ID A7HCE4_ANADF Unreviewed; 413 AA.
AC A7HCE4;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Anae109_2188 {ECO:0000313|EMBL:ABS26390.1};
OS Anaeromyxobacter sp. (strain Fw109-5).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=404589 {ECO:0000313|EMBL:ABS26390.1, ECO:0000313|Proteomes:UP000006382};
RN [1] {ECO:0000313|EMBL:ABS26390.1, ECO:0000313|Proteomes:UP000006382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fw109-5 {ECO:0000313|EMBL:ABS26390.1,
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000769; ABS26390.1; -; Genomic_DNA.
DR AlphaFoldDB; A7HCE4; -.
DR STRING; 404589.Anae109_2188; -.
DR KEGG; afw:Anae109_2188; -.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3284; Bacteria.
DR HOGENOM; CLU_000445_89_2_7; -.
DR Proteomes; UP000006382; Chromosome.
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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 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; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 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.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006382}.
FT DOMAIN 37..90
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 181..398
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 413 AA; 45279 MW; B5CB562743CB6954 CRC64;
MGSTACEAPA RARAPRHLGR GGGERARLLA APGEGQREAV DFSLLDSVPD AMVIADEHGE
IVHANREAER LFGWPRSELA GRPIEILLPS RFRAEHRAHR TGYHAAPRTR PMGLGLDLSG
LRKDGAEFAA EISLSPIEVD GRRCVVAAVR DVTDRKLLEG RARLWSKAQD EVRERDEFLS
VASHELRTPV TALQLQLQLL HRLAARGKDD VPRLLEPRVE ALERQTRRIA LLVNELLDVS
RMRLGRLELR YEALDLADVV RGAAAQVREE VARSGSVLQL DLARAPGRWD RMRLEQVVTN
LLLNASKFGQ GKPIAVEVEA DGPRARLRVT DQGMGIAPEH HARVFERFER AVPIANYGGL
GLGLYVARQV VAAHGGEIRV ESLPGAGATF TVELPRDPPG EHAPAALDAP AVH
//
