ID A0A0V8JK31_9BACI Unreviewed; 366 AA.
AC A0A0V8JK31;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=AS180_13750 {ECO:0000313|EMBL:KSU87306.1};
OS Priestia veravalensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=1414648 {ECO:0000313|EMBL:KSU87306.1, ECO:0000313|Proteomes:UP000053681};
RN [1] {ECO:0000313|EMBL:KSU87306.1, ECO:0000313|Proteomes:UP000053681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGD-V-76 {ECO:0000313|EMBL:KSU87306.1,
RC ECO:0000313|Proteomes:UP000053681};
RA Dastager S.G., Mawlankar R.;
RT "Bacillus caseinolyticus sp nov.";
RL Submitted (NOV-2015) 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}.
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:KSU87306.1}.
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DR EMBL; LNQP01000047; KSU87306.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V8JK31; -.
DR Proteomes; UP000053681; 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: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:UP000053681};
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 245
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 366 AA; 41539 MW; 9179108CF7E9DAF8 CRC64;
MSHQSFFTPK KNKRKKIIIV TIILLAVLIG GGVFYAQSFV QPVDKNSSKK VNITIPQGSS
VRSIGTLLKE EKLIKSESAF RYYIKMSSVS GFQAGTYTFS PSMSLSEMVD MMETGDVSKN
PDVRLAIPEG RQLDEIATII ANRTNYTEEE VMNTLDDPAF IEKMKKKYPD LVTDEVFNKD
IKHPLEGYLY PATYDHYDSN VSLEVILDKM IGKTNGVLAQ YQKEMKSKKY TAHKLLTMAS
LIEEEATEQV DREKIASVFY NRLEEDMPLQ TDPTVLYALG EHRERVYYKD LEVDSPYNTY
REKGLTPGPI ANSGLMSIKA ALEPADTNYL YFLANKDGEV IFTKTLDEHN QEKATHITGP
REEDKK
//
