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Database: UniProt
Entry: A0A1P8WDU7_9PLAN
LinkDB: A0A1P8WDU7_9PLAN
Original site: A0A1P8WDU7_9PLAN 
ID   A0A1P8WDU7_9PLAN        Unreviewed;      1050 AA.
AC   A0A1P8WDU7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=cph_6 {ECO:0000313|EMBL:APZ92230.1};
GN   ORFNames=Fuma_01840 {ECO:0000313|EMBL:APZ92230.1};
OS   Fuerstiella marisgermanici.
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Fuerstiella.
OX   NCBI_TaxID=1891926 {ECO:0000313|EMBL:APZ92230.1, ECO:0000313|Proteomes:UP000187735};
RN   [1] {ECO:0000313|EMBL:APZ92230.1, ECO:0000313|Proteomes:UP000187735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NH11 {ECO:0000313|EMBL:APZ92230.1,
RC   ECO:0000313|Proteomes:UP000187735};
RX   PubMed=28066393; DOI=10.3389/fmicb.2016.02079;
RA   Kohn T., Heuer A., Jogler M., Vollmers J., Boedeker C., Bunk B., Rast P.,
RA   Borchert D., Glockner I., Freese H.M., Klenk H.P., Overmann J.,
RA   Kaster A.K., Rohde M., Wiegand S., Jogler C.;
RT   "Fuerstia marisgermanicae gen. nov., sp. nov., an Unusual Member of the
RT   Phylum Planctomycetes from the German Wadden Sea.";
RL   Front. Microbiol. 7:2079-2079(2016).
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};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP017641; APZ92230.1; -; Genomic_DNA.
DR   RefSeq; WP_077023884.1; NZ_CP017641.1.
DR   AlphaFoldDB; A0A1P8WDU7; -.
DR   STRING; 1891926.Fuma_01840; -.
DR   KEGG; fmr:Fuma_01840; -.
DR   OrthoDB; 231918at2; -.
DR   Proteomes; UP000187735; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; 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; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 4.
DR   Gene3D; 1.10.287.130; -; 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; 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; IPR007895; MASE1.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 4.
DR   PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF05231; MASE1; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF08447; PAS_3; 2.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 4.
DR   SMART; SM00091; PAS; 4.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
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; 3.
DR   PROSITE; PS50112; PAS; 2.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187735};
KW   Transferase {ECO:0000313|EMBL:APZ92230.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        30..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        55..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        78..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        134..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        181..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        245..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        295..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          332..366
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          392..446
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          643..695
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          689..766
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          769..821
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          832..1046
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   1050 AA;  118947 MW;  4EF751109B4D1EB0 CRC64;
     MFSLRFIHNQ PQKTNVSATD VPPLSTRSRW ALFCCVSLGY LIAAEIGHAM SFSGYFATFW
     LPAGLAVATY LAVRPRYWAI LLFATLTANI ASDVGLHDKH LFVSLGFWVA NTTEAMIAVA
     LIRRFDSASK ILQTVRSALT FVLLVCVLST AAGATLGAAV VWKAFDASYA NTWRIWWSAD
     YVGMLVTFPF VWIAIDAYAH WKQRRRRFAV LTGPLEKGIY VGLLIALAAA SHYVFGIQLQ
     RMAYIVFPIL LWLVMRFEVV GAASGLFVLA LIAVADTAGG KGFFGGIEAL PERAFALQSY
     LFVSATTFLT LAATVRERQE AEHRLRMSQF TIEKASNAQF WIRENGSFAY ANELASRYLG
     YSREELCQMS MADVNPDFPD DAWASHWNVT KHQGELRLES TYRRRNGTTF DCELQTVLVD
     FGGEEVIVAS VQDISARKAA ERDLYRSQTA LHTAADAVLW VKPDGHIFYV NDEACIRLMY
     SREDLLKLTV ADINPDLQSV EKFRAEIWPR IHQDKRLMLT MRHERRDGTI FPVEIVIHHI
     EFEGEEFACS FVRDITARVA AEKELDEARA RLELAISGGN VGLWDWDVLS GEVHFSDHWH
     SQLGESPGTL KTFNDWEVRL HPDDADEARA VAQDALVKRK PDYQSTFRLK HKDGSYRWIL
     SRGRLSFDSD GKPNRMVGTH VDVTELQETR AKLEALIELM GVTDGAWNWD LLTDSVDYST
     RFRELLGYAP DDFDGFPNEL DSFKQRIHPD DSDSFWDQIQ QHQKNGQPMD LEVRMRRKDG
     VYRWFRARGA MLRDDDRKQF RMAGSIYDVT HRKNVELQLL ESNSDLEQFA YVASHDLQEP
     LRAVGGFCQL LQRRYSDSLD ETARGYIAKA VEGASRMTTL IEDLLEFSRV GNDKRPLKVI
     CVKDVVAAAM EQMQLPIEES GAQITVEDLP MVAGDAQLLA QLFQNLISNA IKFRQQNIPP
     RIRIFATRTE SFWDVSVEDN GIGIRADHIK QTFTIFKRLH RREEIPGTGI GLAICKRIAE
     RHNGSISVSS TPGKGSVFTL RLAAEEQRYA
//
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