ID Q63QH7_BURPS Unreviewed; 372 AA.
AC Q63QH7;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=peptidoglycan lytic exotransglycosylase {ECO:0000256|ARBA:ARBA00012587};
DE EC=4.2.2.n1 {ECO:0000256|ARBA:ARBA00012587};
DE AltName: Full=Murein hydrolase A {ECO:0000256|ARBA:ARBA00030918};
GN OrderedLocusNames=BPSL3046 {ECO:0000313|EMBL:CAH37057.1};
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH37057.1, ECO:0000313|Proteomes:UP000000605};
RN [1] {ECO:0000313|EMBL:CAH37057.1, ECO:0000313|Proteomes:UP000000605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243 {ECO:0000313|EMBL:CAH37057.1,
RC ECO:0000313|Proteomes:UP000000605};
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M., Atkins T.,
RA Crossman L.C., Pitt T., Churcher C., Mungall K., Bentley S.D., Sebaihia M.,
RA Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F.,
RA Challis G.L., Cherevach I., Chillingworth T., Cronin A., Crosset B.,
RA Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H.,
RA Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S.,
RA Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
RN [2] {ECO:0007829|PDB:6QK4}
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 25-372, AND DISULFIDE BONDS.
RX PubMed=31363151; DOI=10.1038/s41598-019-47483-z;
RA Jenkins C.H., Wallis R., Allcock N., Barnes K.B., Richards M.I., Auty J.M.,
RA Galyov E.E., Harding S.V., Mukamolova G.V.;
RT "The lytic transglycosylase, LtgG, controls cell morphology and virulence
RT in Burkholderia pseudomallei.";
RL Sci. Rep. 9:11060-11060(2019).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exolytic cleavage of the (1->4)-beta-glycosidic linkage
CC between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine
CC (GlcNAc) residues in peptidoglycan, from either the reducing or the
CC non-reducing ends of the peptidoglycan chains, with concomitant
CC formation of a 1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n1;
CC Evidence={ECO:0000256|ARBA:ARBA00001420};
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DR EMBL; BX571965; CAH37057.1; -; Genomic_DNA.
DR RefSeq; WP_004549948.1; NZ_CP009538.1.
DR RefSeq; YP_109641.1; NC_006350.1.
DR PDB; 6QK4; X-ray; 1.73 A; B=25-372.
DR PDBsum; 6QK4; -.
DR AlphaFoldDB; Q63QH7; -.
DR SMR; Q63QH7; -.
DR STRING; 272560.BPSL3046; -.
DR GeneID; 56597095; -.
DR KEGG; bps:BPSL3046; -.
DR PATRIC; fig|272560.51.peg.2221; -.
DR eggNOG; COG2821; Bacteria.
DR PHI-base; PHI:9429; -.
DR Proteomes; UP000000605; Chromosome 1.
DR GO; GO:0019867; C:outer membrane; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009254; P:peptidoglycan turnover; IEA:InterPro.
DR CDD; cd14668; mlta_B; 1.
DR CDD; cd14485; mltA_like_LT_A; 1.
DR Gene3D; 2.40.40.10; RlpA-like domain; 2.
DR InterPro; IPR010611; 3D_dom.
DR InterPro; IPR026044; MltA.
DR InterPro; IPR005300; MltA_B.
DR InterPro; IPR036908; RlpA-like_sf.
DR PANTHER; PTHR30124; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE A; 1.
DR PANTHER; PTHR30124:SF0; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE A; 1.
DR Pfam; PF06725; 3D; 1.
DR Pfam; PF03562; MltA; 1.
DR PIRSF; PIRSF019422; MltA; 1.
DR SMART; SM00925; MltA; 1.
DR SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:6QK4};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosidase {ECO:0000313|EMBL:CAH37057.1};
KW Hydrolase {ECO:0000313|EMBL:CAH37057.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000000605};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..372
FT /note="peptidoglycan lytic exotransglycosylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004266685"
FT DOMAIN 134..267
FT /note="Lytic transglycosylase MltA"
FT /evidence="ECO:0000259|SMART:SM00925"
FT DISULFID 76..89
FT /evidence="ECO:0007829|PDB:6QK4"
SQ SEQUENCE 372 AA; 39978 MW; D4E7BC70757BF4B9 CRC64;
MGFSRRLAGW AAAVAAAALL AACVGSPVRQ GARPAGAAIV PGQIAAARLT PVAWQQVPGW
QDDSLIGATI ALRQNCARLA RQANWQRACA AAMRLDDLDV GSARTFFETY FTPFQFANND
GTLDGLVTGY YEPLLHGSRV RRGPYQYALY RWPAGYRAGA SMPARAQLMR SGALSGNELV
WVDDPIEAFF LQVQGSGRVV LDDGTVMRVG YGGTNNQPYR SIGKWLLDHG ELGAGQATMQ
GIKAWARANP SRVDALLDTN PRFVFFREMP SQEDVPHGGA DGPVGALGVP LTPERSIAVD
PSSIPLGTPV FLQTTRPMTN APLNRLVFAQ DVGTAIKGGV RADYFWGLGD DAGDQAGRMK
QNGRMWLLFP NS
//
