ID W2U5H5_9DEIN Unreviewed; 337 AA.
AC W2U5H5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=TNMX_01655 {ECO:0000313|EMBL:ETN89460.1};
OS Thermus sp. NMX2.A1.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=570924 {ECO:0000313|EMBL:ETN89460.1, ECO:0000313|Proteomes:UP000018848};
RN [1] {ECO:0000313|EMBL:ETN89460.1, ECO:0000313|Proteomes:UP000018848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NMX2.A1 {ECO:0000313|EMBL:ETN89460.1,
RC ECO:0000313|Proteomes:UP000018848};
RA Litthauer D., van Heerden E., Tlalajoe N.;
RT "The genome sequence of Thermus sp. NMX2.A1.";
RL Submitted (AUG-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 -!- 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:ETN89460.1}.
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DR EMBL; ATNI01000026; ETN89460.1; -; Genomic_DNA.
DR RefSeq; WP_038028785.1; NZ_ATNI01000026.1.
DR AlphaFoldDB; W2U5H5; -.
DR PATRIC; fig|570924.3.peg.302; -.
DR Proteomes; UP000018848; 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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 215
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 337 AA; 37673 MW; D83E56A9EA5EF159 CRC64;
MREGSRRWLW RGVVALFVTF ALLLFYALWL LGPTGKEATV RIPRGATGQE VARILEEAGL
LRSGYLFSAY LRFSGQARRL VPGVYRLKGD GAFRLARALT GGEKPLTVTL TFPEGERAVD
YAKRLSQAGL DGDGFLRIVQ EPGALRPPYV EGRSLEGYLF PATYTFDLLV APEEVVRALL
RRFEAELTPP VRRLLEERRL SVHAWVTLAS IVQAEAGSQK EMPYIAGVFL NRLERGMPLQ
ADPTVAYALG KRLPELSRKA GDFAHDSPYN TYRYAGLPPG PIGNPGREAL LAVLNPVRTD
PKGRPYLYFF HAKGELFLNT SFEAHLEDLR LHRYSSP
//
