ID A0A2N3IIG6_9BACT Unreviewed; 411 AA.
AC A0A2N3IIG6;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=Rain11_0792 {ECO:0000313|EMBL:PKQ70132.1};
OS Raineya orbicola.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Raineyaceae; Raineya.
OX NCBI_TaxID=2016530 {ECO:0000313|EMBL:PKQ70132.1, ECO:0000313|Proteomes:UP000233387};
RN [1] {ECO:0000313|EMBL:PKQ70132.1, ECO:0000313|Proteomes:UP000233387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPSPC-11 {ECO:0000313|EMBL:PKQ70132.1,
RC ECO:0000313|Proteomes:UP000233387};
RA Albuquerque L., Polonia A.R.M., Barroso C., Froufe H.J.C., Lage O.,
RA Lobo-Da-Cunha A., Egas C., Da Costa M.S.;
RT "Raineya orbicola gen. nov., sp. nov. a slightly thermophilic bacterium of
RT the phylum Bacteroidetes and the description of Raineyaceae fam. nov.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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};
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:PKQ70132.1}.
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DR EMBL; NKXO01000010; PKQ70132.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3IIG6; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000233387; Unassembled WGS sequence.
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 NCBIfam; NF033484; Stp1_PP2C_phos; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000233387};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 286..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..252
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 310..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 46206 MW; EF7681E628D04AFE CRC64;
MKSSTQELKN FEFGNATDVG KVRSNNEDYL GYFQTPNGHL FVLCDGMGGH QAGEKASQLA
VESLKDFFNK EFYTSPQEAL RKAIVEANWI IFSTSQKFSE YAGMGTTLVA VLIRDNQVFY
AHVGDSRLYY FEQATQTLHR ITKDHSFVQE LVDRGLIKDE DAEKHPRKNE ILRALGIHQE
VVPEVGTLPI LPADNDLLLL CSDGLNGMIS DFQIAEIITD KTLNILQRTQ KLIEKANEAG
GTDNITVQLV RFYAQQRSQA TLPAGIYKSV VLTQLPSGKK ISSKHYILGG VIAVVALLVG
VWAFQHSGTA EKKSTDTLQA KPTPDYSQRK YPVENKQENE EYTQPKDSTE KKKDTKLKPK
PTEKDEKKQE KTDKKTTENP KKDTKTTDAK SNTQKNNPKN TQQNKSKTEQ K
//
