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Database: UniProt
Entry: D2Z2V9_9BACT
LinkDB: D2Z2V9_9BACT
Original site: D2Z2V9_9BACT 
ID   D2Z2V9_9BACT            Unreviewed;       905 AA.
AC   D2Z2V9;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=PAS/PAC sensor signal transduction histidine kinase {ECO:0000313|EMBL:EFC90177.1};
GN   ORFNames=Dpep_0145 {ECO:0000313|EMBL:EFC90177.1};
OS   Dethiosulfovibrio peptidovorans DSM 11002.
OC   Bacteria; Synergistota; Synergistia; Synergistales;
OC   Dethiosulfovibrionaceae; Dethiosulfovibrio.
OX   NCBI_TaxID=469381 {ECO:0000313|EMBL:EFC90177.1, ECO:0000313|Proteomes:UP000006427};
RN   [1] {ECO:0000313|EMBL:EFC90177.1, ECO:0000313|Proteomes:UP000006427}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11002 {ECO:0000313|EMBL:EFC90177.1,
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   -!- 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:EFC90177.1}.
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DR   EMBL; ABTR02000001; EFC90177.1; -; Genomic_DNA.
DR   RefSeq; WP_005658719.1; NZ_ABTR02000001.1.
DR   AlphaFoldDB; D2Z2V9; -.
DR   STRING; 469381.Dpep_0145; -.
DR   PaxDb; 469381-Dpep_0145; -.
DR   eggNOG; COG2202; Bacteria.
DR   eggNOG; COG4585; Bacteria.
DR   Proteomes; UP000006427; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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; 1.
DR   Gene3D; 1.20.5.1930; -; 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; 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   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR   PANTHER; PTHR24421:SF10; SENSORY TRANSDUCTION HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/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; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EFC90177.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006427};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        296..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          327..374
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          401..453
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          510..562
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          814..905
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   905 AA;  101025 MW;  31F84203D18CF43D CRC64;
     MKFSRMALSE WGAYMVGVIF CMVVYLGGMF FLDRSEVSKS REEGLLRRSE QLTLAARATS
     DRLNDMVRHF STVSRYVSSS FISSDFDRDS LREIQSLELI SFPQILDISV VTYDDDQWMY
     GSENRTIFEQ SLHWGKLFLS RYMERGRGNW IPPFSISPGL RMMGIVYPLR QGRIAYGAMV
     VTLDLDRLLG HVVYDLKMGG SSYILSPLGD VVLSSDTETV GHSVFGDLHG RKADLRLMTR
     DVLNRSSGES LEQLSGEGLR VLAWHSARIG GQKLVLVHVS PDPAHLNVVF HFRRRLPLTV
     FLGVTLVILS LLFVSSYRKV WGILTEGERR YAAVLEAQTD PLIRFRSDWT ITFVNQACCR
     FWGLSREKLI GSSLANRLKG TERLGLQSLL DGLDRGESRQ GEWTQSINSP DGSERWIRWS
     CVPVSGVGST GLEIQAVGRD ITSLYSLQRE LARRKDALNA ILEGAPVPIC MTGLNGEVKR
     FNRTGKILSA NDGALRRMAR RVVRQGYGIY GEELSFSDEK GNRRVFSVNV VPYKDENGGI
     KGTIVAGMEL TEVRNIARRL LEEREDRYRK ILNAIGDGVL LCRKGVDELF RVDLSNPVAS
     EMIGGDVRPP VGRSLGEIFS SPSLRQVETL LSCSRGPVGL TGDLRRPDGS SLPVEMSLTV
     FSEDNLPVLL IVMKDISERL EARAREKNYA RQLRKLIGRL DEVEQQERQR MAAYLHDVVG
     QNLASVKIRL GLAMRDASGS VREGLKQCVV LADQIISETR AMTFELGSPL LDELGFGPAL
     ERMCDVVRRD RGLAVSVKDD GSADLLDRRS RGLLYRSIRE LLINVAKHAE VSEAFVSLER
     DGKFVVATVL DEGRGYDPEN LDRSAADLSF GLLSIRERLA GMGGELICRS SPGKGTRATI
     KLPVR
//
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