ID   A0PRI4_MYCUA            Unreviewed;       412 AA.
AC   A0PRI4;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   10-JUN-2026, entry version 97.
DE   RecName: Full=Response regulatory domain-containing protein {ECO:0000259|PROSITE:PS50110};
GN   OrderedLocusNames=MUL_2625 {ECO:0000313|EMBL:ABL04953.1};
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=362242 {ECO:0000313|EMBL:ABL04953.1, ECO:0000313|Proteomes:UP000000765};
RN   [1] {ECO:0000313|EMBL:ABL04953.1, ECO:0000313|Proteomes:UP000000765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99 {ECO:0000313|EMBL:ABL04953.1,
RC   ECO:0000313|Proteomes:UP000000765};
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D., Davies J.K., Jenkin G.A., Small P.L., Jones L.M., Tekaia F.,
RA   Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
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DR   EMBL; CP000325; ABL04953.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0PRI4; -.
DR   KEGG; mul:MUL_2625; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG2208; Bacteria.
DR   HOGENOM; CLU_035411_0_0_11; -.
DR   Proteomes; UP000000765; Chromosome.
DR   GO; GO:0016791; F:phosphatase activity; IEA:TreeGrafter.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   CDD; cd00156; REC; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR052016; Bact_Sigma-Reg.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43156:SF2; STAGE II SPORULATION PROTEIN E; 1.
DR   PANTHER; PTHR43156; STAGE II SPORULATION PROTEIN E-RELATED; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF07228; SpoIIE; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000765}.
FT   DOMAIN          27..143
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         78
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   412 AA;  43995 MW;  7D54272D172E71D0 CRC64;
     MRVPHEHDLT AGLGPSTGQR AQWQTLSLLL VEDARADAML VEELIADAAV DIQVVWARSM
     AHAERELSAA RPDCVLLDLN LPDASGIDAL DRIANRDATV PVVVLTGLND EYFGATAVAA
     GAQDYLVKGR VDPEMLRRAM LYAIERKRAE LIAADLHATQ LRARENALLE RGLLPSPLLL
     DSPGVDIVAR YRPSREDALL CGDFYDVVQT VDRVVHVLIG DVAGHGPNEA ALGAALRIAF
     RALTLAGVHG GELMRQLDRV LRAERTGEGI FATVLSLAIP PQPAGSADGA HIQVIRAGHP
     GMLLHGGGTV HWLEPPAGPA LGLNLGNWCQ HEVELPVDHG LLLLTDGLFE GYSGHRRERL
     GEHGLLSLAR SHAGLSGPAF VDALIDGAQQ RAQSLGGLTD DIAVLRVERT PA
//