ID   C5BUS2_BEUC1            Unreviewed;       462 AA.
AC   C5BUS2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   02-SEP-2026, entry version 78.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|PROSITE-ProRule:PRU01082};
DE            EC=3.1.3.16 {ECO:0000256|PROSITE-ProRule:PRU01082};
GN   OrderedLocusNames=Bcav_0030 {ECO:0000313|EMBL:ACQ78296.1};
OS   Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / CCUG 43141 / JCM
OS   11478 / NBRC 16432 / NCIMB 13614 / HKI 0122).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Beutenbergiaceae; Beutenbergia.
OX   NCBI_TaxID=471853 {ECO:0000313|EMBL:ACQ78296.1, ECO:0000313|Proteomes:UP000007962};
RN   [1] {ECO:0000313|EMBL:ACQ78296.1, ECO:0000313|Proteomes:UP000007962}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-8 / DSM 12333 / NBRC 16432
RC   {ECO:0000313|Proteomes:UP000007962};
RX   PubMed=21304633; DOI=10.4056/sigs.1162;
RA   Land M., Pukall R., Abt B., Goker M., Rohde M., Glavina Del Rio T.,
RA   Tice H., Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA   Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Hauser L., Chang Y.J., Jefferies C.C.,
RA   Saunders E., Brettin T., Detter J.C., Han C., Chain P., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Beutenbergia cavernae type strain (HKI
RT   0122).";
RL   Stand. Genomic Sci. 1:21-28(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU01082};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU01082};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU01082};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU01082};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000256|PROSITE-ProRule:PRU01082};
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DR   EMBL; CP001618; ACQ78296.1; -; Genomic_DNA.
DR   RefSeq; WP_012725076.1; NC_012669.1.
DR   AlphaFoldDB; C5BUS2; -.
DR   STRING; 471853.Bcav_0030; -.
DR   KEGG; bcv:Bcav_0030; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_025431_1_1_11; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000007962; Chromosome.
DR   CDD; cd00143; PP2Cc; 1.
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   Pfam; PF13672; PP2C_2; 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:0000256|PROSITE-ProRule:PRU01082};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01082};
KW   Protein phosphatase {ECO:0000256|PROSITE-ProRule:PRU01082};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007962};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        305..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..239
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          247..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          396..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..286
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..418
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..439
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   462 AA;  47947 MW;  13010CB39F36316C CRC64;
     MTIALRYAAR SDVGLVRSVN QDSGYAGPHL LVLADGMGGP AGGDIASSVA IAHLAGLDGE
     SHGADDLLDH LDRAVQDAHE ELRDLAAEDP ELAGLGTTLI AMLRSGNKLA MVHVGDSRAY
     VFRDARLERI TSDHTFVQHL VDIGRLTEEE AEHHPQRSVL LRVLGDSGPD VVLDESVREA
     RVGDRYLLCS DGLSSYVSAD TITTTVGEVR DPAACAEALI ELALRAGAPD NVTCVVADVV
     DVDALPDGAA PDPTPQVVGA AATDRHRPTR GGSGAAARAA ALNPAADVEP DEDPKPARRR
     WVRPVLVVAL VLAILAGAGY GFSRWTQTQY YVAASGDYVA IYQGIPQEIG PVRLSHVVVT
     TDLRVEDLPP FAQDRLTETI VTGSFESARG IVRGLEEQST APEDPTASPT PTPSPSPTAP
     GQGGTPAPSL PPASPAPTEP PDDTTGAPAG PTGDVPAVVG SA
//