SERB1_MYCTU
ID SERB1_MYCTU Reviewed; 308 AA.
AC P9WGJ3; L0T6W2; P66801; Q11169;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Phosphoserine phosphatase SerB1 {ECO:0000303|PubMed:25037224};
DE Short=PSP {ECO:0000303|PubMed:25037224};
DE Short=PSPase;
DE EC=3.1.3.3 {ECO:0000305|PubMed:25037224};
DE AltName: Full=O-phosphoserine phosphohydrolase;
GN Name=serB1 {ECO:0000303|PubMed:25037224, ECO:0000312|EMBL:CCP43242.1};
GN OrderedLocusNames=Rv0505c; ORFNames=MTCY20G9.32c;
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 DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=12657046; DOI=10.1046/j.1365-2958.2003.03425.x;
RA Sassetti C.M., Boyd D.H., Rubin E.J.;
RT "Genes required for mycobacterial growth defined by high density
RT mutagenesis.";
RL Mol. Microbiol. 48:77-84(2003).
RN [3]
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).
RN [4]
RP FUNCTION, AND 3D-STRUCTURE MODELING.
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RX PubMed=25037224; DOI=10.1074/jbc.m114.597682;
RA Arora G., Tiwari P., Mandal R.S., Gupta A., Sharma D., Saha S., Singh R.;
RT "High throughput screen identifies small molecule inhibitors specific for
RT Mycobacterium tuberculosis phosphoserine phosphatase.";
RL J. Biol. Chem. 289:25149-25165(2014).
CC -!- FUNCTION: Likely catalyzes the dephosphorylation of O-phospho-L-serine
CC into L-serine. {ECO:0000305|PubMed:25037224}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-serine = L-serine + phosphate;
CC Xref=Rhea:RHEA:21208, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57524; EC=3.1.3.3;
CC Evidence={ECO:0000305|PubMed:25037224};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-D-serine = D-serine + phosphate;
CC Xref=Rhea:RHEA:24873, ChEBI:CHEBI:15377, ChEBI:CHEBI:35247,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58680; EC=3.1.3.3;
CC Evidence={ECO:0000305|PubMed:25037224};
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 -!- DISRUPTION PHENOTYPE: Transposon mutagenesis experiments have
CC identified that SerB2 is essential for the pathogen's viability while
CC SerB1 is not. {ECO:0000269|PubMed:12657046}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCP43242.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL123456; CCP43242.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_177732.1; NC_000962.3.
DR AlphaFoldDB; P9WGJ3; -.
DR SMR; P9WGJ3; -.
DR STRING; 83332.Rv0505c; -.
DR PaxDb; P9WGJ3; -.
DR DNASU; 887270; -.
DR GeneID; 887270; -.
DR KEGG; mtu:Rv0505c; -.
DR PATRIC; fig|83332.12.peg.560; -.
DR TubercuList; Rv0505c; -.
DR eggNOG; COG0560; Bacteria.
DR OMA; FGRGLYK; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0036424; F:L-phosphoserine phosphatase activity; IEA:UniProtKB-EC.
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..308
FT /note="Phosphoserine phosphatase SerB1"
FT /id="PRO_0000156893"
FT TRANSMEM 280..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 62
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT ACT_SITE 64
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 62
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 64
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 169..170
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 237
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
SQ SEQUENCE 308 AA; 32673 MW; EA722C653C3A88DC CRC64;
MMVSSHLGSP DQAGHVDLAS PADPPPPDAS ASHSPVDMPA PVAAAGSDRQ PPIDLTAAAF
FDVDNTLVQG SSAVHFGRGL AARHYFTYRD VLGFLYAQAK FQLLGKENSN DVAAGRRKAL
AFIEGRSVAE LVALGEEIYD EIIADKIWDG TRELTQMHLD AGQQVWLITA TPYELAATIA
RRLGLTGALG TVAESVDGIF TGRLVGEILH GTGKAHAVRS LAIREGLNLK RCTAYSDSYN
DVPMLSLVGT AVAINPDARL RSLARERGWE IRDFRIARKA ARIGVPSALA LGAAGGALAA
LASRRQSR
