ID B1ZNI9_OPITP Unreviewed; 716 AA.
AC B1ZNI9;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Oter_1135 {ECO:0000313|EMBL:ACB74423.1};
OS Opitutus terrae (strain DSM 11246 / JCM 15787 / PB90-1).
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae; Opitutus.
OX NCBI_TaxID=452637 {ECO:0000313|EMBL:ACB74423.1, ECO:0000313|Proteomes:UP000007013};
RN [1] {ECO:0000313|EMBL:ACB74423.1, ECO:0000313|Proteomes:UP000007013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11246 / JCM 15787 / PB90-1
RC {ECO:0000313|Proteomes:UP000007013};
RX PubMed=21398538; DOI=10.1128/JB.00228-11;
RA van Passel M.W., Kant R., Palva A., Copeland A., Lucas S., Lapidus A.,
RA Glavina del Rio T., Pitluck S., Goltsman E., Clum A., Sun H., Schmutz J.,
RA Larimer F.W., Land M.L., Hauser L., Kyrpides N., Mikhailova N.,
RA Richardson P.P., Janssen P.H., de Vos W.M., Smidt H.;
RT "Genome sequence of the verrucomicrobium Opitutus terrae PB90-1, an
RT abundant inhabitant of rice paddy soil ecosystems.";
RL J. Bacteriol. 193:2367-2368(2011).
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; CP001032; ACB74423.1; -; Genomic_DNA.
DR RefSeq; WP_012373961.1; NC_010571.1.
DR AlphaFoldDB; B1ZNI9; -.
DR STRING; 452637.Oter_1135; -.
DR KEGG; ote:Oter_1135; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG3437; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_114_15_0; -.
DR OrthoDB; 9760752at2; -.
DR Proteomes; UP000007013; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
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; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ACB74423.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000007013};
KW Transferase {ECO:0000313|EMBL:ACB74423.1}.
FT DOMAIN 19..136
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 201..271
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 273..325
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 343..565
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 596..709
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 145..204
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 68
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 645
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 716 AA; 78522 MW; 115724FF659F2744 CRC64;
MASDPANSVA LPERTPPVNI LLVDDEPRNL DVLESLLHSA EYSLVRAQTA ERALMLLLEG
VFAVIVLDIN MPGMSGIELA GLIKQRRRTQ HIPIIFLTAY FQEDKDVLQG YGTGAVDYLT
KPVNPEILRS KIAVFVELFR KTQALAASNA ALEAEIRQRQ QAEESLRQAN DELEARVAAR
TAELVQLNQE LQQRERALRA SEAQVRFVTD YAPAFITQFD REHRFKFVNR TYARRFGLEP
QQVIGQHFVE IMGEEADQIM RPHFEAALAG ERVEFEAEIA YAGLGPRWVY VIHEPERAAS
GEIVGLLAVV TDITDRKLAE QEVARARDQA LIAAKAKDDF LARLSHELRT PLNPVLLLAS
EAAGDPTLPP EVRADFESIA QNVTLEARLI DDLLDLTAIT RGKLALALRP VRVHETLENA
LALVRQDLAQ KNLRLVRQFD APKDLVDGDD MRLKQIFWNV IKNAVKFTPP AGQITLCTRL
SPDGGRMAIT VTDTGIGMTA EECARIFTAF TQGDHALSGG GRYGGLGLGL AISRMLVQLH
AGSISATSLG RDLGATFTIE LPLSHAPMPV APPAGSATPF ARPGEPTPPP ETRALRVLLI
EDHQPTCRTL CELLTRRRYR VVTANTVADA YAAAARESFD FVISDVGLPD GNGCELMADL
RARYGLRGAA LTGYGRDEDV ARSHAAGFVT HLTKPVSVRA LDQALQQLVA SLEPAN
//