ID A0A371PNN7_9BACL Unreviewed; 371 AA.
AC A0A371PNN7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
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 ECO:0000313|EMBL:REK77810.1};
GN ORFNames=DX130_02640 {ECO:0000313|EMBL:REK77810.1};
OS Paenibacillus paeoniae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=2292705 {ECO:0000313|EMBL:REK77810.1, ECO:0000313|Proteomes:UP000261905};
RN [1] {ECO:0000313|EMBL:REK77810.1, ECO:0000313|Proteomes:UP000261905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M4BSY-1 {ECO:0000313|EMBL:REK77810.1,
RC ECO:0000313|Proteomes:UP000261905};
RA Tuo L.;
RT "Paenibacillus sp. M4BSY-1, whole genome shotgun sequence.";
RL Submitted (AUG-2018) 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:REK77810.1}.
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DR EMBL; QUBQ01000001; REK77810.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371PNN7; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000261905; 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; 2.
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:UP000261905};
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 21..48
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 253
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 371 AA; 41620 MW; 3D1E804C35AF9773 CRC64;
MEEKQTQKKK NKRRKNQKPR TWLINLWVFV SLVGIMVLVA GGAAFYLWNN LEPTPKGEMK
QVTITRGMSA NSVADLLEEN GIIKNGFVFS YYLKMKDEGS KFQAGTYELQ PGMDKSAVIA
KLNAGDTIAA ETIRFTIPEG FTVLQIADKL AADGLINKDK FLELAETDRA WGDAETVRGL
PKSDKLHKRL EGYMFPETYE MKKESKEEDI IIRMVTETDR KLSALPEGWQ DAMDASGRTL
HEILTIASLV EREVVVDEER ALVAGVIYNR IATPMRLQID ATVQYALDTP KARLSLSDLE
INSPYNTYKI DGLPPGPIAS PSLASIEAAL FPADTKYLFY VTKKDGTQTH LFAETFKEHQ
KNIALSEKTT Q
//