EMTAL_SHIFL
ID EMTAL_SHIFL Reviewed; 219 AA.
AC Q83RQ0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Endo-type membrane-bound lytic murein transglycosylase A-like protein {ECO:0000255|HAMAP-Rule:MF_01381};
DE EC=4.2.2.n2 {ECO:0000255|HAMAP-Rule:MF_01381};
DE AltName: Full=Peptidoglycan lytic endotransglycosylase {ECO:0000255|HAMAP-Rule:MF_01381};
GN Name=emtA2 {ECO:0000255|HAMAP-Rule:MF_01381}; Synonyms=mltE;
GN OrderedLocusNames=SF1183;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
CC -!- FUNCTION: Murein-degrading enzyme. May play a role in recycling of
CC muropeptides during cell elongation and/or cell division (Potential).
CC {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endolytic cleavage of the (1->4)-beta-glycosidic linkage
CC between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine
CC (GlcNAc) residues in peptidoglycan with concomitant formation of a
CC 1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01381};
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000255|HAMAP-Rule:MF_01381}.
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DR EMBL; AE005674; AAN42798.1; -; Genomic_DNA.
DR RefSeq; NP_707091.1; NC_004337.2.
DR AlphaFoldDB; Q83RQ0; -.
DR SMR; Q83RQ0; -.
DR STRING; 198214.SF1183; -.
DR EnsemblBacteria; AAN42798; AAN42798; SF1183.
DR GeneID; 1024114; -.
DR KEGG; sfl:SF1183; -.
DR PATRIC; fig|198214.7.peg.1398; -.
DR HOGENOM; CLU_103257_0_0_6; -.
DR Proteomes; UP000001006; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0016837; F:carbon-oxygen lyase activity, acting on polysaccharides; IEA:UniProtKB-UniRule.
DR GO; GO:0008932; F:lytic endotransglycosylase activity; IEA:InterPro.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR HAMAP; MF_01381; EmtA; 1.
DR InterPro; IPR023946; EmtA.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR000189; Transglyc_AS.
DR InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR Pfam; PF01464; SLT; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Lyase; Reference proteome.
FT CHAIN 1..219
FT /note="Endo-type membrane-bound lytic murein
FT transglycosylase A-like protein"
FT /id="PRO_0000312917"
SQ SEQUENCE 219 AA; 23829 MW; DDEA0935C625F987 CRC64;
MPVVTLTGIP GYTGLRIEID MVCLFDWLLA GCSSKHDYTN PPWNAKVPVQ RAMQWMPISQ
KAGAAWGVDP QLITAIIAIE SGGNPNAVSK SNAIGLMQLK ASTSGRDVYR RMGWSGEPTT
SELKNPERNI SMGAAYLNIL ETGPLAGIED PKVLQYALVV SYANGAGALL RTFSSDRKKA
ISKINDLDAD EFLDHVARNH PAPQAPRYIY KLEQALDAM
