ID Q2RM97_MOOTA Unreviewed; 680 AA. AC Q2RM97; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 27-MAR-2024, entry version 87. DE SubName: Full=Serine phosphatase {ECO:0000313|EMBL:ABC18442.1}; GN OrderedLocusNames=Moth_0103 {ECO:0000313|EMBL:ABC18442.1}; OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320). OC Bacteria; Bacillota; Clostridia; Moorellales; Moorellaceae; Moorella. OX NCBI_TaxID=264732 {ECO:0000313|EMBL:ABC18442.1}; RN [1] {ECO:0000313|EMBL:ABC18442.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 39073 {ECO:0000313|EMBL:ABC18442.1}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chertkov O., Saunders E.H., Brettin T., RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., RA Kyrpides N., Anderson I., Richardson P., Ragsdale S.; RT "Complete sequence of Moorella thermoacetica ATCC 39073."; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. 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; CP000232; ABC18442.1; -; Genomic_DNA. DR RefSeq; YP_428985.1; NC_007644.1. DR AlphaFoldDB; Q2RM97; -. DR STRING; 264732.Moth_0103; -. DR EnsemblBacteria; ABC18442; ABC18442; Moth_0103. DR KEGG; mta:Moth_0103; -. DR PATRIC; fig|264732.11.peg.108; -. DR eggNOG; COG2208; Bacteria. DR HOGENOM; CLU_017349_0_0_9; -. DR OrthoDB; 9763774at2; -. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR InterPro; IPR045768; SpoIIE_N. DR PANTHER; PTHR43156:SF12; STAGE II SPORULATION PROTEIN E; 1. DR PANTHER; PTHR43156; STAGE II SPORULATION PROTEIN E-RELATED; 1. DR Pfam; PF07228; SpoIIE; 1. DR Pfam; PF19732; SpoIIE_N; 1. DR SMART; SM00331; PP2C_SIG; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR PROSITE; PS51746; PPM_2; 1. PE 4: Predicted; KW Membrane {ECO:0000256|SAM:Phobius}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 21..41 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 61..78 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 85..101 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 132..153 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 165..184 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 196..219 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 226..245 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 251..269 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 281..299 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 464..674 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000259|PROSITE:PS51746" SQ SEQUENCE 680 AA; 72220 MW; 5A249F950625D308 CRC64; MSGQTRAHSM RQQTGVLAGS EFFLDVLLLG AVFFLVRAAL LEELFPFGPA VIIAVGARRR LLWPAVVVAA VSAWLAGLPQ VYSRLLIFLF LGLACTLYPS LNQRGPLTRA TLAPVAITLV RGLGLTLWQP SFYGWVQVIF EALLAWGLSL GLLETATARR QEERLLGGGL FLLGLLLGLQ GWQVSGLSIQ GIISRYILLL AALAGGAGTG AAAGAAVGFL PSLSALITPS LAGLMAFTGL VAGSLKNLGK PGVISGFLLA HLVLANYFLG SDGVQAALRE SGLAVLFLVA TPPLLVYYFR EFLAVPVAAQ QAPADTSPRD NLKVALKSLA QNLKFHGFNE SPLETVRQVA RAACRGCPAG KVCWELEGEQ MLNTLQELLH RGSQGPLTLA ALPEWLASRC NRGRELLAAL TTRAGKGQPQ PLEDGLTNWL ASIFDNLAVM VENRGIKKEN SAGSGTGQPA LKISVGMAAT PRHRAEVTGD AFVAATLEPG RQLLILGDGM GAGREAADAS GTALELLQDL LAAGFSPELA LRTVNMVLLL RTTRENFTTI DLAMVNCHNG QTEFYKLGAC PSFIQGKDGV KILRSHSLPV GILEDLQVEA LKEELQEGDL LVMVSDGVLE AHRDLNEKEK WVSKALQRAG DARPQEIADR LLKQARALAG GNPPDDMTVV VARVEKAASA //