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Database: UniProt
Entry: A0A0G1R8Q0_9BACT
LinkDB: A0A0G1R8Q0_9BACT
Original site: A0A0G1R8Q0_9BACT 
ID   A0A0G1R8Q0_9BACT        Unreviewed;       319 AA.
AC   A0A0G1R8Q0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   13-SEP-2023, entry version 26.
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=UX25_C0012G0009 {ECO:0000313|EMBL:KKU17290.1};
OS   Candidatus Woesebacteria bacterium GW2011_GWC2_45_9.
OC   Bacteria; Candidatus Woesebacteria.
OX   NCBI_TaxID=1618589 {ECO:0000313|EMBL:KKU17290.1, ECO:0000313|Proteomes:UP000034922};
RN   [1] {ECO:0000313|EMBL:KKU17290.1, ECO:0000313|Proteomes:UP000034922}
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:KKU17290.1}.
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DR   EMBL; LCLM01000012; KKU17290.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1R8Q0; -.
DR   STRING; 1618589.UX25_C0012G0009; -.
DR   PATRIC; fig|1618589.3.peg.226; -.
DR   Proteomes; UP000034922; 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            202
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ   SEQUENCE   319 AA;  35625 MW;  A855264E3BE11EE3 CRC64;
     MKRFLFLLLI IVALVTGGTF WWYSVAKSPS AETSLRDFLI VKGSSASHIG NKLEKEGLIR
     NALAFKIYVQ VSGKAGRIQA GEYRLSPSYS LFRMVDELTR GPAEIWVTIP EGLRREEIAA
     RFASAFGQGE GFIQEFLSAS AELEGFLFPD TYLFPKDAEA ISVVKKMRQT FDIKTAELKD
     GIDVSTLTLK EIIMLASIIE RETKMDEERP MVAGVLINRL NIDMGLQADA TVQYAVGTAG
     NWWPILTKED LLVNSPYNTY RFRGLPPAPI ANPGLSSITA AVFPEESDYL YYLHDAKGQA
     YFARTLAEHN ENVRQYLGN
//
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