ID A0A0G1THH0_9BACT Unreviewed; 340 AA.
AC A0A0G1THH0;
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=UX75_C0035G0008 {ECO:0000313|EMBL:KKU53608.1};
OS Candidatus Moranbacteria bacterium GW2011_GWE2_47_10.
OC Bacteria; Candidatus Moranbacteria.
OX NCBI_TaxID=1618714 {ECO:0000313|EMBL:KKU53608.1, ECO:0000313|Proteomes:UP000034744};
RN [1] {ECO:0000313|EMBL:KKU53608.1, ECO:0000313|Proteomes:UP000034744}
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:KKU53608.1}.
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DR EMBL; LCNJ01000035; KKU53608.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1THH0; -.
DR PATRIC; fig|1618714.3.peg.799; -.
DR Proteomes; UP000034744; 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 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 225
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 340 AA; 37945 MW; 5EDA640F3DB85245 CRC64;
MKIIKRIIIL VCLLAIFMGG YLFVNYRTDT SVGKADEAKV VVVAKGDSVD EVAEKLEEQE
LISRQLYFIY YVWIHNIENK IIAGEYEIAP GLKIAEIAEI LIKGEVKPAY VKVTFPEGWT
AEQMAERLDG KNLPGGEFLE IAMDPPAEIK NGFDFLKDIP SGASLEGFLF PDTYFFAQEA
SAEDIVGKML ENFDLKFNQD LRYRIAVQNK DPFEMITMAS IIESEVKTEE DRKIVSGIFW
NRLGIGMALQ SDATVSYGLG GEKKIQHDAN DIDSDSPYNT YKFRGLPPGP VSNPGISSIR
AAIDPTDSDY IYFLNNPKTG KTFFSVTFEE HVANKAANGL
//
