ID   MLTG_STRP2              Reviewed;         551 AA.
AC   A0A0H2ZLQ1;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Endolytic murein transglycosylase {ECO:0000255|HAMAP-Rule:MF_02065, ECO:0000305};
DE            EC=4.2.2.- {ECO:0000250|UniProtKB:P28306, ECO:0000255|HAMAP-Rule:MF_02065};
DE   AltName: Full=Peptidoglycan polymerization terminase {ECO:0000255|HAMAP-Rule:MF_02065};
GN   Name=mltG {ECO:0000255|HAMAP-Rule:MF_02065, ECO:0000303|PubMed:26933838};
GN   OrderedLocusNames=SPD_1346 {ECO:0000312|EMBL:ABJ53954.1};
OS   Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=373153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D39 / NCTC 7466;
RX   PubMed=17041037; DOI=10.1128/jb.01148-06;
RA   Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA   Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT   "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT   pneumoniae and comparison with that of unencapsulated laboratory strain
RT   R6.";
RL   J. Bacteriol. 189:38-51(2007).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, DOMAIN, DISRUPTION PHENOTYPE, AND
RP   MUTAGENESIS OF GLU-428 AND TYR-488.
RC   STRAIN=D39 / NCTC 7466;
RX   PubMed=26933838; DOI=10.1111/mmi.13366;
RA   Tsui H.T., Zheng J.J., Magallon A.N., Ryan J.D., Yunck R., Rued B.E.,
RA   Bernhardt T.G., Winkler M.E.;
RT   "Suppression of a deletion mutation in the gene encoding essential PBP2b
RT   reveals a new lytic transglycosylase involved in peripheral peptidoglycan
RT   synthesis in Streptococcus pneumoniae D39.";
RL   Mol. Microbiol. 100:1039-1065(2016).
CC   -!- FUNCTION: Functions as a peptidoglycan terminase that cleaves nascent
CC       peptidoglycan strands endolytically to terminate their elongation (By
CC       similarity). Involved in peripheral peptidoglycan (PG) synthesis
CC       (PubMed:26933838). {ECO:0000250|UniProtKB:P28306, ECO:0000255|HAMAP-
CC       Rule:MF_02065, ECO:0000269|PubMed:26933838}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_02065,
CC       ECO:0000305|PubMed:26933838}; Single-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_02065}. Note=Localizes separately from FtsZ
CC       with the peripheral PG synthesis machine.
CC       {ECO:0000269|PubMed:26933838}.
CC   -!- DOMAIN: The cytoplasmic N-terminal region is not required for endolytic
CC       transglycosylase activity under normal culture conditions.
CC       {ECO:0000269|PubMed:26933838}.
CC   -!- DISRUPTION PHENOTYPE: Deletion or inactivation severely impairs growth
CC       in encapsulated and unencapsulated strains and leads to the formation
CC       of spherical shaped cells. {ECO:0000269|PubMed:26933838}.
CC   -!- MISCELLANEOUS: Peptidoglycan cleavage activity could not be detected in
CC       vitro under a variety of assay conditions, but a gene deletion can be
CC       complemented with E.coli mltG, leading to the conclusion that this gene
CC       is the functional homolog of the E.coli endolytic transglycosylase.
CC       {ECO:0000269|PubMed:26933838}.
CC   -!- SIMILARITY: Belongs to the transglycosylase MltG family.
CC       {ECO:0000255|HAMAP-Rule:MF_02065, ECO:0000305}.
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DR   EMBL; CP000410; ABJ53954.1; -; Genomic_DNA.
DR   RefSeq; WP_001291641.1; NC_008533.2.
DR   AlphaFoldDB; A0A0H2ZLQ1; -.
DR   SMR; A0A0H2ZLQ1; -.
DR   STRING; 373153.SPD_1346; -.
DR   EnsemblBacteria; ABJ53954; ABJ53954; SPD_1346.
DR   KEGG; spd:SPD_1346; -.
DR   eggNOG; COG1559; Bacteria.
DR   HOGENOM; CLU_025574_1_0_9; -.
DR   OMA; IAMPGKA; -.
DR   OrthoDB; 190480at2; -.
DR   BioCyc; SPNE373153:G1G6V-1452-MON; -.
DR   Proteomes; UP000001452; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008932; F:lytic endotransglycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd08010; MltG_like; 1.
DR   HAMAP; MF_02065; MltG; 1.
DR   InterPro; IPR003770; MLTG-like.
DR   PANTHER; PTHR30518; PTHR30518; 1.
DR   Pfam; PF02618; YceG; 1.
DR   TIGRFAMs; TIGR00247; TIGR00247; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell wall biogenesis/degradation; Lyase; Membrane;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..551
FT                   /note="Endolytic murein transglycosylase"
FT                   /id="PRO_0000436707"
FT   TOPO_DOM        1..187
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:26933838"
FT   TRANSMEM        188..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02065"
FT   TOPO_DOM        209..551
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:26933838"
FT   REGION          38..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..178
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            428
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02065,
FT                   ECO:0000269|PubMed:26933838"
FT   MUTAGEN         428
FT                   /note="E->A,Q: Lack of activity."
FT                   /evidence="ECO:0000269|PubMed:26933838"
FT   MUTAGEN         488
FT                   /note="Y->D: Decreased endolytic transglycosylase activity.
FT                   Grows slightly slower and forms cells of shorter lengths
FT                   and greater sphericity. In unencapsulated strains,
FT                   suppresses the requirement for essential genes that mediate
FT                   peripheral PG synthesis."
FT                   /evidence="ECO:0000269|PubMed:26933838"
SQ   SEQUENCE   551 AA;  60797 MW;  D59F3864D830A86B CRC64;
     MSEKSREEEK LSFKEQILRD LEKVKGYDEV LKEDEAVVRT PANEPSAEEL MADSLSTVEE
     IMRKAPTVPT HPSQGVPASP ADEIQRETPG VPSHPSQDVP SSPAEESGSR PGPGPVRPKK
     LEREYNETPT RVAVSYTTAE KKAEQAGPET PTPATETVDI IRDTSRRSRR EGAKPAKPKK
     EKKSHVKAFV ISFLVFLALL SAGGYFGYQY VLDSLLPIDA NSKKYVTVGI PEGSNVQEIG
     TTLEKAGLVK HGLIFSFYAK YKNYTDLKAG YYNLQKSMST EDLLKELQKG GTDEPQEPVL
     ATLTIPEGYT LDQIAQTVGQ LQGDFKESLT AEAFLAKVQD ETFISQAVAK YPTLLESLPV
     KDSGARYRLE GYLFPATYSI KESTTIESLI DEMLAAMDKN LSPYYSTIKS KNLTVNELLT
     IASLVEKEGA KTEDRKLIAG VFYNRLNRDM PLQSNIAILY AQGKLGQNIS LAEDVAIDTN
     IDSPYNVYKN VGLMPGPVDS PSLDAIESSI NQTKSDNLYF VADVTEGKVY YANNQEDHDR
     NVAEHVNSKL N