ID   C4LLR9_CORK4            Unreviewed;       552 AA.
AC   C4LLR9;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   Name=ppp {ECO:0000313|EMBL:ACR16923.1};
GN   OrderedLocusNames=ckrop_0126 {ECO:0000313|EMBL:ACR16923.1};
OS   Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 /
OS   CCUG 35717).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=645127 {ECO:0000313|EMBL:ACR16923.1, ECO:0000313|Proteomes:UP000001473};
RN   [1] {ECO:0000313|EMBL:ACR16923.1, ECO:0000313|Proteomes:UP000001473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717
RC   {ECO:0000313|Proteomes:UP000001473};
RX   PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA   Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA   Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S.,
RA   Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT   "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT   revealed insights into the physiology of a lipophilic corynebacterium that
RT   lacks mycolic acids.";
RL   J. Biotechnol. 136:22-30(2008).
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; CP001620; ACR16923.1; -; Genomic_DNA.
DR   RefSeq; WP_012730811.1; NC_012704.1.
DR   AlphaFoldDB; C4LLR9; -.
DR   STRING; 645127.ckrop_0126; -.
DR   KEGG; ckp:ckrop_0126; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_025431_0_0_11; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000001473; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
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; PF00481; PP2C; 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:0000313|EMBL:ACR16923.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001473};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        357..378
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          280..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          480..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..313
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..503
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..542
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   552 AA;  57655 MW;  AC13796D15128A7D CRC64;
     MTYALTYAAA SHVGLIRGNN EDSAYAGPHL LALADGMGGH AAGEIASQLM ISHIAHVDDV
     GPGDDMCGQL ADAMAEGNAA IANQIDINPA TEGMGCTLDA FFFNDDTLAI CHVGDSRGYL
     YRDGQLEQIT KDDTYVQSLV DEGQLAPEDV SNHPQRSLIL KALTGRPVEP TLMLREVRPG
     DRYLLCSDGL SDPVSHDTIA DIVSRGTLDQ AAERLIDLAL RSGGPDNVTV VLGEIVDTSD
     DDYAPAAPLL VGALDPEQTD VARPDTAAGR AVGMKLIQQN KEAQAQRNPG GRSGSQPASP
     DNGGSSNNGG AQASRGDLAD PVRGAGDRAD SAHGGSAVAG GHGHNHEKHN KKKGRRIGLT
     VGVIVLVLAV IIGAGGWWGK KTLDNRYYIA TDNNELVVYK GADETILGKT LHSTYQRACL
     DAKGNLTLLD ANSTKKCHRF QLTDLPPSTR TNVDNLPSGD YNDVQTQMER LAKQALPVCV
     TRESSHGNAD NPDAGRDDRS GEPAPSDAAT SGEPAPSAPS AGESAANNAS GDTANGQPGD
     LTTPGDTCRE VK
//