ID A0A0G0LDJ9_9BACT Unreviewed; 351 AA.
AC A0A0G0LDJ9;
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=UT12_C0004G0013 {ECO:0000313|EMBL:KKQ89983.1};
OS Candidatus Curtissbacteria bacterium GW2011_GWC2_38_9.
OC Bacteria; Candidatus Curtissbacteria.
OX NCBI_TaxID=1618414 {ECO:0000313|EMBL:KKQ89983.1, ECO:0000313|Proteomes:UP000034893};
RN [1] {ECO:0000313|EMBL:KKQ89983.1, ECO:0000313|Proteomes:UP000034893}
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:KKQ89983.1}.
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DR EMBL; LBVP01000004; KKQ89983.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0LDJ9; -.
DR Proteomes; UP000034893; 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 CDD; cd08010; MltG_like; 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 TRANSMEM 29..50
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 232
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 351 AA; 39428 MW; 61E75C516E950F4C CRC64;
MAAFLSSIKE RVSITGQPLW RPKLIRKKFL IFSILFVVLI LAPIVLNQYY NYLLKSRSTQ
ESFQIFIIKP GQPIAQIAKN LEKAGLVKNA LAFRLLVAQM GIAKNIQYGD FRLSPNKTSR
EIAQELTHGA IDVWVTLPEG MRVEQQADLI ESKLKVSSND KYQFDKKEYI KLAQEGYMFP
DTYLIAKDAA AKDIVERLRQ TFDEKVAKNL LVTSSGLSED EIVILASLIE KEAKSDEERS
TIAGILLNRV DVGMALEVDA TVSYAKGYDS ANNTWWPTVT VADYKSVKSS YNTYLNAGLP
PAPIASPGLE SIRSAASPAQ TDYFYYLHDS KGQIHYAKTV EEHNKNIQDF L
//
