ID W0EE08_9FIRM Unreviewed; 341 AA.
AC W0EE08;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=DESME_10675 {ECO:0000313|EMBL:AHF07439.1};
OS Desulfitobacterium metallireducens DSM 15288.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=871968 {ECO:0000313|EMBL:AHF07439.1, ECO:0000313|Proteomes:UP000010847};
RN [1] {ECO:0000313|EMBL:AHF07439.1, ECO:0000313|Proteomes:UP000010847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15288 {ECO:0000313|Proteomes:UP000010847};
RG DOE Joint Genome Institute;
RA Smidt H., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) 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 -!- SIMILARITY: Belongs to the transglycosylase MltG family.
CC {ECO:0000256|HAMAP-Rule:MF_02065}.
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DR EMBL; CP007032; AHF07439.1; -; Genomic_DNA.
DR RefSeq; WP_006716019.1; NZ_CP007032.1.
DR AlphaFoldDB; W0EE08; -.
DR STRING; 871968.DESME_10675; -.
DR KEGG; dmt:DESME_10675; -.
DR eggNOG; COG1559; Bacteria.
DR HOGENOM; CLU_025574_2_2_9; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000010847; Chromosome.
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: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 Reference proteome {ECO:0000313|Proteomes:UP000010847};
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 229
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 341 AA; 38241 MW; 606214C5C98EA0A6 CRC64;
MRRSKRINQL KKGLSSLVIL LALAVVSGGV WWSWADQPYS NQNTSEMIAI TPGMTANQVG
TELERRHLIR SARAFRLLAS QLQADSKLIA GDYLLSADMS PKSMLTKLLS GTEVEAIRLT
IPEGYTTDQI VNLLVQKGIG TKEEYAQVLA TDGFDYSFLQ GIPQDSHRLD GFLFPDTYFL
DKKTTPHTAI DLLLQRFQKE LTAEVQTQLQ GMNLSIRDWV NLSSLVEKEA VQETDRPIIA
GVLMNRLDRK MPLQVDATIQ YILGTPKAKL YNKDLQIESP YNTYLHNGLP PGPIASPGHA
SLNAVLHPEK SDYLFYLAKS DGYHVFAKTF AEHLENQKKY S
//
