPLV PRGEFTNPAS DDIVRALSGN ELTRINPVGK
ADLIRGIVPI YSTWNDRDVV GAVVVNYYVP YSLVNKMKEI TESYHEFRQL KIMKNPIRTG
YIVTLFLITV VIVFLAYWIA VYLANSMSKP VQELLEATRA VAEGNLDVQI ESASLDEIGM
LVTSFNRMTT DLRTKQQTLN AVNHELTKIN LELDQRRRYM EIVLRNVAAG VISIDREGCI
TTINKSAEKL LSISNGAVVG RNFRELLQDA HLDIVKDILR DLLLSKQDTI NRQIVLDVNG
NRLALHLHLN MLRDENGSFV GTVLVLDDLT QVMKVQRMAA WREVARRIAH EIKNPLTPIQ
LSAQRLRKRY LSRFSDDEKV FDECTEMIIK SVDDLKNLVN EFSNFARMPA IQPEPNDLND
IIREALTLYQ QAHRDVQFDF KPDSRLPFLK IDRSQIKRVV INLLENAVAA MDGQGTVRIV
SNYDAELRLA SFVVVDTGPG IPAEDKPRLF EPYFSTKKTG TGLGLAIVNS VVSDHNGFVR
IRDNDPHGAC FVVELPAA
//