ID A0A3E2NP29_9SPHI Unreviewed; 345 AA.
AC A0A3E2NP29;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, 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:RFZ82766.1};
GN ORFNames=DYU05_11385 {ECO:0000313|EMBL:RFZ82766.1};
OS Mucilaginibacter terrenus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=2482727 {ECO:0000313|EMBL:RFZ82766.1, ECO:0000313|Proteomes:UP000260823};
RN [1] {ECO:0000313|EMBL:RFZ82766.1, ECO:0000313|Proteomes:UP000260823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZH6 {ECO:0000313|EMBL:RFZ82766.1,
RC ECO:0000313|Proteomes:UP000260823};
RA Huang Y., Zhou Z.;
RT "Mucilaginibacter terrae sp. nov., isolated from manganese diggings.";
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 -!- 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:RFZ82766.1}.
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DR EMBL; QWDE01000002; RFZ82766.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2NP29; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000260823; 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 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:UP000260823};
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 219
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 345 AA; 38639 MW; E0A622729E8582C0 CRC64;
MKGLKFLIVA VILAVIAFSY WVYSSLHTPN AHDKGNQYIQ IQHGSSPGQI LAKLAAEGII
SSQTPLKIYM KVTGTGNEMQ AGEYQFDSPI TPLEVLEKLR KGKLRTVKLI VPEGFTRFDI
AKRIVGEFPQ NKPAGEDSVL DLMNDNSLIK DIAPEAKSLE GYMYPNTYDF PRAVNTEAIL
KKMVEEFRKV WKPEYASRAA KLKLTSHQVI TIASLIETES RLDEERPVVA SVIYNRLKKG
MPLGIDQTAV YIAKMEHRWD GVINRSDLES ASPYNTRKVV GLPPGPISSV SKSSIKAALY
PASTNYIYYV LNVEKNDKSH NFYSSAADFE RGKAAYQAWL AKERK
//