PSTP_MYCTO
ID PSTP_MYCTO Reviewed; 514 AA.
AC P9WHW4; L0T2B3; P71588; Q8VKT2;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Serine/threonine protein phosphatase PstP {ECO:0000250|UniProtKB:P9WHW5};
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:P9WHW5};
DE AltName: Full=Mycobacterial Ser/Thr phosphatase {ECO:0000250|UniProtKB:P9WHW5};
DE Short=Mstp {ECO:0000250|UniProtKB:P9WHW5};
DE AltName: Full=PP2C-family Ser/Thr phosphatase {ECO:0000250|UniProtKB:P9WHW5};
GN Name=pstP; Synonyms=mstp, ppp; OrderedLocusNames=MT0021;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Plays an important role in regulating cell division and
CC growth by reversible phosphorylation signaling. May play important
CC roles in regulating cellular metabolism and signaling pathways, which
CC could mediate the growth and development of the cell. Plays a role in
CC establishing and maintaining infection. {ECO:0000250|UniProtKB:P9WHW5}.
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:0000250|UniProtKB:P9WHW5};
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:0000250|UniProtKB:P9WHW5};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P9WHW5};
CC Note=Binds 3 Mn(2+) ions per subunit (By similarity). The third
CC manganese ion is unlikely to be involved in catalysis but contributes
CC instead to stabilize a flap segment, which is partially disordered in
CC the absence of bound metal (By similarity).
CC {ECO:0000250|UniProtKB:P9WHW5};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P9WHW5};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK44243.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000516; AAK44243.1; ALT_INIT; Genomic_DNA.
DR PIR; H70699; H70699.
DR RefSeq; WP_003899776.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WHW4; -.
DR SMR; P9WHW4; -.
DR EnsemblBacteria; AAK44243; AAK44243; MT0021.
DR KEGG; mtc:MT0021; -.
DR PATRIC; fig|83331.31.peg.22; -.
DR HOGENOM; CLU_025431_0_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Hydrolase; Manganese; Membrane; Metal-binding;
KW Protein phosphatase; Transmembrane; Transmembrane helix.
FT CHAIN 1..514
FT /note="Serine/threonine protein phosphatase PstP"
FT /id="PRO_0000428111"
FT TOPO_DOM 1..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..514
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 9..238
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 420..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..440
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..508
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WHW5"
FT BINDING 38
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WHW5"
FT BINDING 39
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WHW5"
FT BINDING 118
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P9WHW5"
FT BINDING 160
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P9WHW5"
FT BINDING 191
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WHW5"
FT BINDING 191
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P9WHW5"
FT BINDING 229
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WHW5"
SQ SEQUENCE 514 AA; 53802 MW; DD78F54F64AC2905 CRC64;
MARVTLVLRY AARSDRGLVR ANNEDSVYAG ARLLALADGM GGHAAGEVAS QLVIAALAHL
DDDEPGGDLL AKLDAAVRAG NSAIAAQVEM EPDLEGMGTT LTAILFAGNR LGLVHIGDSR
GYLLRDGELT QITKDDTFVQ TLVDEGRITP EEAHSHPQRS LIMRALTGHE VEPTLTMREA
RAGDRYLLCS DGLSDPVSDE TILEALQIPE VAESAHRLIE LALRGGGPDN VTVVVADVVD
YDYGQTQPIL AGAVSGDDDQ LTLPNTAAGR ASAISQRKEI VKRVPPQADT FSRPRWSGRR
LAFVVALVTV LMTAGLLIGR AIIRSNYYVA DYAGSVSIMR GIQGSLLGMS LHQPYLMGCL
SPRNELSQIS YGQSGGPLDC HLMKLEDLRP PERAQVRAGL PAGTLDDAIG QLRELAANSL
LPPCPAPRAT SPPGRPAPPT TSETTEPNVT SSPASPSPTT SASAPTGTTP AIPTSASPAA
PASPPTPWPV TSSPTMAALP PPPPQPGIDC RAAA
