ID B0VH73_CLOAI Unreviewed; 638 AA.
AC B0VH73;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Putative bifunctional signal transducer for sigma factor regulation / phosphoserine phosphatase {ECO:0000313|EMBL:CAO80688.1};
DE EC=3.1.3.3 {ECO:0000313|EMBL:CAO80688.1};
GN OrderedLocusNames=CLOAM0806 {ECO:0000313|EMBL:CAO80688.1};
OS Cloacimonas acidaminovorans (strain Evry).
OC Bacteria; Candidatus Cloacimonadota; Candidatus Cloacimonadia;
OC Candidatus Cloacimonadales; Candidatus Cloacimonadaceae; Cloacimonas.
OX NCBI_TaxID=459349 {ECO:0000313|EMBL:CAO80688.1, ECO:0000313|Proteomes:UP000002019};
RN [1] {ECO:0000313|EMBL:CAO80688.1, ECO:0000313|Proteomes:UP000002019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Evry {ECO:0000313|Proteomes:UP000002019};
RX PubMed=18245282; DOI=10.1128/JB.01248-07;
RA Pelletier E., Kreimeyer A., Bocs S., Rouy Z., Gyapay G., Chouari R.,
RA Riviere D., Ganesan A., Daegelen P., Sghir A., Cohen G.N., Medigue C.,
RA Weissenbach J., Le Paslier D.;
RT "'Candidatus Cloacamonas acidaminovorans': genome sequence reconstruction
RT provides a first glimpse of a new bacterial division.";
RL J. Bacteriol. 190:2572-2579(2008).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CU466930; CAO80688.1; -; Genomic_DNA.
DR RefSeq; WP_015424547.1; NC_020449.1.
DR AlphaFoldDB; B0VH73; -.
DR STRING; 459349.CLOAM0806; -.
DR KEGG; caci:CLOAM0806; -.
DR eggNOG; COG2208; Bacteria.
DR eggNOG; COG3850; Bacteria.
DR HOGENOM; CLU_020306_0_0_0; -.
DR OrthoDB; 9802500at2; -.
DR Proteomes; UP000002019; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0036424; F:L-phosphoserine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd12913; PDC1_MCP_like; 1.
DR CDD; cd12912; PDC2_MCP_like; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR PANTHER; PTHR43156; STAGE II SPORULATION PROTEIN E-RELATED; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF07228; SpoIIE; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:CAO80688.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002019};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 301..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 326..379
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 413..633
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT COILED 367..394
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 638 AA; 73083 MW; EF5347CA1552E978 CRC64;
MKQRQEKRGL AYQIIVFIFI SLFLIFTAFI GITRILFSHI MMENAQETVS HLANETTYQI
ESRLTNVVDI SRTILTLYHY NHFERNKLDS ILHDWVYEFE TLEAITIAYA PSYYQEGYSR
TIFHSHNRAV YQELHPADYQ YLDWFQIPFE LKSKYWTEPW YDATATQETV ISYCLPLFAE
GNCVGIMRLD TKLSALQKIV SPLKLKHSGY AFLVSSIGTI ITHPADSLTF NESIFSLAEA
TNDKNLRQIG KKMINGNIDF VRLQDNAVFG DSWLYYCPLL TNNWSLGIII PHKDVVGDLN
LLLIIQTLFS LIIFLTISFI VYYRTLSVSR PIRLFTEVAE RIGQGDFDAK LPKTGNSYEI
DRLILAFEKM QESLKDYIKN LEITNAEKNR IETEVKIASE IQRKLIPENT LQPYEIKELR
CYGILEPAGD IGGDLYDFFP IDKSHFLFVI ADVAGKGIVA SMTMTMVSTY LRTVSTYHYT
ASEIMQNLNN FLCKQTSASN FVTALLGIIN LKNGELEFSN AGHTPMIIRK TDLSYKIFTE
THSYPLGIFA NREIGSMTIK LEKGEEIILV TDGVTETMNA TEDFLGLKGL ENIIKNLSST
NPEQTVRQIL QHVHSFAQNT PQKDDITILV IDYKKSED
//
