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Database: UniProt
Entry: B1ZNI9_OPITP
LinkDB: B1ZNI9_OPITP
Original site: B1ZNI9_OPITP 
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
//
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