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Database: UniProt
Entry: A0A011MU16_9PROT
LinkDB: A0A011MU16_9PROT
Original site: A0A011MU16_9PROT 
ID   A0A011MU16_9PROT        Unreviewed;       910 AA.
AC   A0A011MU16;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=kdpD {ECO:0000313|EMBL:EXI66036.1};
GN   ORFNames=AW08_02775 {ECO:0000313|EMBL:EXI66036.1};
OS   Candidatus Accumulibacter adjunctus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=1454001 {ECO:0000313|EMBL:EXI66036.1, ECO:0000313|Proteomes:UP000020218};
RN   [1] {ECO:0000313|EMBL:EXI66036.1, ECO:0000313|Proteomes:UP000020218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK-12 {ECO:0000313|Proteomes:UP000020218};
RA   Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT   "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT   clades.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXI66036.1}.
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DR   EMBL; JFAX01000017; EXI66036.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A011MU16; -.
DR   STRING; 1454001.AW08_02775; -.
DR   PATRIC; fig|1454001.3.peg.2827; -.
DR   Proteomes; UP000020218; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd01987; USP_OKCHK; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; IPR038318; KdpD_sf.
DR   InterPro; IPR025201; KdpD_TM.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR   PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR   PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR   Pfam; PF13493; DUF4118; 1.
DR   Pfam; PF13492; GAF_3; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF02702; KdpD; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020218};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EXI66036.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        410..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        442..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        488..507
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          682..897
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   910 AA;  99826 MW;  98E05FB154BFCA47 CRC64;
     MAPQLGREMK DGRPDPDLIL DRIKEEEMRA ARGKLKIFFG ASAGVGKTYA MLSAARQQAE
     QGTDVVIGVV ETHGRKETEA LLTGLERLPL QAVAYRDRVL PEFDIDGALA RKPALLLVDE
     LAHSNVPGSR HAKRWQDVEE LQSSGIDVYS TVNVQHLETL NDVVGGITGI RVWETVPDHV
     FDAADEVVLV DLTPDELLQR LKEGKVYLPQ QAERAIQNFF RKGNLIALRE LALRRTADRV
     DSEMIQYRRD RSVTRAWHTS ESLLACIGPG DGSDRIIRSA ARIATKLDVP WHVIYVETPK
     LRHLSDQRRL QILKSLKLAQ EMGAETASLP GSDAMATIID YARDHNLSKL LVGRDRAQAW
     RPWKRSFADR VGKLAPDLDI IQVARVDTPA DRRQEESTGE SLLDRLHAPW QSFAMSSVFC
     ALVTLIAMPL HTVFDRANIA MLFLMAVVLS AVRYGLGPAV AAAFLNVAAF DFFFVPPRFS
     FAVGDVQYLM TFAVMLAVGL VTAKLTADLK FQARVASRRE QRVRALYEMS RDLSGALMPE
     QIAEISQRFA ATGFGARAAI MLADERDRLH EAIPVPGGVP AVDVGISQWA FDHSAEAGWG
     TDTLAGSPLL YVPLKAPMRT RGVLVLEPKH SRRLLAPEQR RLLDTFARLV AISLERVHYV
     DVARATTVQM ESERLRNSLL SAISHDLRTP LAALVGLADS MSMTQPPPTG EQCDIAASMR
     DEALRMNSLV NNLLDMARLQ AGAVKLNRQW QPLEEVVGSA IKAMRSTMAG HRLGVNLPDG
     LPLLEFDAVL VERVLCNLLE NAVTYTPAGS LIEIGAAPGA RDQVDIWVED DGPGLPAGKE
     ELIFSKFERG QKESAASGVG LGLAICRAIV TAHGGTIRAE NRRGGGARFV FSLPRGQPPS
     LAGAEEDSPQ
//
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