ID D3PAS4_DEFDS Unreviewed; 912 AA.
AC D3PAS4;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-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 OrderedLocusNames=DEFDS_0186 {ECO:0000313|EMBL:BAI79697.1};
OS Deferribacter desulfuricans (strain DSM 14783 / JCM 11476 / NBRC 101012 /
OS SSM1).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Deferribacteraceae; Deferribacter.
OX NCBI_TaxID=639282 {ECO:0000313|EMBL:BAI79697.1, ECO:0000313|Proteomes:UP000001520};
RN [1] {ECO:0000313|EMBL:BAI79697.1, ECO:0000313|Proteomes:UP000001520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14783 / JCM 11476 / NBRC 101012 / SSM1
RC {ECO:0000313|Proteomes:UP000001520};
RX PubMed=20189949; DOI=10.1093/dnares/dsq005;
RA Takaki Y., Shimamura S., Nakagawa S., Fukuhara Y., Horikawa H., Ankai A.,
RA Harada T., Hosoyama A., Oguchi A., Fukui S., Fujita N., Takami H.,
RA Takai K.;
RT "Bacterial lifestyle in a deep-sea hydrothermal vent chimney revealed by
RT the genome sequence of the thermophilic bacterium Deferribacter
RT desulfuricans SSM1.";
RL DNA Res. 17:123-137(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};
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DR EMBL; AP011529; BAI79697.1; -; Genomic_DNA.
DR RefSeq; WP_013006945.1; NC_013939.1.
DR AlphaFoldDB; D3PAS4; -.
DR STRING; 639282.DEFDS_0186; -.
DR KEGG; ddf:DEFDS_0186; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_318786_0_0_0; -.
DR OrthoDB; 9813024at2; -.
DR Proteomes; UP000001520; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000001520};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 232..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 558..770
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 790..905
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 839
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 912 AA; 105287 MW; 77FC9246FB45BC70 CRC64;
MKKSEHFSTF LFKRFSLIAL IFIIFFIAYI LFILKSDYNK FIKDYFADSI SKIETITKTK
FVSEHKNLEN IAEIYLKEPN SLDINLFKYQ LYKLKKLRHF FIIKKDEVIF NFSKVRILSP
EEILKFNKNE ISLEKGILSY ILVTKLDDSK IISIFNINQL LFDLEKEIES DIYLYSKNNI
LLTFYTPEII PFNKSNVDKI VSHKNFYFYT QYLPDFNVFI VLKKNKSYFT PYIYNNLKFA
IAIILALIVI IILISNTLKK YLLAPLNKFS NSIKDIEEGK SIKEITYTKI IEFNDFLKKY
YAKLASLKES EQNLLKILNT LEMGIYIVDK DYNLKFINEA EKHFINADNE VIDKKCYQIF
ANRNTPCEGC NYISKIEATS NDFINIAKLR NNNDLRKYAV IKSYKISDNF LIAIHDYTVT
MQLNKKIQYE KEKLETVINN VKEGIALINF DGSIDLANQA FYNITCFDNN TNVINELILE
SNGEKYNLLN LQDLSNRYYF TNNKNQTYIL NIFKAPLFFN TKGEGFLIVL YNITDEVHRE
MEELRKNKLE SIGLLAGGIA HDFNNILASI KNYISLVKLS GADSIDVIYK IDEIVDQGKN
ISNKLFTLSS GDIIKNDIIN LKDVINTAKE LSLAGSNITL DINSKINDVY IKGDETQIFQ
VFQNLFINAK EAMKNKGKIT LSIETKYISK NLMGLTKGDY ALIRVKDNGP GIEEGIIDKI
FDPYFSTKER GSGLGLFITY NIIKNHNGHI SIKSIKGEGT EFIIYLPLAR KQDEKAQNEN
IMHLGRIRKR ILVVDDDFYI RDSMNLLMKS IGCSVKSVAT GEEAIEMLKT EKFDIIFADV
TIKGGMGARD LIKYLIKNKI DVKTVVMSGY SEDDLLSNYQ IYGFAAALKK PINIDDIYAI
LEKLSDEEKN EL
//
