ID A0A0A2MJM3_9FLAO Unreviewed; 346 AA.
AC A0A0A2MJM3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=Q766_09400 {ECO:0000313|EMBL:KGO92842.1};
OS Flavobacterium subsaxonicum WB 4.1-42 = DSM 21790.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1121898 {ECO:0000313|EMBL:KGO92842.1, ECO:0000313|Proteomes:UP000030111};
RN [1] {ECO:0000313|EMBL:KGO92842.1, ECO:0000313|Proteomes:UP000030111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WB 4.1-42 {ECO:0000313|EMBL:KGO92842.1,
RC ECO:0000313|Proteomes:UP000030111};
RA Zeng Z., Chen C.;
RL Submitted (SEP-2013) 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:KGO92842.1}.
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DR EMBL; JRLY01000007; KGO92842.1; -; Genomic_DNA.
DR RefSeq; WP_026993124.1; NZ_KE383911.1.
DR AlphaFoldDB; A0A0A2MJM3; -.
DR STRING; 1121898.GCA_000422725_02804; -.
DR eggNOG; COG1559; Bacteria.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000030111; 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 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:UP000030111};
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 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 215
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 346 AA; 39541 MW; E829C7D26F9793F5 CRC64;
MNLRKIVGIV SLVVVTGGTI YGYMLYKDIF SANTAFNKEE VAVFIPTGAD FEQVKTLVKP
YVEDMDRFIS TAEKKEYPNN VKAGKFIFTN GMNSNDLIIA LRQPRTVDIA FNNQETLQRA
VGRIAQQIEP DSLQLLEAFT DKAFLEENGF NEDNVLSIFI PNTYEFFWNT TATKVRDKLM
KEYRRFWTPE RLAKAEAQGL TPLQVSALAA IVHKETVKND ERPRVAGVYL NRLKKGMKLE
ADPTVIYAIK KQSGDFDQVI KRVFFKDLVI DSPYNMYKYE GLPPGPIAMP DITAIDAVLN
PEQHNYIYFC ASVTNFGYHE FAVTPAQHEV NRQKYVVWVE KMGIKR
//
