ID I0XT59_9LEPT Unreviewed; 786 AA.
AC I0XT59;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Stage II sporulation protein E {ECO:0000313|EMBL:EIE02067.1};
GN ORFNames=LEP1GSC185_1091 {ECO:0000313|EMBL:EIE02067.1};
OS Leptospira licerasiae serovar Varillal str. VAR 010.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1049972 {ECO:0000313|EMBL:EIE02067.1, ECO:0000313|Proteomes:UP000004889};
RN [1] {ECO:0000313|EMBL:EIE02067.1, ECO:0000313|Proteomes:UP000004889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VAR 010 {ECO:0000313|EMBL:EIE02067.1};
RX PubMed=23145189; DOI=10.1371/journal.pntd.0001853;
RA Ricaldi J.N., Fouts D.E., Selengut J.D., Harkins D.M., Patra K.P.,
RA Moreno A., Lehmann J.S., Purushe J., Sanka R., Torres M., Webster N.J.,
RA Vinetz J.M., Matthias M.A.;
RT "Whole Genome Analysis of Leptospira licerasiae Provides Insight into
RT Leptospiral Evolution and Pathogenicity.";
RL PLoS Negl. Trop. Dis. 6:E1853-E1853(2012).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIE02067.1}.
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DR EMBL; AHOO02000005; EIE02067.1; -; Genomic_DNA.
DR RefSeq; WP_008591525.1; NZ_AHOO02000005.1.
DR AlphaFoldDB; I0XT59; -.
DR PATRIC; fig|1049972.3.peg.414; -.
DR OrthoDB; 344775at2; -.
DR Proteomes; UP000004889; Unassembled WGS sequence.
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 PANTHER; PTHR43156:SF2; MULTIDOMAIN REGULATORY PROTEIN RV1364C; 1.
DR PANTHER; PTHR43156; STAGE II SPORULATION PROTEIN E-RELATED; 1.
DR Pfam; PF07228; SpoIIE; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SUPFAM; SSF81606; PP2C-like; 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 106..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 251..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 308..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 569..784
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|SMART:SM00331"
SQ SEQUENCE 786 AA; 89878 MW; 4DE4626DF5AC49B6 CRC64;
MRNILIVFLS VILFSLILFS GLLNSYSKEA RLPFYFYPNG KIAVSNGSYT DLVGMKIDLI
EYEIVRKLGA DYGLSGHSFH FFAKEGSIVK SLTLDMRSSF EVLKDFLPDI FLSLLYFLVA
IWFFFYTRDL YIFLLFGSLS SLFLFNFFLL AFHDFLFPFF FFLYFTGFLI LDVSFRLRGK
EIPSRWFAPQ VIFSLVAGFV GLSQKGNPDL FQFLSVNGGY FNVFSAGICI LQLVFHTFRN
KGNFQEVSKK LSIVLAFFLI TIVPFVMAEF GSTKSFFMIR PYLMAALILF PVLIIFGTYT
YSLVPVQIAF SSSLTSIYSI LILTFGYLFG LEFFVRWNPG FLGKHQREWN LFYVVVAAYF
LGSLNNKLYK WIDYWSFRNN PKLHTALEEL SVMIGAPISM RATINNLIRR LVDALEVKKL
QILIPADKFS GTDLRNINFI RIPYGSEIWT YFEDHTEVTI TSHLAYGLGI RESVFKFLNQ
MEVQLAYPLF NFEKGKEVIA VFLVGEKINR KNFTLGELRF LKECTRLASL LIRNYSLLVD
EVEKKRIVRD LNMAAVLDKT LHLPELETIK SVQLGYFTLP AVGISGDYLD ILKLSPKKQL
LFLGDVSGHG LGSGYLVSAV RGIIRRQLGN SSSLPDIFRA INLFLIERYR GSEFMTSIAG
IYNASDGAFS FVNAGHTPPI CIRKGGRIEL RNETQRVLGV LPTDYRILTI HLNPGDKLVL
FTDGVTETFD ENEEIFGEEN LLRILSLNHD KDAQSLADLI KKTLEEFRNY KEPSDDISFV
CLEVSE
//
