ID A0A941E0A6_9BURK Unreviewed; 331 AA.
AC A0A941E0A6;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 02-APR-2025, entry version 7.
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:MBR7798581.1};
GN ORFNames=KDM90_00970 {ECO:0000313|EMBL:MBR7798581.1};
OS Undibacterium fentianense.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Oxalobacteraceae; Undibacterium.
OX NCBI_TaxID=2828728 {ECO:0000313|EMBL:MBR7798581.1, ECO:0000313|Proteomes:UP000678545};
RN [1] {ECO:0000313|EMBL:MBR7798581.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FT137W {ECO:0000313|EMBL:MBR7798581.1};
RA Lu H.;
RT "novel species isolated from subtropical streams in China.";
RL Submitted (APR-2021) 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 -!- 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:MBR7798581.1}.
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DR EMBL; JAGSPJ010000001; MBR7798581.1; -; Genomic_DNA.
DR RefSeq; WP_212673746.1; NZ_JAGSPJ010000001.1.
DR Proteomes; UP000678545; 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; ENDOLYTIC MUREIN TRANSGLYCOSYLASE; 1.
DR PANTHER; PTHR30518:SF2; ENDOLYTIC MUREIN TRANSGLYCOSYLASE; 1.
DR Pfam; PF02618; YceG; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02065};
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:UP000678545};
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 217
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 331 AA; 36840 MW; 5F8D54203722BE08 CRC64;
MAFLKKILLF LVLFVLIVGG IGIWTFKTWS DTPITLDKAT EFTIKPGSNI RSAARQLVDA
GVPLHPYLFE ILARVSGKAT SLKAGSFEAI SQETPAQILK KIVDGKFSLT NLSIIEGWNF
KQMRAAIDAH PSIRHDTIGL SDTELLQRIG SHYTHPEGLF FPDTYLFAKN SSDVQVYQQA
HQAMLNQLNE EWGKRLQGLP YKDVYQALIM ASIIEKETGQ AAERGMIASV FVNRLRAGML
LQTDPTVIYG MGDKFQGNIR KRDLTTDTAY NTYTRAGLPP TPIALPGKDA IKAALNPEPS
NAYYFVARGN GTSQFSENLN EHNRAVNKYQ R
//
