ID A0A0G0CJQ7_9BACT Unreviewed; 332 AA.
AC A0A0G0CJQ7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 22.
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=UR34_C0012G0009 {ECO:0000313|EMBL:KKP43657.1};
OS candidate division WS6 bacterium GW2011_GWC1_33_20.
OC Bacteria; Candidatus Dojkabacteria.
OX NCBI_TaxID=1619089 {ECO:0000313|EMBL:KKP43657.1, ECO:0000313|Proteomes:UP000034302};
RN [1] {ECO:0000313|EMBL:KKP43657.1, ECO:0000313|Proteomes:UP000034302}
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:KKP43657.1}.
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DR EMBL; LBOV01000012; KKP43657.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0CJQ7; -.
DR PATRIC; fig|1619089.3.peg.527; -.
DR Proteomes; UP000034302; 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; 3.30.160.60; 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 219
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 332 AA; 37805 MW; 14F58206462E6FE1 CRC64;
MKSLTKIFLL ALLTVLVAGF LIKKNYDSAI ETPNNDSTEK VALEIDTGES VDSIVNKLVE
EGILKEKWVY YFKLYLKLND LSSKIQAGNY QIPLNLSIKE IAETIQQAKD LDIWVTIPEG
LRKDEIANIL STELVKGGNA NFSKEEFLAL TTDTTYISTL GIPYVTSNLE GFLFPDKYAF
SKDALTKDVL KKLVDTFISK VGINDTYQDI IIASMVEREA YNSEDRPLIA DIIKRRYAEG
WLLQIDATLL YPKKDWKYVI SNSDKEENNP YNTYKVQGLP PTPICNPGLS SINATRNPKP
NNYYYYIHDT EGNVYFAETL SEHNRNIQTY LR
//
