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Database: UniProt
Entry: A0A369C777_9GAMM
LinkDB: A0A369C777_9GAMM
Original site: A0A369C777_9GAMM 
ID   A0A369C777_9GAMM        Unreviewed;       544 AA.
AC   A0A369C777;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DFQ59_106104 {ECO:0000313|EMBL:RCX29872.1};
OS   Thioalbus denitrificans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalbus.
OX   NCBI_TaxID=547122 {ECO:0000313|EMBL:RCX29872.1, ECO:0000313|Proteomes:UP000252707};
RN   [1] {ECO:0000313|EMBL:RCX29872.1, ECO:0000313|Proteomes:UP000252707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26407 {ECO:0000313|EMBL:RCX29872.1,
RC   ECO:0000313|Proteomes:UP000252707};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JUL-2018) 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:RCX29872.1}.
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DR   EMBL; QPJY01000006; RCX29872.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369C777; -.
DR   OrthoDB; 9815750at2; -.
DR   Proteomes; UP000252707; 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   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; 1.
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; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065:SF52; SENSOR PROTEIN KINASE PILS; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
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); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:RCX29872.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252707};
KW   Transferase {ECO:0000313|EMBL:RCX29872.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        30..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        134..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        157..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          327..540
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   544 AA;  59580 MW;  4B04A2BE98DA84C9 CRC64;
     MGWFGNGIGN TILSRPGLGQ TWKPLQILNL YRLLLALILS VLFFSGMGPN FLGSHQPWLF
     GWLSGAYVLF ALATVITIRR QRPGFREQTT LQVLMDIAVI TLLMHASGGV TTGMGMLLVV
     NVAGGSLLLP GRHAFLFAAM ASLAILAEQF YADLFRIFST TAYTQSGILG AMLFAGAFLA
     DGLSRRARAS EALAAQRGVD LASLERLNEH IIQHMQSGII VVDPELRIRL MNNAAWYLLG
     LPASVEGQRL GQVSAQLDVQ LRRWLLDHEY QPVSFRVAPT AAELMPRFTA LGSGGGSGNL
     VFLEDMARTS QQAQQLKLAS LGRLTASIAH EVRNPLGAIS HAAQLLGETP DLQAGDQRLI
     EIIGAHTRRV NEIVESILQL SRREASHPEV LDLKSWLAAF SEEFSLQHAL GPGHLFLSIR
     PPETRVLIDA TQFRQILTNL CENSLRYGRP PDGHYQLVLQ GGITRETKGP YLDIIDNGPG
     IDPEVAFQIF EPFFTTDRTG GTGLGLYIAR ELAEANRARL DYIPVPTGGC CFRILFADPR
     IQTL
//
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