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Database: UniProt
Entry: A7H929_ANADF
LinkDB: A7H929_ANADF
Original site: A7H929_ANADF 
ID   A7H929_ANADF            Unreviewed;       441 AA.
AC   A7H929;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Anae109_1016 {ECO:0000313|EMBL:ABS25225.1};
OS   Anaeromyxobacter sp. (strain Fw109-5).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=404589 {ECO:0000313|EMBL:ABS25225.1, ECO:0000313|Proteomes:UP000006382};
RN   [1] {ECO:0000313|EMBL:ABS25225.1, ECO:0000313|Proteomes:UP000006382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fw109-5 {ECO:0000313|EMBL:ABS25225.1,
RC   ECO:0000313|Proteomes:UP000006382};
RX   PubMed=25614562; DOI=10.1128/genomeA.01449-14;
RA   Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA   Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA   Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA   Loeffler F.E., Fields M.W.;
RT   "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT   metal-reducing bacterium isolated from a contaminated subsurface
RT   environment.";
RL   Genome Announc. 3:0-0(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; CP000769; ABS25225.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7H929; -.
DR   STRING; 404589.Anae109_1016; -.
DR   KEGG; afw:Anae109_1016; -.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_623548_0_0_7; -.
DR   Proteomes; UP000006382; Chromosome.
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   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   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 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   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006382};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        91..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        118..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        143..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          225..429
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   441 AA;  46295 MW;  D55EEDF28ED8033C CRC64;
     MAAISRLQPT DAFQAAVEAP VPEGVPRARG LPGDLVPLAF HLPALAVLAL SGLSANRLGV
     VALAAAVQQA HYLTWRRQPG KLCVNADIDQ IAWMVVALQA CFLFTAGVAV AATGGVRSPL
     LVTIAGGYAA GVAAVGDRLQ TRVLLAATAL VVGVIALLPP VLTGPGLAGA AHGLLTVMSV
     LGIGALLAPV HARARKRRDA FARARKEMAS DALARAQSLE QIGSKVAHEL KNPLTGVKAL
     VQLGLRNPAE ATSHERLEVV DREVTRMQEI LHNYLSFTRP LQTVTPRRVQ LGPLVSDTLV
     VLSARADEAR VRLYAQGDAT LEADPRRIKE ALLNLVANAI EATPAGGEVV VEVRPAGDEA
     EIVVRDTGRG MPPDTLRRIG TPFFTTREDG TGLGVVLARS VIAQHGGSLR YESEPGHGTR
     VRVTLPRVSN GARHGPCSAR G
//
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