ID A0A0G0DI16_9BACT Unreviewed; 320 AA.
AC A0A0G0DI16;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 24.
DE RecName: Full=Endolytic murein transglycosylase {ECO:0000256|HAMAP-Rule:MF_02065};
DE EC=4.2.2.- {ECO:0000256|HAMAP-Rule:MF_02065};
DE AltName: Full=Peptidoglycan polymerization terminase {ECO:0000256|HAMAP-Rule:MF_02065};
GN Name=mltG {ECO:0000256|HAMAP-Rule:MF_02065};
GN ORFNames=UR56_C0005G0021 {ECO:0000313|EMBL:KKP62775.1};
OS Candidatus Roizmanbacteria bacterium GW2011_GWC2_34_23.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1618484 {ECO:0000313|EMBL:KKP62775.1, ECO:0000313|Proteomes:UP000034004};
RN [1] {ECO:0000313|EMBL:KKP62775.1, ECO:0000313|Proteomes:UP000034004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- FUNCTION: Functions as a peptidoglycan terminase that cleaves nascent
CC peptidoglycan strands endolytically to terminate their elongation.
CC {ECO:0000256|HAMAP-Rule:MF_02065}.
CC -!- SIMILARITY: Belongs to the transglycosylase MltG family.
CC {ECO:0000256|HAMAP-Rule:MF_02065}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKP62775.1}.
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DR EMBL; LBPR01000005; KKP62775.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0DI16; -.
DR STRING; 1618484.UR56_C0005G0021; -.
DR PATRIC; fig|1618484.3.peg.267; -.
DR Proteomes; UP000034004; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
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 Gene3D; 3.30.1490.480; Endolytic murein transglycosylase; 1.
DR HAMAP; MF_02065; MltG; 1.
DR InterPro; IPR003770; MLTG-like.
DR NCBIfam; TIGR00247; endolytic transglycosylase MltG; 1.
DR PANTHER; PTHR30518:SF2; ENDOLYTIC MUREIN TRANSGLYCOSYLASE; 1.
DR PANTHER; PTHR30518; UNCHARACTERIZED; 1.
DR Pfam; PF02618; YceG; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_02065};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_02065};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02065};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_02065};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_02065}.
FT SITE 199
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 320 AA; 36783 MW; CDAEE85299922A24 CRC64;
MKKTNILLFL LVIISISFYF FYSEGSLPVN KSSKVSKIFI IKQGEPLNLI VNNLASEGLI
RNKIIFYLIV KKLGIERKIQ AGDFRISENM SAQEVATNLT HGTIDIWLTL IEGMRKEEMA
QIISKTLDIP EIEIVRTTNE GYIFPDTYLV PRTATSEIVL SIINKNFESK FDEKLHTQAK
NKKLTEKQVL ILASLVEREA RQSSTREKVA GIILKRYLAD WPLQIDATVQ YVLGYQPNEK
SWWKKELTED DLKIDSPYNT YKNKGLPPEP IANPSLSSIK AVINANENTP YWYYLTDKNG
IMHYAVTLEE HETNVQKYLQ
//
