LYS25_MYCTU
ID LYS25_MYCTU Reviewed; 240 AA.
AC I6XEI5;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Putative peptidoglycan hydrolase Rv2525c {ECO:0000303|PubMed:25260828};
DE EC=3.2.1.17 {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=Rv2525c {ECO:0000312|EMBL:CCP45319.1},
GN LH57_13835 {ECO:0000312|EMBL:AIR15295.1};
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 IDENTIFICATION, AND GENOME REANNOTATION.
RC STRAIN=ATCC 25618 / H37Rv;
RA Lew J.M.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RA Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J.,
RA Monaco A., King S., Sohrabi A.;
RT "Phylogenetic analysis of Mycobacterial species using whole genome
RT sequences.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=H37Rv;
RX PubMed=16952959; DOI=10.1128/jb.00631-06;
RA Saint-Joanis B., Demangel C., Jackson M., Brodin P., Marsollier L.,
RA Boshoff H., Cole S.T.;
RT "Inactivation of Rv2525c, a substrate of the twin arginine translocation
RT (Tat) system of Mycobacterium tuberculosis, increases beta-lactam
RT susceptibility and virulence.";
RL J. Bacteriol. 188:6669-6679(2006).
RN [5]
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 [6]
RP FUNCTION AS AN ESTERASE, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF GLY-113; SER-115 AND GLY-117.
RC STRAIN=H37Rv;
RX PubMed=25869294; DOI=10.1007/s12010-015-1555-9;
RA Dang G., Chen L., Li Z., Deng X., Cui Y., Cao J., Yu S., Pang H., Liu S.;
RT "Expression, purification and characterisation of secreted esterase Rv2525c
RT from Mycobacterium tuberculosis.";
RL Appl. Biochem. Biotechnol. 176:1-12(2015).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 36-240, AND FUNCTION.
RC STRAIN=H37Rv;
RX PubMed=25260828; DOI=10.1016/j.jsb.2014.09.003;
RA Bellinzoni M., Haouz A., Miras I., Magnet S., Andre-Leroux G.,
RA Mukherjee R., Shepard W., Cole S.T., Alzari P.M.;
RT "Structural studies suggest a peptidoglycan hydrolase function for the
RT Mycobacterium tuberculosis Tat-secreted protein Rv2525c.";
RL J. Struct. Biol. 188:156-164(2014).
CC -!- FUNCTION: May function as a peptidoglycan hydrolase with glycosidase
CC activity (PubMed:25260828). In vitro, displays esterase activity toward
CC p-nitrophenyl esters of various acyl chain length (C4 to C16), with a
CC preference for p-nitrophenyl butyrate (C4) (PubMed:25869294).
CC {ECO:0000269|PubMed:25869294, ECO:0000305|PubMed:25260828}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC between N-acetyl-D-glucosamine residues in chitodextrins.;
CC EC=3.2.1.17; Evidence={ECO:0000305|PubMed:25260828};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0 for the hydrolysis of p-nitrophenyl butyrate.
CC {ECO:0000269|PubMed:25869294};
CC Temperature dependence:
CC Optimum temperature is 38 degrees Celsius for the hydrolysis of p-
CC nitrophenyl butyrate. {ECO:0000269|PubMed:25869294};
CC -!- PATHWAY: Cell wall degradation; peptidoglycan degradation.
CC {ECO:0000305|PubMed:25260828}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16952959}.
CC -!- INDUCTION: Upon exposure to antituberculous drugs such as isoniazid,
CC ethionamide or PA-824, Rv2525c expression is significantly up-regulated
CC together with those of other genes involved in cell wall processes.
CC {ECO:0000269|PubMed:16952959}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC {ECO:0000255|PROSITE-ProRule:PRU00648, ECO:0000305|PubMed:16952959}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene display an increase in
CC susceptibility to some beta-lactam antibiotics and, despite slower
CC growth in vitro, enhanced virulence in both cellular and murine models
CC of tuberculosis. No detectable difference in the lipid profiles.
CC {ECO:0000269|PubMed:16952959}.
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; CCP45319.1; -; Genomic_DNA.
DR EMBL; CP009480; AIR15295.1; -; Genomic_DNA.
DR RefSeq; NP_217041.1; NC_000962.3.
DR RefSeq; WP_003412957.1; NZ_NVQJ01000032.1.
DR PDB; 4PMN; X-ray; 1.44 A; A/B=36-240.
DR PDB; 4PMO; X-ray; 1.33 A; A/B=36-240.
DR PDB; 4PMQ; X-ray; 1.61 A; A=36-240.
DR PDB; 4PMR; X-ray; 1.81 A; A=36-240.
DR PDBsum; 4PMN; -.
DR PDBsum; 4PMO; -.
DR PDBsum; 4PMQ; -.
DR PDBsum; 4PMR; -.
DR AlphaFoldDB; I6XEI5; -.
DR SMR; I6XEI5; -.
DR STRING; 83332.Rv2525c; -.
DR PaxDb; I6XEI5; -.
DR PRIDE; I6XEI5; -.
DR DNASU; 888612; -.
DR GeneID; 45426525; -.
DR GeneID; 888612; -.
DR KEGG; mtu:Rv2525c; -.
DR PATRIC; fig|83332.111.peg.2823; -.
DR TubercuList; Rv2525c; -.
DR eggNOG; COG3757; Bacteria.
DR HOGENOM; CLU_075024_1_0_11; -.
DR OMA; HQFEIDK; -.
DR UniPathway; UPA00549; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR InterPro; IPR015020; DUF1906.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR Pfam; PF08924; DUF1906; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall biogenesis/degradation; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..33
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 34..240
FT /note="Putative peptidoglycan hydrolase Rv2525c"
FT /id="PRO_5003706761"
FT MUTAGEN 113
FT /note="G->A: Complete loss of esterase activity."
FT /evidence="ECO:0000269|PubMed:25869294"
FT MUTAGEN 115
FT /note="S->A: 83% loss of esterase activity."
FT /evidence="ECO:0000269|PubMed:25869294"
FT MUTAGEN 117
FT /note="G->A: 83% loss of esterase activity."
FT /evidence="ECO:0000269|PubMed:25869294"
SQ SEQUENCE 240 AA; 25370 MW; AFB4F3331FFCC7F5 CRC64;
MSVSRRDVLK FAAATPGVLG LGVVASSLRA APASAGSLGT LLDYAAGVIP ASQIRAAGAV
GAIRYVSDRR PGGAWMLGKP IQLSEARDLS GNGLKIVSCY QYGKGSTADW LGGASAGVQH
ARRGSELHAA AGGPTSAPIY ASIDDNPSYE QYKNQIVPYL RSWESVIGHQ RTGVYANSKT
IDWAVNDGLG SYFWQHNWGS PKGYTHPAAH LHQVEIDKRK VGGVGVDVNQ ILKPQFGQWA
