ID W0RS02_9BACT Unreviewed; 825 AA.
AC W0RS02;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=J421_5951 {ECO:0000313|EMBL:AHG93486.1};
OS Gemmatirosa kalamazoonensis.
OG Plasmid 2 {ECO:0000313|EMBL:AHG93486.1, ECO:0000313|Proteomes:UP000019151}.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatirosa.
OX NCBI_TaxID=861299 {ECO:0000313|EMBL:AHG93486.1, ECO:0000313|Proteomes:UP000019151};
RN [1] {ECO:0000313|EMBL:AHG93486.1, ECO:0000313|Proteomes:UP000019151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBS708 {ECO:0000313|EMBL:AHG93486.1,
RC ECO:0000313|Proteomes:UP000019151};
RC PLASMID=Plasmid 2 {ECO:0000313|Proteomes:UP000019151};
RX PubMed=24699952;
RA Debruyn J.M., Radosevich M., Wommack K.E., Polson S.W., Hauser L.J.,
RA Fawaz M.N., Korlach J., Tsai Y.C.;
RT "Genome Sequence and Methylome of Soil Bacterium Gemmatirosa
RT kalamazoonensis KBS708T, a Member of the Rarely Cultivated Gemmatimonadetes
RT Phylum.";
RL Genome Announc. 2:e00226-14(2014).
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; CP007130; AHG93486.1; -; Genomic_DNA.
DR AlphaFoldDB; W0RS02; -.
DR KEGG; gba:J421_5951; -.
DR PATRIC; fig|861299.3.peg.6002; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_114_15_0; -.
DR InParanoid; W0RS02; -.
DR Proteomes; UP000019151; Plasmid 2.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 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; 3.
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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
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; 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; 3.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 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; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
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; SSF47384; Homodimeric domain of signal transducing 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; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Plasmid {ECO:0000313|EMBL:AHG93486.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019151}.
FT DOMAIN 103..155
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 156..199
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 322..392
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 396..447
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 465..680
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 703..820
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 270..325
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 438..465
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 753
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 825 AA; 90912 MW; 0E6E3708162669F6 CRC64;
MVLPHTPPSA PTYDPPSDGR GAEQKLRERE QQMDLLEQIA GLGSWEIDLA TDGIRWSREL
RRIHGVDETT APRTHSEFMA MVHPDDRATI DAAMSELAAG EPVTVDFRIV RPDGEVRLLQ
ARGKLVPGPD GALTRVIGTS LDVTERRGTE LALRASEESY RAIFQGASDA MFLHDMTTGA
VLEVNEAACE LMGYSADELK TIGLEGLTDA DAGYTTERAW GYATRALAGE PQRFEWLSRH
KDGSPVWSEM TLRRVTIRGV DRILAMARGI NDRKAAEAAL RRAYEELERR VAERTAELAA
SNAALAEEIA ERKEAERALS EREEHFRRII ENTSDWVMIC DPTGALTYVG PSAERMLGYK
PEEVLGFRPP DMTHPDDAQK LVDALRWVAE HPGQVITVPA RVRHKDGSWR VFEYMGRTLA
PDSFAEGAIA FARDITERTQ AEEALARAKE EAERANRAKS EFLSRMSHEL RTPMNSILGF
GQLLARNELP PTQAKSVQHI LKAGRHLLSL INEVLEISRI EAGRERFSLE PVALGPVLGE
VLGLVRPLAQ QCGVELREGR WPDGAWAQAD RQRLAQVLLN LLSNAIKYNR RGGHVRIVAA
RDDGRWAVRV EDGGSGIPTD RVDQLFTPFA RLGAEQTEIE GTGLGLALSK RLCEAMGGGL
ALESTGPEGS VFRVDLAVAA DPMRTFDETG GHAVVQAPHR EATLLYVEDN LANLSLVETI
LLSRPGWRTI PALQGQLGVA LAREYVPDVV LLDLHLPDIP GDEVLRRLRA DPRTASIPVI
VVSADATPAS LERLRASGAD AYLTKPLDVD EFLRAVERFL PAVRP
//
