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Database: UniProt
Entry: A0A0S6W5B1_9BACT
LinkDB: A0A0S6W5B1_9BACT
Original site: A0A0S6W5B1_9BACT 
ID   A0A0S6W5B1_9BACT        Unreviewed;       713 AA.
AC   A0A0S6W5B1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=U14_04894 {ECO:0000313|EMBL:GAK53628.1};
OS   Candidatus Moduliflexus flocculans.
OC   Bacteria; Candidatus Moduliflexota; Candidatus Moduliflexia;
OC   Candidatus Moduliflexales; Candidatus Moduliflexaceae.
OX   NCBI_TaxID=1499966 {ECO:0000313|EMBL:GAK53628.1};
RN   [1] {ECO:0000313|EMBL:GAK53628.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Sekiguchi Y., Ohashi A., Parks D.H., Yamauchi T., Tyson G.W.,
RA   Hugenholtz P.;
RT   "First genomic representation of candidate bacterial phylum KSB3 points to
RT   enhanced environmental sensing as a trigger of wastewater bulking.";
RL   PeerJ 3:e740-e740(2015).
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; DF820459; GAK53628.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S6W5B1; -.
DR   STRING; 1499966.U14_04894; -.
DR   HOGENOM; CLU_000445_114_15_0; -.
DR   Proteomes; UP000030700; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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; 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; 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; 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; PF13188; PAS_8; 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   Kinase {ECO:0000313|EMBL:GAK53628.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000030700};
KW   Transferase {ECO:0000313|EMBL:GAK53628.1}.
FT   DOMAIN          8..125
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          144..187
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          200..250
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          268..483
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          507..623
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         57
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         556
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   713 AA;  80146 MW;  9C110B9E1F49F4CF CRC64;
     MNMDAPQKVL IVDDEPHLRA GYLRIATQAG YEVASASGVA DGWQRALEFR PDVALLDVAL
     GDGSGLDLCR KIKTNPEMSG TLVIMLSGTQ ITSEDQANGL DAGADGYLIK PIQPRELVAR
     IKALLRIKEV EIHLQRTLDE LRQSEARFQK VITYHADAIL VVDRQSRIRF ANPAAERLFS
     RHKDDLIKQE FGLPIGDADQ FAELEIHQPT GSKIMVEMRA VEIEWDGEAA YLASLRDISE
     RKKMEFALQR AKEAAEAANN AKTQFLAHMS HEIRTPLNGI LGYAQLLKRG GDLTDYQQHG
     LDVIQQSGEH LLTVINDILD LSRIEAGKLE LSPTNFHLSR SLLTLVEMIK IRAEQKGLSF
     IYENESGRAS LVYGDEKALR QVLLNLLGNA IKFTSDGHVA LRVRMAEDGR RIRFDVEDTG
     VGIPPEKIDF VFAPFERLHH GQEGTGLGLA ISRRLVEIMG DSLRVQSQIN LGTRFWFEID
     LPAIDERSNA PLRHVRRIIG CRGKTPVIGI VDDYADHRRL LKEMLLLCGV AVVEWANGRE
     TCEQIERQMP DLVFMDIVMA DMDGLETTRQ LRQRPSLSSL PIIALSASAF EETRQQSLMA
     GCQEFLSKPV IEEMLWETLQ QYLPTAWVFE DEPPDVEAVE LPSQAVSSDI PSREQLGRLY
     EFTQIGDILG AREEIRLLKL RHPECADFLK QLEAMAARFN LVGIRSHIEQ YAK
//
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