ID I0XPD6_9LEPT Unreviewed; 707 AA.
AC I0XPD6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=7TM diverse intracellular signaling domain / stage II sporulation protein E multi-domain protein {ECO:0000313|EMBL:EIE00744.1};
GN ORFNames=LEP1GSC185_0129 {ECO:0000313|EMBL:EIE00744.1};
OS Leptospira licerasiae serovar Varillal str. VAR 010.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1049972 {ECO:0000313|EMBL:EIE00744.1, ECO:0000313|Proteomes:UP000004889};
RN [1] {ECO:0000313|EMBL:EIE00744.1, ECO:0000313|Proteomes:UP000004889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VAR 010 {ECO:0000313|EMBL:EIE00744.1};
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:EIE00744.1}.
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DR EMBL; AHOO02000011; EIE00744.1; -; Genomic_DNA.
DR RefSeq; WP_008590819.1; NZ_AHOO02000011.1.
DR AlphaFoldDB; I0XPD6; -.
DR PATRIC; fig|1049972.3.peg.2612; -.
DR OrthoDB; 311727at2; -.
DR Proteomes; UP000004889; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF07228; SpoIIE; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 231..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 299..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 329..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 382..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 410..429
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 488..704
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|SMART:SM00331"
FT COILED 435..466
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 707 AA; 79837 MW; C5EE6985FF42A8D4 CRC64;
MEHFFPILNA FLILSFRIRL KRIFFQMKKA ITFLILIYLP FFFSGCSESS AKVEHPAIVQ
GVLELKNYDL EEQGPILLSG LWKFRWLYWK SSGLESQNSY EVVSVPSSWN GKNGSRLGEG
YGTYELSLKL NRNYGELAFI LQEQSSSYFL YVNGKLLASC GEVEFPSSSD ITIFEVKPAW
CNKLVKFTPE VEDLTIDVQI ANRDHRLGGF WAPIRFGTAS SMEKTWNAER FLDLFLAGGL
FCIGLLHLIY AAVRKGESAS MYFGTFCLIM AARGLFSGTR IISEYIDFLK YHHYVRIEYV
TFYLAIPVFL SYILSVFPRE LKRILVDLVW WIAVGACIVV LVFPVRIFTF TITVYYLVAF
LAGTLGLFSL TKAALRRRKG ALIILAGFVF IYAAMIHDIL YATFYLDTGY FTNIGAFVFI
VAQSVFLSIR SSESLDRLLD LSRNLERRVE ERTKQLRNAL RLIQNDLNVA REIQKGLLNL
EDTAEKKIGK IKFGILHKPL AEVGGDLYDI TELPNGKIRI FLADAPGHGI QAALITILIR
SIYEDLRLKE ESPGKLLSAI GSLFHGKFGN VSTFFSASIL EISSDGKKLT LSLAGSPPVL
VQNKDEEHII ECENPLVGLL ENFHFEDKEV SLTPGFRILC FTDGLTESSR LPGDFYGIER
VLASLRNGDS QSLEELLSGI QEDLFRFLGS SEPKDDILVL GIEDQRS
//