PE16_MYCTU
ID PE16_MYCTU Reviewed; 528 AA.
AC L7N697; I6XBG6;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Esterase PE16 {ECO:0000305};
DE EC=3.1.1.- {ECO:0000269|PubMed:23383323};
DE AltName: Full=PE family protein PE16 {ECO:0000305};
GN Name=PE16 {ECO:0000303|PubMed:23383323};
GN OrderedLocusNames=Rv1430 {ECO:0000312|EMBL:CCP44189.1};
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]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, MUTAGENESIS OF SER-199, AND ACTIVE SITE.
RC STRAIN=H37Rv;
RX PubMed=23383323; DOI=10.1371/journal.pone.0055320;
RA Sultana R., Vemula M.H., Banerjee S., Guruprasad L.;
RT "The PE16 (Rv1430) of Mycobacterium tuberculosis is an esterase belonging
RT to serine hydrolase superfamily of proteins.";
RL PLoS ONE 8:E55320-E55320(2013).
CC -!- FUNCTION: Esterase that hydrolyzes short to medium chain fatty acid
CC esters with the highest specific activity for p-nitrophenyl caproate
CC (pNPC6). Has lower activity with p-nitrophenyl caprylate (pNPC8) and p-
CC nitrophenyl butyrate (pNPC4). Has weak activity with p-nitrophenyl
CC caprate (pNPC10) and p-nitrophenyl laurate (pNPC12). Does not possess
CC lipolytic activity and cutinase activity.
CC {ECO:0000269|PubMed:23383323}.
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:23383323};
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:23383323};
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:23383323};
CC -!- ACTIVITY REGULATION: Esterase activity is significantly inhibited by
CC the serine modifier phenylmethylsulfonyl fluoride (PMSF).
CC {ECO:0000269|PubMed:23383323}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.2 mM for pNPC4 {ECO:0000269|PubMed:23383323};
CC KM=5.15 mM for pNPC6 {ECO:0000269|PubMed:23383323};
CC KM=10 mM for pNPC8 {ECO:0000269|PubMed:23383323};
CC Note=kcat is 341 sec(-1) with pNPC4 as substrate. kcat is 534 sec(-1)
CC with pNPC6 as substrate. kcat is 305 sec(-1) with pNPC8 as substrate.
CC {ECO:0000269|PubMed:23383323};
CC pH dependence:
CC Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:23383323};
CC Temperature dependence:
CC Optimum temperature is 37-38 degrees Celsius.
CC {ECO:0000269|PubMed:23383323};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the mycobacterial PE family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44189.1; -; Genomic_DNA.
DR RefSeq; WP_003407378.1; NZ_NVQJ01000038.1.
DR RefSeq; YP_177810.1; NC_000962.3.
DR AlphaFoldDB; L7N697; -.
DR STRING; 83332.Rv1430; -.
DR SwissLipids; SLP:000001335; -.
DR PaxDb; L7N697; -.
DR DNASU; 886652; -.
DR GeneID; 886652; -.
DR KEGG; mtu:Rv1430; -.
DR PATRIC; fig|83332.111.peg.1589; -.
DR TubercuList; Rv1430; -.
DR eggNOG; COG3391; Bacteria.
DR eggNOG; COG5651; Bacteria.
DR OMA; TIATQEM; -.
DR PhylomeDB; L7N697; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000084; PE-PGRS_N.
DR InterPro; IPR013228; PE-PPE_C.
DR Pfam; PF00934; PE; 1.
DR Pfam; PF08237; PE-PPE; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Membrane; Reference proteome; Serine esterase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..528
FT /note="Esterase PE16"
FT /id="PRO_0000448332"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1..93
FT /note="PE"
FT /evidence="ECO:0000255"
FT DOMAIN 149..369
FT /note="PE-PPE"
FT /evidence="ECO:0000255"
FT REGION 94..143
FT /note="Linker"
FT /evidence="ECO:0000305|PubMed:23383323"
FT ACT_SITE 199
FT /evidence="ECO:0000305|PubMed:23383323"
FT MUTAGEN 199
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:23383323"
SQ SEQUENCE 528 AA; 54584 MW; 3D27409215D347A9 CRC64;
MSFVFAVPEM VAATASDLAS LGAALSEATA AAAIPTTQVL AAAADEVSAA IAELFGAHGQ
EFQALSAQAS AFHDRFVRAL SAAAGWYVDA EAANAALVDT AATGASELGS GGRTALILGS
TGTPRPPFDY MQQVYDRYIA PHYLGYAFSG LYTPAQFQPW TGIPSLTYDQ SVAEGAGYLH
TAIMQQVAAG NDVVVLGFSQ GASVATLEMR HLASLPAGVA PSPDQLSFVL LGNPNNPNGG
ILARFPGLYL QSLGLTFNGA TPDTDYATTI YTTQYDGFAD FPKYPLNILA DVNALLGIYY
SHSLYYGLTP EQVASGIVLP VSSPDTNTTY ILLPNEDLPL LQPLRGIVPE PLLDLIEPDL
RAIIELGYDR TGYADVPTPA ALFPVHIDPI AVPPQIGAAI GGPLTALDGL LDTVINDQLN
PVVTSGIYQA GAELSVAAAG YGAPAGVTNA IFIGQQVLPI LVEGPGALVT ADTHYLVDAI
QDLAAGDLSG FNQNLQLIPA TNIALLVFAA GIPAVAAVAI LTGQDFPV
