ID A0A0G0DCA5_9BACT Unreviewed; 334 AA.
AC A0A0G0DCA5;
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=UR94_C0010G0018 {ECO:0000313|EMBL:KKP91894.1};
OS Parcubacteria group bacterium GW2011_GWA2_36_10.
OC Bacteria.
OX NCBI_TaxID=1618808 {ECO:0000313|EMBL:KKP91894.1, ECO:0000313|Proteomes:UP000034083};
RN [1] {ECO:0000313|EMBL:KKP91894.1, ECO:0000313|Proteomes:UP000034083}
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_02065};
CC Single-pass membrane protein {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:KKP91894.1}.
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DR EMBL; LBRC01000010; KKP91894.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0DCA5; -.
DR STRING; 1618808.UR94_C0010G0018; -.
DR PATRIC; fig|1618808.3.peg.285; -.
DR Proteomes; UP000034083; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 221
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 334 AA; 38331 MW; C852B5C7CAB3CD91 CRC64;
MKLKYIFLSL VIIIIAPILW FFFLLNSANN LESQKSFIIE QGKGVNEISD NLAKADLIKN
KFVFETWLWL LKSEDKVKAG IYSFPAGSSI RQLTKLILAI PENTASKFTI IEGWGRNWPE
FKKVLETHDF SYDEFLGLTA SAKTWREQYD FLADAPSTAS LEGFLFPDTY FVDQYTDNII
LLNKILINFE QKLRPELRAE IKKQNKTIFE VVTLASIIER EVPEHADKKM IADVFLKRLK
NNIGLQSDAT INFVTGKGLT QPSRDDLKID SPYNTYKYRG LPPGPIANPS ISSIEAVIYP
TPNDYYYFLT TKEGEVIYSQ TYQEHLANKA KYLD
//
