ID   Y2439_ANADF             Reviewed;         238 AA.
AC   A7HD44;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Response regulator receiver protein Anae109_2439;
GN   OrderedLocusNames=Anae109_2439;
OS   Anaeromyxobacter sp. (strain Fw109-5).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter;
OC   unclassified Anaeromyxobacter.
OX   NCBI_TaxID=404589;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fw109-5;
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).
RN   [2]
RP   FUNCTION, PTM, PHOSPHORYLATION AT ASP-52 AND ASP-169 BY GCHK, AND
RP   MUTAGENESIS OF ASP-52 AND ASP-169.
RC   STRAIN=Fw109-5;
RX   PubMed=21852234; DOI=10.1074/jbc.m111.274811;
RA   Kitanishi K., Kobayashi K., Uchida T., Ishimori K., Igarashi J.,
RA   Shimizu T.;
RT   "Identification and functional and spectral characterization of a globin-
RT   coupled histidine kinase from Anaeromyxobacter sp. Fw109-5.";
RL   J. Biol. Chem. 286:35522-35534(2011).
CC   -!- FUNCTION: Member of the two-component regulatory system
CC       GcHK/Anae109_2439. Is involved in a signal transduction system
CC       responding to oxygen availability. {ECO:0000269|PubMed:21852234}.
CC   -!- PTM: Is diphosphorylated by GchK. {ECO:0000269|PubMed:21852234}.
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DR   EMBL; CP000769; ABS26640.1; -; Genomic_DNA.
DR   RefSeq; WP_012097228.1; NC_009675.1.
DR   AlphaFoldDB; A7HD44; -.
DR   SMR; A7HD44; -.
DR   STRING; 404589.Anae109_2439; -.
DR   EnsemblBacteria; ABS26640; ABS26640; Anae109_2439.
DR   KEGG; afw:Anae109_2439; -.
DR   eggNOG; COG0745; Bacteria.
DR   eggNOG; COG4566; Bacteria.
DR   HOGENOM; CLU_096477_0_0_7; -.
DR   OMA; PFCALVD; -.
DR   OrthoDB; 1687028at2; -.
DR   Proteomes; UP000006382; Chromosome.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF00072; Response_reg; 2.
DR   SMART; SM00448; REC; 2.
DR   SUPFAM; SSF52172; SSF52172; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome; Repeat;
KW   Two-component regulatory system.
FT   CHAIN           1..238
FT                   /note="Response regulator receiver protein Anae109_2439"
FT                   /id="PRO_0000415893"
FT   DOMAIN          3..117
FT                   /note="Response regulatory 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DOMAIN          121..228
FT                   /note="Response regulatory 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   MOD_RES         52
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT                   ECO:0000269|PubMed:21852234"
FT   MOD_RES         169
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT                   ECO:0000269|PubMed:21852234"
FT   MUTAGEN         52
FT                   /note="D->A: Is monophosphorylated by GcHK, but not
FT                   diphosphorylated. Is not phosphorylated at all; when
FT                   associated with A-169."
FT                   /evidence="ECO:0000269|PubMed:21852234"
FT   MUTAGEN         169
FT                   /note="D->A: Is monophosphorylated by GcHK, but not
FT                   diphosphorylated. Is not phosphorylated at all; when
FT                   associated with A-52."
FT                   /evidence="ECO:0000269|PubMed:21852234"
SQ   SEQUENCE   238 AA;  25852 MW;  9E5E485A49499E4C CRC64;
     MRRYLIVDDN RDFAENLAEI LRDGGDEVAI AENGQEALAL ARKTRFDALL TDMRMPLMGG
     AELVHELRRI DPGAAAMVIT AHVADDALEA ARREGLLAVL PKPVAVPRIL DLLAAARRDG
     LVAVVEDDSR MSDNLCEALR GRGFAAVTAA SVTETERLGP VEPFCALVDL RVPGGADGDA
     LRRLRERFPG LPVIVVTGTH EVPPVPHQGY FTKPFDTAEL LSAVERLHRE RGQTVVPE