ID   Y3661_MYCTU             Reviewed;         287 AA.
AC   P9WGJ1; L0TDF7; O69629;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Probable phosphatase Rv3661 {ECO:0000305};
DE            EC=3.1.3.- {ECO:0000305};
GN   OrderedLocusNames=Rv3661; ORFNames=MTV025.009;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q58989};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q58989};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.
CC       {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; AL123456; CCP46484.1; -; Genomic_DNA.
DR   PIR; F70788; F70788.
DR   RefSeq; NP_218178.1; NC_000962.3.
DR   RefSeq; WP_003419689.1; NZ_NVQJ01000028.1.
DR   AlphaFoldDB; P9WGJ1; -.
DR   SMR; P9WGJ1; -.
DR   STRING; 83332.Rv3661; -.
DR   PaxDb; P9WGJ1; -.
DR   DNASU; 885316; -.
DR   GeneID; 45427656; -.
DR   GeneID; 885316; -.
DR   KEGG; mtu:Rv3661; -.
DR   TubercuList; Rv3661; -.
DR   eggNOG; COG0560; Bacteria.
DR   OMA; DHDQMER; -.
DR   PhylomeDB; P9WGJ1; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; HDA:MTBBASE.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006385; HAD_hydro_SerB1.
DR   InterPro; IPR023214; HAD_sf.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01490; HAD-SF-IB-hyp1; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Hydrolase; Magnesium; Membrane; Metal-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..287
FT                   /note="Probable phosphatase Rv3661"
FT                   /id="PRO_0000156895"
FT   TRANSMEM        258..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..23
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"
FT   ACT_SITE        31
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q58989"
FT   ACT_SITE        33
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q58989"
FT   BINDING         31
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q58989"
FT   BINDING         33
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q58989"
FT   BINDING         204
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q58989"
SQ   SEQUENCE   287 AA;  30711 MW;  46EC2610AB9F0A5B CRC64;
     MTVSDSPAQR QTPPQTPGGT APRARTAAFF DLDKTIIAKS STLAFSKPFF AQGLLNRRAV
     LKSSYAQFIF LLSGADHDQM DRMRTHLTNM CAGWDVAQVR SIVNETLHDI VTPLVFAEAA
     DLIAAHKLCG RDVVVVSASG EEIVGPIARA LGATHAMATR MIVEDGKYTG EVAFYCYGEG
     KAQAIRELAA SEGYPLEHCY AYSDSITDLP MLEAVGHASV VNPDRGLRKE ASVRGWPVLS
     FSRPVSLRDR IPAPSAAAIA TTAAVGISAL AAGAVTYALL RRFAFQP