ID A0A255ZUM2_9FLAO Unreviewed; 347 AA.
AC A0A255ZUM2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 12.
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=CHX27_06620 {ECO:0000313|EMBL:OYQ45198.1};
OS Flavobacterium aurantiibacter.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2023067 {ECO:0000313|EMBL:OYQ45198.1, ECO:0000313|Proteomes:UP000216035};
RN [1] {ECO:0000313|EMBL:OYQ45198.1, ECO:0000313|Proteomes:UP000216035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH167 {ECO:0000313|EMBL:OYQ45198.1,
RC ECO:0000313|Proteomes:UP000216035};
RA Cai H.;
RT "Flavobacterium cyanobacteriorum sp. nov., isolated from cyanobacterial
RT aggregates in a eutrophic lake.";
RL Submitted (JUL-2017) 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:OYQ45198.1}.
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DR EMBL; NOXX01000185; OYQ45198.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255ZUM2; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000216035; 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; 3.30.1490.480; 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:UP000216035};
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 216
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 347 AA; 39565 MW; 4C6D422E9F81CB32 CRC64;
MSKKGKILAI VSVVIVAVAI AYGYSLYSKI FSANTKFEET EVYVNIPSES DFEKVKSIMT
AYVQNMETFE MVAGKKKYNT NVKSGRFLLR KGMNNNDIIN SLRQSLPVNI TFNNQERLED
FCARIASQIE ADSLGLMAAI TQEQFLTENN LTTDNVLSIF IPNSYEFFWD TDAMSFRNRM
LKEHRKFWTP ERLEKAKAQN LTPTEVYILA SIVHKETVKT DERPRVAGVY LNRLKKGIKL
EADPTVIYAV KKNSGDFTLQ IKRVLNRDLA TDNPYNTYKF SGLPPGPIAM PDISAIDAVL
NPEKHDYIYF CASVSRFGYH EFAVTAAQHE VNRQKYVAWI NAQGIKR
//
