ID S5TF31_9CORY Unreviewed; 479 AA.
AC S5TF31;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=B841_00140 {ECO:0000313|EMBL:AGS33511.1};
OS Corynebacterium maris DSM 45190.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1224163 {ECO:0000313|EMBL:AGS33511.1, ECO:0000313|Proteomes:UP000015388};
RN [1] {ECO:0000313|EMBL:AGS33511.1, ECO:0000313|Proteomes:UP000015388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Coryn-1 {ECO:0000313|Proteomes:UP000015388};
RA Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT "The complete genome sequence of Corynebacterium maris Coryn-1 (=DSM
RT 45190).";
RL Submitted (NOV-2012) 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};
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DR EMBL; CP003924; AGS33511.1; -; Genomic_DNA.
DR RefSeq; WP_020933446.1; NC_021915.1.
DR AlphaFoldDB; S5TF31; -.
DR STRING; 1224163.B841_00140; -.
DR KEGG; cmd:B841_00140; -.
DR PATRIC; fig|1224163.3.peg.27; -.
DR eggNOG; COG0631; Bacteria.
DR HOGENOM; CLU_025431_0_0_11; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000015388; 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 Reference proteome {ECO:0000313|Proteomes:UP000015388};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 319..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..235
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 243..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 479 AA; 50904 MW; 3B803A9F3AEEDAAB CRC64;
MSLILNYAVS SDRGLVRQDN EDSAYAGPHI LVLADGMGGH AAGEIASQIM VNHMIKLDRD
PQDNDLLALL GGYSDDANRE IAQTVRTQPE TEGMGTTLTS LLFNGTHFGL IHVGDSRGYR
LRDGKLEQIT VDDTFVQSLV EKGKLDPGDV SSHPQKALIL KAYTGTPVEP SLRILDAKPG
DRLLLCSDGL SDPVTASTIE EALRQGTPEI ATQRLVELAL RSGGPDNVTV VVADVLEDTE
IDEKTRAQVP KTPVTAGALN GPVEVSHPDT AAGRAAALSR PAASAQPNKS VSVPPPAVEK
FDEDEPGDDA EEGPRKGRWI GVIVALLVIL GLIGGGWWLY SRMDDNYFLA AEEVDGEERF
VIEQGVNFSV FGRDLHEPVQ GACLNAGDDL RVLDLADLPA AGDDDCAAFG PQDLPESARA
GLDALDGGSY EQVTQQLRNL AQQALPVCIT VEPEDPDAET QTEAGAGDLA QPGVNCREV
//
