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Database: UniProt
Entry: A0A1A8XMZ1_9PROT
LinkDB: A0A1A8XMZ1_9PROT
Original site: A0A1A8XMZ1_9PROT 
ID   A0A1A8XMZ1_9PROT        Unreviewed;      1307 AA.
AC   A0A1A8XMZ1;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ACCAA_200075 {ECO:0000313|EMBL:SBT05313.1};
OS   Candidatus Accumulibacter aalborgensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=1860102 {ECO:0000313|EMBL:SBT05313.1, ECO:0000313|Proteomes:UP000199169};
RN   [1] {ECO:0000313|EMBL:SBT05313.1, ECO:0000313|Proteomes:UP000199169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3 {ECO:0000313|EMBL:SBT05313.1};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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};
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DR   EMBL; FLQX01000095; SBT05313.1; -; Genomic_DNA.
DR   STRING; 1860102.ACCAA_200075; -.
DR   Proteomes; UP000199169; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd18774; PDC2_HK_sensor; 1.
DR   CDD; cd00156; REC; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 3.
DR   Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
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; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 3.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 3.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 3.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SBT05313.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000199169};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SBT05313.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        341..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          363..415
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          681..900
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          925..1038
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1054..1169
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1192..1307
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          887..916
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          571..653
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         974
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1103
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1241
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1307 AA;  139813 MW;  AC82FAB619659777 CRC64;
     MKLGSKLILQ TVLPAVVAVS VLLGIVTLVT SNALQDAAER SLAAVAEARR EEVHSYLHRM
     QQDIVSMGSA PAVIEALGAF SAAFAACGSA ADSQLQQLYT RTGELSGNHR GACQSGYARA
     YGQHDAFFRQ RHVTYGWHDM LLVDRQGNVV YSLDKGSDFA TNLLSGPWRQ SGLARAASIA
     LHESVSGVPV FSDAERYPPA GNRAGMFLAI PLLEPGSGQP LGALAVRIAF EPLDKLTHFK
     AGLGESGEAF LVGTAGWLLT NTFFDKESSV LGRQLKTEAV RRVLAGDEGS DQLADYRGQQ
     SFIAWRPLQP FAGALGDQPR WGVIAKIGRD EALASLHSLQ WLMLASGLLI ALAAIVLGVV
     FTQRLFGPVL AMRDALTRLA NGERTSIPGG DRRDEIGEMA QAAEKFRELS EGVARDRWLR
     EHVAALTTAV SQETHLAGVA EIILALLRRQ LDIPVASFFL RDAGGDYRRA GAQGLARRSQ
     CVDRFAPGES LVGQCARDGQ PVVLSPVPGG LTLISTGLAE FPPEELVLYP IRHQDETLAV
     VELASTHRLS SDEHAFLAAL VGPLGLHLAN IDAAERNVAL LEESRAQAAI LEQQKAELGQ
     KNTEMQALTD EMRAQSIELK AQNEAFRTNQ EELRAQQEEL AHQNQTLEAQ GRQLDFSRQD
     AEARARELAQ SNRYKSQFLA NMSHELRTPL NSILILARHL AENTGGHLDG DEVESASVIH
     ESGNQLLSLI NDILDLSRIE AGKLEVRAED FPIADLLHYL RRLIEPLAEK KSIGFTIDAG
     ASDLGTMRSD RRLLTQVLTN LLSNAVKFTD HGAVRLTVRP VDDDICFEVV DSGIGIAGDQ
     IGHIFGAFQQ IDGGTARKYG GSGLGLAISR HLVELLGGAI EVDSTPGSGS RFSVRMPRVT
     PATGASGPRP APAAPPATTA LPQGLILVVE DDDRLLPIVV RLIETLGYPV RAVGSGEEAL
     AAIAAERPAG VLLDLGLPGV SGMEVLRRIR SAPATTDLPV TIMSGAADSG EAQTLGAAGY
     IRKPITRDAV QRAIRGMLDA APPLPSAPAT ARPRVLLVED DEAGSLAVRV LFKDTAIEFS
     VVKDGSAGLA ALQATRFDAV ILDLTLPDMS GFEWLERVAT ETPMHPPVIV YSACDLDDAG
     LLRLRTHAQA VIAKGRLNGQ TSQRLREEVL LALAAPAREP FAAPPAAARR GALLVVDDDV
     RSQSALSKVL RSRGFAVSVA TSGAQALEML AGGQFDALLT DIMMPEMDGF ELIRRLRSGA
     AQTMPIIAVT AKAMPADIDL CLAAGATDYL AKPVDIDQLL KLLDKCL
//
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