ID   A9B4U9_HERA2            Unreviewed;       527 AA.
AC   A9B4U9;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   OrderedLocusNames=Haur_3034 {ECO:0000313|EMBL:ABX05672.1};
OS   Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC   Bacteria; Chloroflexota; Chloroflexia; Herpetosiphonales;
OC   Herpetosiphonaceae; Herpetosiphon.
OX   NCBI_TaxID=316274 {ECO:0000313|EMBL:ABX05672.1, ECO:0000313|Proteomes:UP000000787};
RN   [1] {ECO:0000313|Proteomes:UP000000787}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23779 / DSM 785 / 114-95
RC   {ECO:0000313|Proteomes:UP000000787};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABX05672.1, ECO:0000313|Proteomes:UP000000787}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23779 / DSM 785 / 114-95
RC   {ECO:0000313|Proteomes:UP000000787};
RX   PubMed=22675585; DOI=10.4056/sigs.2194987;
RA   Kiss H., Nett M., Domin N., Martin K., Maresca J.A., Copeland A.,
RA   Lapidus A., Lucas S., Berry K.W., Glavina Del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Richardson P., Bruce D., Goodwin L., Han C., Detter J.C.,
RA   Schmutz J., Brettin T., Land M., Hauser L., Kyrpides N.C., Ivanova N.,
RA   Goker M., Woyke T., Klenk H.P., Bryant D.A.;
RT   "Complete genome sequence of the filamentous gliding predatory bacterium
RT   Herpetosiphon aurantiacus type strain (114-95(T)).";
RL   Stand. Genomic Sci. 5:356-370(2011).
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; CP000875; ABX05672.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9B4U9; -.
DR   STRING; 316274.Haur_3034; -.
DR   KEGG; hau:Haur_3034; -.
DR   eggNOG; COG0631; Bacteria.
DR   eggNOG; COG3170; Bacteria.
DR   HOGENOM; CLU_516564_0_0_0; -.
DR   InParanoid; A9B4U9; -.
DR   BioCyc; HAUR316274:GHYA-3066-MONOMER; -.
DR   Proteomes; UP000000787; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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   Gene3D; 4.10.1080.10; TSP type-3 repeat; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   InterPro; IPR028974; TSP_type-3_rpt.
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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        279..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          59..272
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          354..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..391
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..415
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..527
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   527 AA;  55537 MW;  D19B33E4BD1EEC59 CRC64;
     MSQAANLPNL VVYGQSDVGR QRNNNEDNLA WRHADERSVG TKLVNGVTEL FAKIRGGGAT
     GFSVKIDHKL LASHGRLYVV ADGVGGNDDG ELASRAVVEY TTKFFYNSDP KNYKSKQDQL
     NAAIQYATKM VYKEAGNTNR ASTLVLALVW DEGTFRKIIF SNVGDSKGYL FRANNTEYDR
     AVQTKDHVNA MNKSLWQSMG DPEVTPHFSD ELVLGKDDVI VLCSDGLSDG VQAEEIGKIA
     TRNAPQNATT ELISLANERG GHDNITNVVV RNGPAPIQWG ALGGILGVVL LVAALLGGIV
     FIGGDDVNRT QGGRNAIMIP TRPIITMVDG SFATVTLPAE TATAEAELIR QATENPVPTD
     TLGPQATSVP GTNPTARPAA TATNRPAANN PTPIPATNPP AVQPTNPPVV IQPTNPPAPG
     DRDGDGVTDD VDPCPDVAGP NNGCPAPVEP TAPPAVVDTD GDTIPDNVDD CPNEPGDPSR
     NGCPKPVEQA TNTPKPPTDT PRPTDTPQPT AVPTSPINPN DPPTPRP
//