ID   A1R0V1_PAEAT            Unreviewed;       550 AA.
AC   A1R0V1;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   OrderedLocusNames=AAur_0032 {ECO:0000313|EMBL:ABM07710.1};
OS   Paenarthrobacter aurescens (strain TC1).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Paenarthrobacter.
OX   NCBI_TaxID=290340 {ECO:0000313|EMBL:ABM07710.1, ECO:0000313|Proteomes:UP000000637};
RN   [1] {ECO:0000313|EMBL:ABM07710.1, ECO:0000313|Proteomes:UP000000637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC1 {ECO:0000313|EMBL:ABM07710.1,
RC   ECO:0000313|Proteomes:UP000000637};
RX   PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA   Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA   Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V., Khouri H.,
RA   Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT   "Secrets of soil survival revealed by the genome sequence of Arthrobacter
RT   aurescens TC1.";
RL   PLoS Genet. 2:2094-2106(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = 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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001512};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = 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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001482};
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DR   EMBL; CP000474; ABM07710.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1R0V1; -.
DR   STRING; 290340.AAur_0032; -.
DR   KEGG; aau:AAur_0032; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_025431_1_1_11; -.
DR   Proteomes; UP000000637; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR47992:SF267; ALPHABET, ISOFORM E; 1.
DR   PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        398..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          2..233
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          260..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          494..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..289
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..330
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   550 AA;  58253 MW;  0B5A9129DA0925F1 CRC64;
     MRYAARSDVG RIRSKNDDSA YVGRHLAVVA DGMGGHAGGD VASASTVLDM IHLDHDDYPE
     GAETVLADEI QTANSLLSEL VHQNPKLSGM GTTVTALLLE GRKLHFAHIG DSRAYRLRNN
     KFEQVSIDHT FVQRLIDEGR LRPEEAETHP HKNVLMRVLG DVDASPELDL DVLDVEPGER
     WLLCSDGLNY VAGHVVERMV RETKDLHECA EILVALTLEA GAPDNVTVVM LEIAEETDDD
     VNTAAVDIVP AAALAAVDEP EAVTATKSAD DLSADKAAED TKADSQAKAA READAGSSFS
     AGDPGDSKDD AASSDESKEP PATTDPHLGE HLSAEVLREE LASRPHELVG AAATAAETGS
     IPTVAGRTVA RRAATVLTHK AEQDRVEVEE PARRRVRWLM PAVAAVVVLG VVVGLWLGYA
     WTQTRYYVGE YDQRVAIFNG ISQRLGPIQL SRLEAVTDIR VDSLPEYGQQ SVRQTVPAGD
     LNGAQGIVEN LRNTGSASAN CPSPSPTASA SGSATTTPTP TPTATVPIPS TAAVASPTPS
     PVPTPCEAAK
//