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Database: UniProt
Entry: C6X8E5_METGS
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Original site: C6X8E5_METGS 
ID   C6X8E5_METGS            Unreviewed;       496 AA.
AC   C6X8E5;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Exopolyphosphatase {ECO:0000256|ARBA:ARBA00020416};
DE            EC=3.6.1.11 {ECO:0000256|ARBA:ARBA00012451};
GN   OrderedLocusNames=Msip34_0166 {ECO:0000313|EMBL:ACT49415.1};
OS   Methylovorus glucosotrophus (strain SIP3-4).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylovorus.
OX   NCBI_TaxID=582744 {ECO:0000313|EMBL:ACT49415.1, ECO:0000313|Proteomes:UP000002743};
RN   [1] {ECO:0000313|Proteomes:UP000002743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SIP3-4 {ECO:0000313|Proteomes:UP000002743};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Clum A., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Kayluzhnaya M., Chistoserdova L.;
RT   "Complete sequence of chromosome of Methylovorus sp. SIP3-4.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACT49415.1, ECO:0000313|Proteomes:UP000002743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SIP3-4 {ECO:0000313|EMBL:ACT49415.1,
RC   ECO:0000313|Proteomes:UP000002743};
RX   PubMed=21622745; DOI=10.1128/JB.00404-11;
RA   Lapidus A., Clum A., Labutti K., Kaluzhnaya M.G., Lim S., Beck D.A.,
RA   Glavina Del Rio T., Nolan M., Mavromatis K., Huntemann M., Lucas S.,
RA   Lidstrom M.E., Ivanova N., Chistoserdova L.;
RT   "Genomes of three methylotrophs from a single niche uncover genetic and
RT   metabolic divergence of Methylophilaceae.";
RL   J. Bacteriol. 193:3757-3764(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[phosphate](n) + H2O = [phosphate](n-1) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:21528, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14279,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16838,
CC         ChEBI:CHEBI:43474; EC=3.6.1.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00000209};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the GppA/Ppx family.
CC       {ECO:0000256|ARBA:ARBA00007125}.
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DR   EMBL; CP001674; ACT49415.1; -; Genomic_DNA.
DR   RefSeq; WP_015829183.1; NC_012969.1.
DR   AlphaFoldDB; C6X8E5; -.
DR   STRING; 582744.Msip34_0166; -.
DR   KEGG; mei:Msip34_0166; -.
DR   eggNOG; COG0248; Bacteria.
DR   HOGENOM; CLU_025908_4_0_4; -.
DR   OrthoDB; 9793035at2; -.
DR   Proteomes; UP000002743; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004309; F:exopolyphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006793; P:phosphorus metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR022371; Exopolyphosphatase.
DR   InterPro; IPR048950; Ppx_GppA_C.
DR   InterPro; IPR003695; Ppx_GppA_N.
DR   InterPro; IPR030673; PyroPPase_GppA_Ppx.
DR   NCBIfam; TIGR03706; exo_poly_only; 1.
DR   PANTHER; PTHR30005; EXOPOLYPHOSPHATASE; 1.
DR   PANTHER; PTHR30005:SF14; EXOPOLYPHOSPHATASE; 1.
DR   Pfam; PF02541; Ppx-GppA; 1.
DR   Pfam; PF21447; Ppx-GppA_III; 1.
DR   PIRSF; PIRSF001267; Pyrophosphatase_GppA_Ppx; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Hydrolase {ECO:0000313|EMBL:ACT49415.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002743}.
FT   DOMAIN          27..306
FT                   /note="Ppx/GppA phosphatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02541"
FT   DOMAIN          314..482
FT                   /note="Ppx/GppA phosphatase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21447"
SQ   SEQUENCE   496 AA;  54994 MW;  89F8EAC4C438DC19 CRC64;
     MATQIPAPTE IAAVDLGSNS FRLQLAKVVD GHLIFHDSLR EAVRLGAGLG KDKRLDEDAQ
     RRAIECLKRF GERLRGLPPH AVRAVATNTF RVAKNAPQLL KEAEAALGFP IEIIAGREEA
     RMIFVGVSHC LPLCEHKRLV IDIGGGSTEF IVGEGVEPIQ MESLYMGCVS YSLRFFPEGR
     LTEDNFEQAR IAAATEIQAI RKNFSSSNWQ EAVGSSGTAR SLGEIIRLNG LSDGSITYEG
     LRFIRQQLIK ARDIKKIELA GVSADRAAVL PGGLSIMLAA FEALNIDKMT TADTALREGV
     LYELLGRIHH HDTREATVSS FMRRYHVDAA QAKRVHRLAL DLLAQVSDQL RMDVSKAENY
     LTWAAKLHEI GISIAHSGYH KHSAYVIENA DMPGFSKMDQ ETLGFLVRAQ RRSLAKLAVP
     MLSDDHCLLV LILRLAVLFH RSRLSDRQPK LGLKGHGQRF ELSVEPGWLS ENPLTDAELR
     NEVDYWREIG ISLTLA
//
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