ID A0A0L0LM15_9BACT Unreviewed; 327 AA.
AC A0A0L0LM15;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 13-SEP-2023, entry version 21.
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=ABA06_04055 {ECO:0000313|EMBL:KND51452.1};
OS Parcubacteria bacterium C7867-001.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1659195 {ECO:0000313|EMBL:KND51452.1, ECO:0000313|Proteomes:UP000037027};
RN [1] {ECO:0000313|EMBL:KND51452.1, ECO:0000313|Proteomes:UP000037027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7867-001 {ECO:0000313|EMBL:KND51452.1};
RX PubMed=26257709; DOI=10.3389/fmicb.2015.00713;
RA Nelson W.C., Stegen J.C.;
RT "The reduced genomes of Parcubacteria (OD1) contain signatures of a
RT symbiotic lifestyle.";
RL Front. Microbiol. 6:713-713(2015).
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:KND51452.1}.
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DR EMBL; LFCK01000002; KND51452.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0LM15; -.
DR STRING; 1659195.ABA06_04055; -.
DR Proteomes; UP000037027; 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 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 211
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 327 AA; 36704 MW; 54A89F5AE810257A CRC64;
MVLVRHWKKI FGWSVLALVA LALAFLLIYA QLFGPADKTA GTEQFFITPE DTIDTVATRL
KYEHFVRSDI AARIALLEVA TKGLHAGGYT ISASMDTLAI ADILGEPPYL AWIKIPRGYR
KEQIATLLTR ELGWDNAQKE EWLASFKGTS FYEGIFFPTT YLIPTEEAPA RVAERMKQKF
SDTYALLVEK SAKRSTPWPE IVIIASLIDR EAAGPEDVKL ISGVIWNRLA KKMPLGIDAT
LQYIKGTEGS WWPTVHSEDK YLESAFNTYF KSGLPPHPID NPNKVALEAA LNPATTTCLY
YLHDYKGQIH CSNTYKGHVA NVNKYLK
//
