ID L0DIJ9_SINAD Unreviewed; 1366 AA.
AC L0DIJ9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Sinac_4454 {ECO:0000313|EMBL:AGA28643.1};
OS Singulisphaera acidiphila (strain ATCC BAA-1392 / DSM 18658 / VKM B-2454 /
OS MOB10).
OC Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC Singulisphaera.
OX NCBI_TaxID=886293 {ECO:0000313|EMBL:AGA28643.1, ECO:0000313|Proteomes:UP000010798};
RN [1] {ECO:0000313|EMBL:AGA28643.1, ECO:0000313|Proteomes:UP000010798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1392 / DSM 18658 / VKM B-2454 / MOB10
RC {ECO:0000313|Proteomes:UP000010798};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Chertkov O.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Singulisphaera acidiphila DSM 18658.";
RL Submitted (FEB-2012) 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; CP003364; AGA28643.1; -; Genomic_DNA.
DR RefSeq; WP_015247759.1; NC_019892.1.
DR STRING; 886293.Sinac_4454; -.
DR KEGG; saci:Sinac_4454; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR eggNOG; COG3852; Bacteria.
DR HOGENOM; CLU_000445_114_15_0; -.
DR Proteomes; UP000010798; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 4.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF13185; GAF_2; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 4.
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 SUPFAM; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 4.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000010798};
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 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 41..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 131..204
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 209..261
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 262..315
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 340..390
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 558..631
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 636..688
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 855..925
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 928..981
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 999..1220
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1248..1362
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 972..999
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1297
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1366 AA; 148331 MW; ED9078B8BB8A661B CRC64;
MLRIPESTVL RYGAAVVGAV IATALRFALG PLVGDRYPFT IYFALVAFAA WYGGFGPSIL
ALCLGGFAGT VLFLPSGGLD IGGVEVRVGT LVFALVGLTI ALMGGAMRSA RQKAEESARE
ALHHLHAEHE LRERLDITLQ SIGDAVLATD AGGRVVSMNR VAEDLTGWTS AEALGRPLEE
VFRIVDEETG EPVESPVANA LRTGGIVGLT NSTALISRNG TIRPIDDSAA PIRDEEGAIQ
GAVLVFRDDT EQRVAARALR ESEARKAAIL EAAIDCIITM DQEGKVVEFN PAAEETFGYC
RADALGRELC DLIVPPSLRE AHRRGLAHYR ATGEAPILGK RIEVAAMRAD GTEFPVELAV
TRIATTGSAL FTAYLRDITE RKQAEAARAE RSRLAEFGRE IGLVITESAT HGEMLDRCVE
ATVRHLDGAF ARIWTADEAG TLLELRASAG IYTHLDGAHA RIPVGRFKIG TIARERRPHL
TNAVLGDPHV PNQDWVKREG MVAFAGFPLV VGERLVGVWA MFARHALSDE VFEAMAAVAN
GIAVGLDRKR AMEAVVRSEG WLATTLASIG DAVIATDGHG QVRFMNPIAE QLTGWTQGEA
SGRPMEEVFR ILNEQTRMPA EHPVARVIRE GVIVGLANHT VLIAREGAET PIEDSAAPIR
DDQGAVVGVV MVFRNVAEQR RSELLLTDQR KIFEQMARGA PLGDVLEALC EAVERQSAGC
VATVLLADDE GRCLHHAAGR RCPVGYASAI DPVLVGPANG SCGTAVYRGE QVIVADIAND
PLWVDYQDLA LDYGFRACWS TPIPSSEGNV LGTFALYFPA TQRPTPYDQE MVELLARTAG
VAIERQRADD RLRHSEDRYR TLIEVSPQVV WYAEADGSLT YCNTWFLELT GLSKAASQGS
GWMQAIHPDH RDRVREVWRT AAARSANYEV EIPFRRAADG TYRWHVAKGV PVKDQEGQVI
SWVGVATDID DRKRADEERR AAKEEAERAN RAKDQFLAVL SHELRTPLNP ILLAASSMLD
RPTPHEEIHP TLEMIRHNVN LQARLIDDLL DVMRIVQGKM PLHWGVADCH DVIRHALQVC
QSEVFGKTIG LTLDLAADRH HVNADSARLQ QVFWNLIKNA VKFSPDGGTL CLRTRNEGGE
QDRLIVEVSD TGIGVEPDVL PTIFDPFQQG ETSITRRFGG LGLGLAICRG VVEAHGGTIT
AESAGKSRGT TFQITLNALP SREVEEKGTP QGGHPVSELA TAPTSTLKIL VVEDEEATRR
LMARLLRSLG HNVATAGTIA EATEAAEAEV FDLIVSDIGL PDGSGLELMR RIVTHRGPVP
AIALTGYGME EDIVRSREAG FTAHMTKPID FTKLEAMIRQ VAPSGR
//
