ID   Q4JYB7_CORJK            Unreviewed;       523 AA.
AC   Q4JYB7;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 94.
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:CAI36190.1};
GN   OrderedLocusNames=jk0041 {ECO:0000313|EMBL:CAI36190.1};
OS   Corynebacterium jeikeium (strain K411).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=306537 {ECO:0000313|EMBL:CAI36190.1, ECO:0000313|Proteomes:UP000000545};
RN   [1] {ECO:0000313|EMBL:CAI36190.1, ECO:0000313|Proteomes:UP000000545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K411 {ECO:0000313|EMBL:CAI36190.1,
RC   ECO:0000313|Proteomes:UP000000545};
RX   PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005;
RA   Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA   Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA   Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT   "Complete genome sequence and analysis of the multiresistant nosocomial
RT   pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT   human skin flora.";
RL   J. Bacteriol. 187:4671-4682(2005).
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; CR931997; CAI36190.1; -; Genomic_DNA.
DR   RefSeq; WP_011272804.1; NC_007164.1.
DR   AlphaFoldDB; Q4JYB7; -.
DR   STRING; 306537.jk0041; -.
DR   GeneID; 3432973; -.
DR   KEGG; cjk:jk0041; -.
DR   PATRIC; fig|306537.10.peg.52; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_025431_0_0_11; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000000545; 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; 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:0000313|EMBL:CAI36190.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000545};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        362..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          14..248
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          280..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          483..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..344
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..508
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   523 AA;  55708 MW;  D8019FCB2DCD6612 CRC64;
     MTEDKNGNIR RTLNFAACSD RGLVRGNNED SAYAGPRLLA LADGMGGHAA GEVASQFLIN
     ALSPLDSPLI DEPNNRDQLE NLLATATDEG NQDIAAHVDE HPNLDGMGCT LTSMLFRENE
     VAICHIGDSR GYLLRDGELR QVTKDDTFVQ SLVDEGKLDP EDVSSHPQRS LILKALTGRP
     VEPTLWREKT QVGDRFMLCS DGLSDPVSTD TIREVLSRGT PEKAARKLVE MALRGGGPDN
     VTVVVADVVE FDANSNAPTD PELTLPPRPV MAGAIAGEAM DMPRPNSSAA RAAAIQGLST
     TTAASPKKDP KKDQEDDESD PATAHSGHDR TGNANSDHGD DHGEGGAGAS TATKPKKSRR
     GLWVTLAIIL AVVLAAGAAT YVMYQRVKDT YYVASDNSQI KVMNGTESSV LGIKLNSVHQ
     DVCLDEQGKA TFVDPGAGGD CHLFNTSDLT PAAQGALSDL PEDSYDKVTE QVDRLAEQTL
     PVCVTRVPAD KEKSDKKDSQ DSAKKSDAPE DLTTPGVSCR EVK
//