ESTR2_MYCTU
ID ESTR2_MYCTU Reviewed; 227 AA.
AC I6YF08;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Esterase Rv3036c {ECO:0000305};
DE EC=3.1.1.- {ECO:0000269|PubMed:25224799};
GN Name=TB22.2 {ECO:0000312|EMBL:CCP45845.1};
GN OrderedLocusNames=Rv3036c {ECO:0000312|EMBL:CCP45845.1};
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] {ECO:0007744|PubMed:21969609}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=25224799; DOI=10.1016/j.pep.2014.09.003;
RA Chen L., Dang G., Deng X., Cao J., Yu S., Wu D., Pang H., Liu S.;
RT "Characterization of a novel exported esterase Rv3036c from Mycobacterium
RT tuberculosis.";
RL Protein Expr. Purif. 104:50-56(2014).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=27690385; DOI=10.1021/acsinfecdis.6b00135;
RA Tallman K.R., Levine S.R., Beatty K.E.;
RT "Small-molecule probes reveal esterases with persistent activity in dormant
RT and reactivating Mycobacterium tuberculosis.";
RL ACS Infect. Dis. 2:936-944(2016).
CC -!- FUNCTION: Hydrolyzes ester substrates carbon chain lengths ranging from
CC C2 to C14 (PubMed:25224799). In vitro, acetate (C2), butyrate (C4) and
CC caprylate (C6) are hydrolyzed with high efficiency. Has lower activity
CC against laurate (C12), myristate (C14) and caproate (C8), and weak
CC activity against palmitate (C16) (PubMed:25224799).
CC {ECO:0000269|PubMed:25224799}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acid ester + H2O = a fatty acid + an aliphatic alcohol
CC + H(+); Xref=Rhea:RHEA:59388, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:35748;
CC Evidence={ECO:0000269|PubMed:25224799};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+);
CC Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622;
CC Evidence={ECO:0000269|PubMed:25224799};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate +
CC H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477;
CC Evidence={ECO:0000269|PubMed:25224799};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a hexanoate ester + H2O = an aliphatic alcohol + H(+) +
CC hexanoate; Xref=Rhea:RHEA:47352, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:87656;
CC Evidence={ECO:0000269|PubMed:25224799};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dodecanoate ester + H2O = an aliphatic alcohol + dodecanoate
CC + H(+); Xref=Rhea:RHEA:47364, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:87659;
CC Evidence={ECO:0000269|PubMed:25224799};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tetradecanoate ester + H2O = an aliphatic alcohol + H(+) +
CC tetradecanoate; Xref=Rhea:RHEA:47388, ChEBI:CHEBI:2571,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807,
CC ChEBI:CHEBI:87691; Evidence={ECO:0000269|PubMed:25224799};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) +
CC octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657;
CC Evidence={ECO:0000269|PubMed:25224799};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:25224799};
CC Temperature dependence:
CC Optimum temperature is 38 degrees Celsius.
CC {ECO:0000269|PubMed:25224799};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:25224799};
CC Single-pass membrane protein {ECO:0000255}. Secreted, cell wall
CC {ECO:0000269|PubMed:25224799}. Note=Probably anchored in the cell wall
CC and cell membrane via an N-terminal transmembrane helix.
CC {ECO:0000269|PubMed:25224799}.
CC -!- DEVELOPMENTAL STAGE: Remains active in dormant M.tuberculosis.
CC {ECO:0000269|PubMed:27690385}.
CC -!- SIMILARITY: Belongs to the RsiV family. {ECO:0000305}.
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DR EMBL; AL123456; CCP45845.1; -; Genomic_DNA.
DR RefSeq; NP_217552.1; NC_000962.3.
DR RefSeq; WP_003415939.1; NZ_NVQJ01000011.1.
DR AlphaFoldDB; I6YF08; -.
DR SMR; I6YF08; -.
DR STRING; 83332.Rv3036c; -.
DR SwissLipids; SLP:000001444; -.
DR PaxDb; I6YF08; -.
DR PRIDE; I6YF08; -.
DR DNASU; 887320; -.
DR GeneID; 887320; -.
DR KEGG; mtu:Rv3036c; -.
DR PATRIC; fig|83332.111.peg.3383; -.
DR TubercuList; Rv3036c; -.
DR eggNOG; ENOG502ZA8P; Bacteria.
DR OMA; GQPPHNT; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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:0008126; F:acetylesterase activity; IEA:RHEA.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.90.640.20; -; 1.
DR InterPro; IPR021729; DUF3298.
DR InterPro; IPR037126; PdaC/RsiV-like_sf.
DR Pfam; PF11738; DUF3298; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall; Hydrolase; Lipid metabolism; Membrane;
KW Reference proteome; Secreted; Transmembrane; Transmembrane helix.
FT CHAIN 1..227
FT /note="Esterase Rv3036c"
FT /evidence="ECO:0000255"
FT /id="PRO_5010212191"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 227 AA; 24407 MW; 0F2C73D55F4B348B CRC64;
MRYLIATAVL VAVVLVGWPA AGAPPSCAGL GGTVQAGQIC HVHASGPKYM LDMTFPVDYP
DQQALTDYIT QNRDGFVNVA QGSPLRDQPY QMDATSEQHS SGQPPQATRS VVLKFFQDLG
GAHPSTWYKA FNYNLATSQP ITFDTLFVPG TTPLDSIYPI VQRELARQTG FGAAILPSTG
LDPAHYQNFA ITDDSLIFYF AQGELLPSFV GACQAQVPRS AIPPLAI
