ID B5RM78_BORDL Unreviewed; 529 AA. AC B5RM78; DT 04-NOV-2008, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 1. DT 27-MAR-2024, entry version 81. DE SubName: Full=Response regulator receiver (CheY) modulated Serine phosphatase {ECO:0000313|EMBL:ACH93464.1}; DE EC=3.1.3.3 {ECO:0000313|EMBL:ACH93464.1}; GN OrderedLocusNames=BDU_523 {ECO:0000313|EMBL:ACH93464.1}; OS Borrelia duttonii (strain Ly). OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae; OC Borrelia. OX NCBI_TaxID=412419 {ECO:0000313|EMBL:ACH93464.1, ECO:0000313|Proteomes:UP000000611}; RN [1] {ECO:0000313|EMBL:ACH93464.1, ECO:0000313|Proteomes:UP000000611} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ly {ECO:0000313|EMBL:ACH93464.1, RC ECO:0000313|Proteomes:UP000000611}; RX PubMed=18787695; DOI=10.1371/journal.pgen.1000185; RA Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J., RA Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.; RT "The genome of Borrelia recurrentis, the agent of deadly louse-borne RT relapsing fever, is a degraded subset of tick-borne Borrelia duttonii."; RL PLoS Genet. 4:E1000185-E1000185(2008). 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; CP000976; ACH93464.1; -; Genomic_DNA. DR AlphaFoldDB; B5RM78; -. DR STRING; 412419.BDU_523; -. DR KEGG; bdu:BDU_523; -. DR eggNOG; COG2208; Bacteria. DR HOGENOM; CLU_516462_0_0_12; -. DR Proteomes; UP000000611; Chromosome. DR GO; GO:0036424; F:L-phosphoserine phosphatase activity; IEA:UniProtKB-EC. 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; 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:SF14; PHOSPHOSERINE PHOSPHATASE RSBP; 1. DR PANTHER; PTHR43156; STAGE II SPORULATION PROTEIN E-RELATED; 1. DR Pfam; PF07228; SpoIIE; 1. DR SMART; SM00331; PP2C_SIG; 1. DR SUPFAM; SSF52172; CheY-like; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 4: Predicted; KW Hydrolase {ECO:0000313|EMBL:ACH93464.1}; KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}. FT DOMAIN 150..268 FT /note="Response regulatory" FT /evidence="ECO:0000259|PROSITE:PS50110" FT MOD_RES 199 FT /note="4-aspartylphosphate" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169" SQ SEQUENCE 529 AA; 61307 MW; 5A66B48808D82C11 CRC64; MRMNSNNVIN VLNEFGLKIE EIFLLINTYS YALYKETPRY FYDDITNYLE LTLDIANKFQ GEFADSKDLK LGKFMLRSMK CDLMSYLYLS LELIDNSMHY SGIGDAGIAF FKAISCKILS VISYIEIEFE NMVFSSALKN RKDANKGGNQ LLIFSCESAY STKLVNYLIL KDYIVISANT VDLFSQLLCD NFYDLIILDL NSDENIQMIL DLLRNIKSNS LYEMVPVIVI SQITRKDIIQ TFIEEQVDDY FFKSLDLLVL DIRITSFLKK KKVIEQGQKY LDLVLHGREC VESELIEAGN YIENLLPKKI RNEFFHSNWI FVPSKRIGGD FFNYYFVNDD NLIIYLIDIS GHGVGSALLS LNVSSVINSY VMNNNDISPY KVLNYVNTYF VKFRSDMFIT LWYGVLNVKT KHLRFASAGA PPAVVLSEKG NVYLKTKGAI LGIEEMYPCK ESECYLNKFS HLLLFSDGVY EIENNQDIIM SIDDFYKILK KNTLNLDSFV LERLYNKMLN LSKYNVFRDD FSILEFIIY //