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Database: UniProt
Entry: A0A371PNN7_9BACL
LinkDB: A0A371PNN7_9BACL
Original site: A0A371PNN7_9BACL 
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
//
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