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Database: UniProt
Entry: A0A3E2NP29_9SPHI
LinkDB: A0A3E2NP29_9SPHI
Original site: A0A3E2NP29_9SPHI 
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
//
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