ID   A9AXC4_HERA2            Unreviewed;       548 AA.
AC   A9AXC4;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   OrderedLocusNames=Haur_4212 {ECO:0000313|EMBL:ABX06844.1};
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:ABX06844.1, 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:ABX06844.1, 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; ABX06844.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9AXC4; -.
DR   STRING; 316274.Haur_4212; -.
DR   KEGG; hau:Haur_4212; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_474658_0_0_0; -.
DR   InParanoid; A9AXC4; -.
DR   BioCyc; HAUR316274:GHYA-4259-MONOMER; -.
DR   Proteomes; UP000000787; Chromosome.
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; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
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   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   4: Predicted;
FT   DOMAIN          288..540
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   548 AA;  59387 MW;  ED5A955242909DF9 CRC64;
     MSEPTQPMTG GTQPLNPVNQ PEEHEPFAIG TVLKDIYRVT ALLTDTPTLR VYRVALLEPW
     DHCARCGAAL QASDQFCEEC GAQVEEQTAL LQETPAAQPI GAALLDDLPD DPARAALPTV
     REVFVGEDSR FAVLPDGTSL VRFDTLLSEP NTFVDQTDAV DIGIQVARAL AYLHRHGLAL
     GQLTLADLAL TNKREIKLAD AGAIRRSLGK EDQLDDVEHL GLVLEKMAGI QRQTRRLDDS
     NNPSPLDSAF ATILSDLRAK RITDASILAQ TLETLLAEQA TPISLRVRTG YATDVGMIRD
     HNEDSVLTWD LRLNWDAKPV NVGLYVVADG MGGHEGGEVA SGLAITTTAQ TLVPTLLDPQ
     LHAGPVSSKH LAELVKQAAF QANQAVYEES VRRKNDMGTT LTMAVVIGDR AIVGNVGDSR
     TYLYRDGKLQ RISKDHSLVQ RLIDIGQLDP DDIYTHPQRN AILKSLGDSG DPGTDTFEVQ
     LQPNDALFLC SDGMWEMVRD PKMAALFAEH ANPADLCDAL IEAGNAGGGE DNISVVVVRF
     DALPIVQH
//