ID A0A4S4C291_9BACI Unreviewed; 374 AA.
AC A0A4S4C291;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 02-APR-2025, entry version 18.
DE RecName: Full=Endolytic murein transglycosylase {ECO:0000256|HAMAP-Rule:MF_02065};
DE EC=4.2.2.29 {ECO:0000256|HAMAP-Rule:MF_02065};
DE AltName: Full=Peptidoglycan lytic transglycosylase {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 ECO:0000313|EMBL:THF81794.1};
GN ORFNames=E6W99_03855 {ECO:0000313|EMBL:THF81794.1};
OS Metabacillus sediminilitoris.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Metabacillus.
OX NCBI_TaxID=2567941 {ECO:0000313|EMBL:THF81794.1, ECO:0000313|Proteomes:UP000310334};
RN [1] {ECO:0000313|EMBL:THF81794.1, ECO:0000313|Proteomes:UP000310334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSL-17 {ECO:0000313|EMBL:THF81794.1,
RC ECO:0000313|Proteomes:UP000310334};
RA Wei Y., Mao H., Fang J.;
RT "Bacillus sediminilitoris sp. nov., isolated from a tidal flat sediment on
RT the East China Sea.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a peptidoglycan chain = a peptidoglycan chain with N-
CC acetyl-1,6-anhydromuramyl-[peptide] at the reducing end + a
CC peptidoglycan chain with N-acetylglucosamine at the non-reducing
CC end.; EC=4.2.2.29; Evidence={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:THF81794.1}.
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DR EMBL; SSNT01000003; THF81794.1; -; Genomic_DNA.
DR RefSeq; WP_136351882.1; NZ_CP046266.1.
DR AlphaFoldDB; A0A4S4C291; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000310334; 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; 3.30.160.60; 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; ENDOLYTIC MUREIN TRANSGLYCOSYLASE; 1.
DR PANTHER; PTHR30518:SF2; ENDOLYTIC MUREIN TRANSGLYCOSYLASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000310334};
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 28..51
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 260
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 374 AA; 42497 MW; ED39A6105501199F CRC64;
MSAVDSNKDA FRKKLLEKQK EAKVVRKIVL TVFIILTIVF SGLIGGGYLY IKSSLEPVDP
DDQTFKNVTV PIGSSVSAIS NILEENGIIK DARVFKYYIK FKNESGFQAG NYQLSKSMTF
QDIIESLKQG KLMDEVAFQI TIPEGRQLKE IASIVSKKTD FSEELILEKL TNKTFINAMR
AKYPDLLTND IFGKNVNYAL EGYLYPATYP FYKKDPTLEE VLEPMIKKMN DEVKKYIPTL
QEKKMSVHQF VTMASLIEEE ATDQADREKI SSVFYNRLDQ NMPLQTDPTV LYALGEHKDR
VFYKDLEVDS PYNTYKNKGL PPGPIASAGE VSFAAALSPE NTDFLYFLAT KEGEVIFTKT
LDEHNKEKNK HITN
//
