ID F4LRD8_TEPAE Unreviewed; 791 AA.
AC F4LRD8; L0S1M6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Protein serine/threonine phosphatase {ECO:0000313|EMBL:CCP27150.1};
DE EC=3.1.3.16 {ECO:0000313|EMBL:CCP27150.1};
GN OrderedLocusNames=TEPIRE1_2316 {ECO:0000313|EMBL:CCP27150.1};
OS Tepidanaerobacter acetatoxydans (strain DSM 21804 / JCM 16047 / Re1).
OC Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC Tepidanaerobacteraceae; Tepidanaerobacter.
OX NCBI_TaxID=1209989 {ECO:0000313|EMBL:CCP27150.1, ECO:0000313|Proteomes:UP000010802};
RN [1] {ECO:0000313|Proteomes:UP000010802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Re1 {ECO:0000313|Proteomes:UP000010802};
RX PubMed=23469343; DOI=10.1128/genomeA.00213-12;
RA Manzoor S., Bongcam-Rudloff E., Schnurer A., Muller B.;
RT "First genome sequence of a syntrophic acetate-oxidizing bacterium,
RT Tepidanaerobacter acetatoxydans strain Re1.";
RL Genome Announc. 1:E00213-E00213(2013).
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DR EMBL; HF563609; CCP27150.1; -; Genomic_DNA.
DR RefSeq; WP_013779194.1; NC_019954.2.
DR AlphaFoldDB; F4LRD8; -.
DR STRING; 1209989.TepRe1_2151; -.
DR KEGG; tae:TepiRe1_2316; -.
DR KEGG; tep:TepRe1_2151; -.
DR PATRIC; fig|1209989.3.peg.2664; -.
DR eggNOG; COG2208; Bacteria.
DR HOGENOM; CLU_017349_0_0_9; -.
DR OrthoDB; 9763774at2; -.
DR Proteomes; UP000010802; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
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; IPR014221; SpoII_E.
DR InterPro; IPR045768; SpoIIE_N.
DR NCBIfam; TIGR02865; spore_II_E; 1.
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 SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:CCP27150.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000010802};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 37..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 264..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 577..785
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
SQ SEQUENCE 791 AA; 87645 MW; 59539DB6605D0C39 CRC64;
MINRAQLKWY DYLGQKSHES QNTPFASASL KPLAKEVIPV GIIAYLFGMA SINGLYPFAL
SFMAANLLYR KEYILPGIFS FLGTLMAMKS LSSFRYLCAM GIFLLIYNQL NRINWKNEFL
FGTAVFVSNM FAGAVFLINR AVSPYDIFLL ILESGMACVM TFMISGGMPW IFNEQVQPIE
RNICMVMLSG VILSIARNFV FLNMNVRDII GVFLVLLLAL ANGSGAGAAA GIIVGITGFS
LSLSPWSTAI MAFSGLVSGA FNKLGKIGVI TGFSLGYLLY NFHVNSIGTL IISPKTLAAS
FALLLILPQA MIKRVKLYIS NPCNDAQIKA YNLEERARDR LHELASLLND LGGVFKEIFV
KDEDRVLPSE YLDSVCRKVQ LMICSDCGMR RICWEKELKR TMGAFYTLIK HHEGIYDRKE
IPFLFKSRCS QTEKIKEIVK ESSNLFKITC QMDNIIKYNQ ELIQEYFARA ADVVEAMAAG
AWEEDYEINI DDELLERLSG LDIDVERIYT DYSNNRLCVN IIKHPCENSK QCKTLIPTAV
SDALGRKMST KVVDCPLKSG NSMCRLKITS NGVLDVCVGV AGVAKEGQNV SGDGFSYLEL
KEGRYMLALC DGMGVGENAA RHSEKTLTLL ERLSEAGCAQ ETVLKVTNSA MIAVNRDESF
STIDMVLIDT ASGIAKFIKA GAPAGFIKRG TKIEMIKGGS LPLGIIDEIS PKITEKTVRP
GDMIVMVTDG IIDAFSNGQN GEEMLSRFLR ETKTANPQEM AEKVLKKAKE KNSIRDDMTV
LAARIWEKKL S
//
