ID A0A0G0JDI3_9BACT Unreviewed; 345 AA.
AC A0A0G0JDI3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 21.
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=US52_C0045G0019 {ECO:0000313|EMBL:KKQ34844.1};
OS candidate division WS6 bacterium GW2011_GWA2_37_6.
OC Bacteria; Candidatus Dojkabacteria.
OX NCBI_TaxID=1619087 {ECO:0000313|EMBL:KKQ34844.1, ECO:0000313|Proteomes:UP000034852};
RN [1] {ECO:0000313|EMBL:KKQ34844.1, ECO:0000313|Proteomes:UP000034852}
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:KKQ34844.1}.
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DR EMBL; LBTH01000045; KKQ34844.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0JDI3; -.
DR PATRIC; fig|1619087.5.peg.560; -.
DR Proteomes; UP000034852; 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 CDD; cd08010; MltG_like; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
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 230
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 345 AA; 38507 MW; 972E346890600BCE CRC64;
MKKILMVLVL LIAIGGGGAL YANNWYNSGI EKRLSTSSDQ VKFTVEQGEN TESIGKRLKE
AGLIENELIL KLYLRRENKG GSIQAGDFLI PKKATIPEIV EILGRGVDLD VVKVTIIEGY
KLSQISSTLE LAFSGREGVV FDQSEFNTIT KSPDNYTFDA EVQTFLDQYK PAGKSLEGFL
YPDTYEFGNT VSTKFTIESM IKHFITKTAD LNKGDDFYKK LVLASIIERE SMTNEERDEI
SSVFTNRLEI GMALQSDATV NYATGKSDPR PTFADTKIDS PYNTYKYPGL PPTPICNPRI
ESIEAALNPA DTDYYYFIHE QTGSGKVHFA KTESEHNANI AKYLD
//
