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Database: UniProt
Entry: D2Z7L8_9BACT
LinkDB: D2Z7L8_9BACT
Original site: D2Z7L8_9BACT 
ID   D2Z7L8_9BACT            Unreviewed;       531 AA.
AC   D2Z7L8;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=Dpep_1439 {ECO:0000313|EMBL:EFC91465.1};
OS   Dethiosulfovibrio peptidovorans DSM 11002.
OC   Bacteria; Synergistota; Synergistia; Synergistales;
OC   Dethiosulfovibrionaceae; Dethiosulfovibrio.
OX   NCBI_TaxID=469381 {ECO:0000313|EMBL:EFC91465.1, ECO:0000313|Proteomes:UP000006427};
RN   [1] {ECO:0000313|EMBL:EFC91465.1, ECO:0000313|Proteomes:UP000006427}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11002 {ECO:0000313|EMBL:EFC91465.1,
RC   ECO:0000313|Proteomes:UP000006427};
RX   PubMed=21304695;
RA   Labutti K., Mayilraj S., Clum A., Lucas S., Glavina Del Rio T., Nolan M.,
RA   Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Goodwin L., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Spring S., Goker M.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Permanent draft genome sequence of Dethiosulfovibrio peptidovorans type
RT   strain (SEBR 4207).";
RL   Stand. Genomic Sci. 3:85-92(2010).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFC91465.1}.
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DR   EMBL; ABTR02000001; EFC91465.1; -; Genomic_DNA.
DR   RefSeq; WP_005660881.1; NZ_ABTR02000001.1.
DR   AlphaFoldDB; D2Z7L8; -.
DR   STRING; 469381.Dpep_1439; -.
DR   PaxDb; 469381-Dpep_1439; -.
DR   eggNOG; COG3290; Bacteria.
DR   OrthoDB; 9792686at2; -.
DR   Proteomes; UP000006427; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma 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; cd00130; PAS; 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; 2.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR033463; sCache_3.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR016120; Sig_transdc_His_kin_SpoOB.
DR   InterPro; IPR039506; SPOB_a.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43547:SF10; SENSOR HISTIDINE KINASE DCUS; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF17203; sCache_3_2; 1.
DR   Pfam; PF14689; SPOB_a; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   SUPFAM; SSF103190; Sensory domain-like; 1.
DR   SUPFAM; SSF55890; Sporulation response regulatory protein Spo0B; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EFC91465.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006427};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        13..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        174..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          218..266
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          418..528
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   531 AA;  57758 MW;  5A8A42E0E2D1574F CRC64;
     MGNFFRLSLK GKVIGLVFCF FLMSSLVTGL VIRGTVIPMF ERSMAEDAMD IALSVAYIPG
     IIDNVGRPDG AEVIQPIADG VRKKTGTEFV VVIDTDGIRY SHKVPERIGK RVVGGDEGRA
     LLGEAYVSRA VGTLGPSLRA FAPIYRKGEL VGAVLVGILI DRVNAETWRL TTNVLMALAL
     GLVVGIVGAT VLADGVKLSM RGFEPEEIDR LLWEREAMLE SIKEGILAVD ETGKVTLVNG
     EARRLLGLPD SGVIGRQVDV VVPNSRLPQV LSSGVPEYDR EQVSENARIL TNRVPIVCQE
     RTVGAVASFR DMSEVTSMAE ELTGVRRYVD ALRVRNHEFL NKLQTISGLV QLGEHDRAVA
     FISETVQSTQ SVMSFIARRI KNPSVGGLIL GKMGRCRELG IEFRIDEDSY LGPPGRVDSN
     ALVAILGNLL ENGMNALMDV PRERRRIYLS LFDESGRIII SVKDTGPGIP ENLEEDIFER
     GFSTKGEGHG GYGLFNVKSL VEAYGGEINL ESREGVSTEF LVNLPNGGSR S
//
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